[ { "id": "aceip0001", "seq": "AA", "length": "2", "detail": "Milk (bovine) | Carp | Cereals (Wheat) | Pork | Chicken", "source": "Milk | Fish | Cereal | Porcine | Chicken", "ic50": "51.4 μM", "reference": "Three-dimensional holograph vector of atomic interaction field (3D-HoVAIF): a novel rotation-translation invariant 3D structure descriptor and its applications to peptides.; QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.; Peptides with angiotensin I converting enzyme (ACE) inhibitory activity generated from porcine skeletal muscle proteins by the action of meat-borne Lactobacillus.", "doi": "10.1002\/psc.892; 10.1007\/s00894-010-0862-x; 10.1016\/j.jprot.2013.06.023", "pubmedid": "17654623 20941517 23806758", "mw": "160.17", "pi": "5.57", "charge_ph7": "-0.2", "gravy": "1.8", "instability": "5.0", "hydrophobic": "1.0", "boman": "-1.81", "helix": "1.0", "turn_pct": "0.0", "sheet": "0.0" }, { "id": "aceip0002", "seq": "AAP", "length": "3", "detail": "Milk (bovine) | Amaranth | Chicken", "source": "Milk | Plants | Chicken", "ic50": "0 μM", "reference": "Bioactive peptides in amaranth (Amaranthus hypochondriacus) seed.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1021\/jf072911z; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "18211015 23871047", "mw": "257.29", "pi": "5.57", "charge_ph7": "-0.2", "gravy": "0.6667", "instability": "70.87", "hydrophobic": "1.0", "boman": "-1.2067", "helix": "0.6667", "turn_pct": "0.3333", "sheet": "0.0" }, { "id": "aceip0003", "seq": "ACHP", "length": "4", "detail": "Milk (bovine)", "source": "Milk", "ic50": "360.7 μM", "reference": "What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1016\/j.foodchem.2013.05.140", "pubmedid": "23871047", "mw": "426.49", "pi": "6.78", "charge_ph7": "-0.13", "gravy": "-0.125", "instability": "191.65", "hydrophobic": "0.5", "boman": "-0.525", "helix": "0.25", "turn_pct": "0.25", "sheet": "0.0" }, { "id": "aceip0004", "seq": "AD", "length": "2", "detail": "ND", "source": "ND", "ic50": null, "reference": "Quantitative structure-activity relationship study of bitter di- and tri-peptides including relationship with angiotensin I-converting enzyme inhibitory activity.", "doi": "10.1002\/psc.800", "pubmedid": "17117396", "mw": "204.18", "pi": "4.3", "charge_ph7": "-1.2", "gravy": "-0.85", "instability": "-37.45", "hydrophobic": "0.5", "boman": "-0.065", "helix": "0.5", "turn_pct": "0.5", "sheet": "0.0" }, { "id": "aceip0005", "seq": "ADA", "length": "3", "detail": "ND", "source": "ND", "ic50": null, "reference": "Quantitative structure-activity relationship study of bitter di- and tri-peptides including relationship with angiotensin I-converting enzyme inhibitory activity.; QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1002\/psc.800; 10.1007\/s00894-010-0862-x; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "17117396 20941517 23871047", "mw": "275.26", "pi": "4.05", "charge_ph7": "-1.2", "gravy": "0.0333", "instability": "-21.63", "hydrophobic": "0.6667", "boman": "-0.6467", "helix": "0.6667", "turn_pct": "0.3333", "sheet": "0.0" }, { "id": "aceip0006", "seq": "AEL", "length": "3", "detail": "Milk", "source": "Milk", "ic50": "57.1 μM", "reference": "Review on the angiotensin-I-converting enzyme (ACE) inhibitor peptides from marine proteins.; Vegetable foods: a cheap source of proteins and peptides with antihypertensive, antioxidant, and other less occurrence bioactivities.", "doi": "10.1007\/s12010-012-0024-y; 10.1016\/j.talanta.2012.12.041", "pubmedid": "23271625 23598136", "mw": "331.36", "pi": "4.05", "charge_ph7": "-1.2", "gravy": "0.7", "instability": "6.67", "hydrophobic": "0.6667", "boman": "-1.6967", "helix": "1.0", "turn_pct": "0.0", "sheet": "0.3333" }, { "id": "aceip0007", "seq": "AF", "length": "2", "detail": "Soybean", "source": "Legume", "ic50": "<20 mM", "reference": "Binding of peptide substrates and inhibitors of angiotensin-converting enzyme. Importance of the COOH-terminal dipeptide sequence.; Isolation from alpha-zein of thermolysin peptides with angiotensin I-converting enzyme inhibitory activity.; Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Quantitative structure-activity relationship study of bitter di- and tri-peptides including relationship with angiotensin I-converting enzyme inhibitory activity.; Three-dimensional holograph vector of atomic interaction field (3D-HoVAIF): a novel rotation-translation invariant 3D structure descriptor and its applications to peptides.; Model of the exofacial substrate-binding site and helical folding of the human Glut1 glucose transporter based on scanning mutagenesis.; Antihypertensive effect of peptide-enriched soy sauce-like seasoning and identification of its angiotensin I-converting enzyme inhibitory substances.; QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.; Vegetable foods: a cheap source of proteins and peptides with antihypertensive, antioxidant, and other less occurrence bioactivities.; Peptides with angiotensin I converting enzyme (ACE) inhibitory activity generated from porcine skeletal muscle proteins by the action of meat-borne Lactobacillus.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1271\/bbb.60.661; 10.1021\/jf051263l; 10.1002\/psc.800; 10.1002\/psc.892; 10.1021\/bi900521n; 10.1021\/jf903261h; 10.1007\/s00894-010-0862-x; 10.1016\/j.talanta.2012.12.041; 10.1016\/j.jprot.2013.06.023; 10.1016\/j.foodchem.2013.05.140; 10.1080\/10408398.2012.664829", "pubmedid": "6243277 8829536 16448176 17117396 17654623 19449892 19994857 20941517 23598136 23806758 23871047 24915368", "mw": "236.27", "pi": "5.57", "charge_ph7": "-0.2", "gravy": "2.3", "instability": "5.0", "hydrophobic": "1.0", "boman": "-2.395", "helix": "0.5", "turn_pct": "0.0", "sheet": "0.5" }, { "id": "aceip0008", "seq": "AFKAWAVAR", "length": "9", "detail": "Algae (Spirulina platensis) | Algae (Chlorella vulgaris)", "source": "Bacteria", "ic50": "1.7 μM", "reference": "QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1007\/s00894-010-0862-x; 10.1016\/j.foodchem.2012.09.092", "pubmedid": "20941517 23194537", "mw": "1019.2", "pi": "11.0", "charge_ph7": "1.79", "gravy": "0.5444", "instability": "-24.51", "hydrophobic": "0.7778", "boman": "-1.3656", "helix": "0.5556", "turn_pct": "0.0", "sheet": "0.3333" }, { "id": "aceip0009", "seq": "AFL", "length": "3", "detail": "Milk (bovine) | Carp | Cereals (Maize) | Cereals (Soybean+Wheat) | Soybean | pea | Soybean (Fermented) | Soybean Sauce | Pork | Chicken", "source": "Milk | Fish | Cereal | Legume | Porcine | Chicken", "ic50": "<20 mM", "reference": "Analysis of novel angiotensin-I-converting enzyme inhibitory peptides from protease-hydrolyzed marine shrimp Acetes chinensis.; Review on the angiotensin-I-converting enzyme (ACE) inhibitor peptides from marine proteins.; Vegetable foods: a cheap source of proteins and peptides with antihypertensive, antioxidant, and other less occurrence bioactivities.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1002\/psc.789; 10.1007\/s12010-012-0024-y; 10.1016\/j.talanta.2012.12.041; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "16981241 23271625 23598136 23871047", "mw": "349.42", "pi": "5.57", "charge_ph7": "-0.2", "gravy": "2.8", "instability": "6.67", "hydrophobic": "1.0", "boman": "-3.2367", "helix": "0.6667", "turn_pct": "0.0", "sheet": "0.6667" }, { "id": "aceip0010", "seq": "AG", "length": "2", "detail": "ND", "source": "ND", "ic50": "<20 mM", "reference": "Binding of peptide substrates and inhibitors of angiotensin-converting enzyme. Importance of the COOH-terminal dipeptide sequence.; Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Three-dimensional holograph vector of atomic interaction field (3D-HoVAIF): a novel rotation-translation invariant 3D structure descriptor and its applications to peptides.; QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.; Peptides with angiotensin I converting enzyme (ACE) inhibitory activity generated from porcine skeletal muscle proteins by the action of meat-borne Lactobacillus.", "doi": "10.1021\/jf051263l; 10.1002\/psc.892; 10.1007\/s00894-010-0862-x; 10.1016\/j.jprot.2013.06.023", "pubmedid": "6243277 16448176 17654623 20941517 23806758", "mw": "146.14", "pi": "5.57", "charge_ph7": "-0.2", "gravy": "0.7", "instability": "5.0", "hydrophobic": "0.5", "boman": "-1.375", "helix": "0.5", "turn_pct": "0.5", "sheet": "0.0" }, { "id": "aceip0011", "seq": "AGLP", "length": "4", "detail": "Algae (Chlorella vulgaris) | Shrimp", "source": "Bacteria | Shrimp", "ic50": "382->1000 μM", "reference": "Angiotensin I-converting enzyme inhibitory peptides generated from in vitro gastrointestinal digestion of pork meat.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1021\/jf904204n; 10.1080\/10408398.2012.664829", "pubmedid": "20151679 24915368", "mw": "356.42", "pi": "5.57", "charge_ph7": "-0.2", "gravy": "0.9", "instability": "55.65", "hydrophobic": "0.75", "boman": "-1.9175", "helix": "0.5", "turn_pct": "0.5", "sheet": "0.25" }, { "id": "aceip0012", "seq": "AGP", "length": "3", "detail": "Milk", "source": "Milk", "ic50": "<20 mM", "reference": "Angiotensin I-converting enzyme inhibitory activity and insulin secretion stimulative activity of fermented fish sauce.; Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1016\/S1389-1723(03)70138-8; 10.1021\/jf051263l; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "16233562 16448176 23871047", "mw": "243.26", "pi": "5.57", "charge_ph7": "-0.2", "gravy": "-0.0667", "instability": "6.67", "hydrophobic": "0.6667", "boman": "-0.9167", "helix": "0.3333", "turn_pct": "0.6667", "sheet": "0.0" }, { "id": "aceip0013", "seq": "AGS", "length": "3", "detail": "Soybean", "source": "Legume", "ic50": "527.9 μM", "reference": "Analysis of novel angiotensin I-converting enzyme inhibitory peptides from enzymatic hydrolysates of cuttlefish (Sepia officinalis) muscle proteins.; Review on the angiotensin-I-converting enzyme (ACE) inhibitor peptides from marine proteins.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1021\/jf904300q; 10.1007\/s12010-012-0024-y; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "20180574 23271625 23871047", "mw": "233.22", "pi": "5.57", "charge_ph7": "-0.2", "gravy": "0.2", "instability": "6.67", "hydrophobic": "0.3333", "boman": "-0.6367", "helix": "0.3333", "turn_pct": "0.6667", "sheet": "0.0" }, { "id": "aceip0014", "seq": "AGSP", "length": "4", "detail": "Soybean", "source": "Legume", "ic50": "11.6 μM\/L", "reference": "Analysis of novel angiotensin I-converting enzyme inhibitory peptides from enzymatic hydrolysates of cuttlefish (Sepia officinalis) muscle proteins.; Review on the angiotensin-I-converting enzyme (ACE) inhibitor peptides from marine proteins.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1021\/jf904300q; 10.1007\/s12010-012-0024-y; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "20180574 23271625 23871047", "mw": "330.34", "pi": "5.57", "charge_ph7": "-0.2", "gravy": "-0.25", "instability": "117.35", "hydrophobic": "0.5", "boman": "-0.4775", "helix": "0.25", "turn_pct": "0.75", "sheet": "0.0" }, { "id": "aceip0015", "seq": "AGSS", "length": "4", "detail": "Milk (bovine) | Carp | Cereals (Wheat) | Pork | Chicken", "source": "Milk | Fish | Cereal | Porcine | Chicken", "ic50": "672.1 μM", "reference": "Analysis of novel angiotensin I-converting enzyme inhibitory peptides from enzymatic hydrolysates of cuttlefish (Sepia officinalis) muscle proteins.; Review on the angiotensin-I-converting enzyme (ACE) inhibitor peptides from marine proteins.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1021\/jf904300q; 10.1007\/s12010-012-0024-y; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "20180574 23271625 23871047", "mw": "320.3", "pi": "5.57", "charge_ph7": "-0.2", "gravy": "-0.05", "instability": "55.65", "hydrophobic": "0.25", "boman": "-0.2675", "helix": "0.25", "turn_pct": "0.75", "sheet": "0.0" }, { "id": "aceip0016", "seq": "AH", "length": "2", "detail": "Egg (Ovalbumin)", "source": "Egg", "ic50": "0 0", "reference": "Application of at-line two-dimensional liquid chromatography-mass spectrometry for identification of small hydrophilic angiotensin I-inhibiting peptides in milk hydrolysates.", "doi": "10.1007\/s00216-008-1990-3", "pubmedid": "18392815", "mw": "226.23", "pi": "6.79", "charge_ph7": "-0.12", "gravy": "-0.7", "instability": "-37.45", "hydrophobic": "0.5", "boman": "-0.41", "helix": "0.5", "turn_pct": "0.0", "sheet": "0.0" }, { "id": "aceip0017", "seq": "AHEPVK", "length": "6", "detail": "Pork", "source": "Porcine", "ic50": "62.8 μM", "reference": "Novel angiotensin I-converting enzyme inhibitory peptides derived from an edible mushroom, Pleurotus cystidiosus O.K. Miller identified by LC-MS\/MS.; Novel angiotensin I-converting enzyme inhibitory peptides derived from edible mushroom Agaricus bisporus (J.E. Lange) Imbach identified by LC-MS\/MS.", "doi": "10.1186\/1472-6882-13-313; 10.1016\/j.foodchem.2013.10.053", "pubmedid": "24215325 24262574", "mw": "679.76", "pi": "6.79", "charge_ph7": "-0.12", "gravy": "-1.0333", "instability": "53.58", "hydrophobic": "0.5", "boman": "-0.2733", "helix": "0.5", "turn_pct": "0.1667", "sheet": "0.1667" }, { "id": "aceip0018", "seq": "AHHP", "length": "4", "detail": "Bonito", "source": "Fish", "ic50": "847.6 μM", "reference": "What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1016\/j.foodchem.2013.05.140", "pubmedid": "23871047", "mw": "460.49", "pi": "6.96", "charge_ph7": "-0.03", "gravy": "-1.55", "instability": "-20.93", "hydrophobic": "0.5", "boman": "0.0425", "helix": "0.25", "turn_pct": "0.25", "sheet": "0.0" }, { "id": "aceip0019", "seq": "AHSY", "length": "4", "detail": "Fish (Cuttlefish)", "source": "Fish", "ic50": "11.6 μM\/L", "reference": "Analysis of novel angiotensin I-converting enzyme inhibitory peptides from enzymatic hydrolysates of cuttlefish (Sepia officinalis) muscle proteins.; Review on the angiotensin-I-converting enzyme (ACE) inhibitor peptides from marine proteins.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1021\/jf904300q; 10.1007\/s12010-012-0024-y; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "20180574 23271625 23871047", "mw": "476.48", "pi": "6.78", "charge_ph7": "-0.12", "gravy": "-0.875", "instability": "-13.73", "hydrophobic": "0.25", "boman": "0.04", "helix": "0.25", "turn_pct": "0.25", "sheet": "0.25" }, { "id": "aceip0020", "seq": "AI", "length": "2", "detail": "Fish (Cuttlefish)", "source": "Fish", "ic50": "3.41 μM", "reference": "Antihypertensive effect of peptide-enriched soy sauce-like seasoning and identification of its angiotensin I-converting enzyme inhibitory substances.; Vegetable foods: a cheap source of proteins and peptides with antihypertensive, antioxidant, and other less occurrence bioactivities.; Peptides with angiotensin I converting enzyme (ACE) inhibitory activity generated from porcine skeletal muscle proteins by the action of meat-borne Lactobacillus.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1021\/jf903261h; 10.1016\/j.talanta.2012.12.041; 10.1016\/j.jprot.2013.06.023; 10.1080\/10408398.2012.664829", "pubmedid": "19994857 23598136 23806758 24915368", "mw": "202.25", "pi": "5.57", "charge_ph7": "-0.2", "gravy": "3.15", "instability": "5.0", "hydrophobic": "1.0", "boman": "-3.365", "helix": "0.5", "turn_pct": "0.0", "sheet": "0.5" }, { "id": "aceip0021", "seq": "AIP", "length": "3", "detail": "Fish (Cuttlefish)", "source": "Fish", "ic50": "350 μM", "reference": "Inhibition of angiotensin-converting enzyme by synthetic peptide fragments of human kappa-casein.; Bioactive peptides in amaranth (Amaranthus hypochondriacus) seed.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1021\/jf072911z; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "1368540 18211015 23871047", "mw": "299.37", "pi": "5.57", "charge_ph7": "-0.2", "gravy": "1.5667", "instability": "-2.93", "hydrophobic": "1.0", "boman": "-2.2433", "helix": "0.3333", "turn_pct": "0.3333", "sheet": "0.3333" }, { "id": "aceip0022", "seq": "AIPP", "length": "4", "detail": "Milk", "source": "Milk", "ic50": "900 μM", "reference": "Inhibition of angiotensin-converting enzyme by synthetic peptide fragments of human kappa-casein.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1016\/j.foodchem.2013.05.140", "pubmedid": "1368540 23871047", "mw": "396.48", "pi": "5.57", "charge_ph7": "-0.2", "gravy": "0.775", "instability": "48.45", "hydrophobic": "1.0", "boman": "-1.6825", "helix": "0.25", "turn_pct": "0.5", "sheet": "0.25" }, { "id": "aceip0023", "seq": "AITAKL", "length": "6", "detail": "Milk (bovine) | Milk | Cereals | Chicken | Sweet-potato", "source": "Milk | Cereal | Chicken | Potato", "ic50": null, "reference": "Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1080\/10408398.2012.664829", "pubmedid": "24915368", "mw": "615.76", "pi": "8.8", "charge_ph7": "0.79", "gravy": "1.2167", "instability": "-5.82", "hydrophobic": "0.6667", "boman": "-1.9367", "helix": "0.6667", "turn_pct": "0.0", "sheet": "0.5" }, { "id": "aceip0024", "seq": "AIYK", "length": "4", "detail": "Fungi (Agaricus bisporus) | Fungi (P.Cystidiosus)", "source": "Fungi", "ic50": "213 μM", "reference": "Identification of an antihypertensive peptide from peptic digest of wakame (Undaria pinnatifida).; Review on the angiotensin-I-converting enzyme (ACE) inhibitor peptides from marine proteins.; Vegetable foods: a cheap source of proteins and peptides with antihypertensive, antioxidant, and other less occurrence bioactivities.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1016\/s0955-2863(00)00110-8; 10.1007\/s12010-012-0024-y; 10.1016\/j.talanta.2012.12.041; 10.1016\/j.foodchem.2013.05.140; 10.1080\/10408398.2012.664829", "pubmedid": "11091100 23271625 23598136 23871047 24915368", "mw": "493.6", "pi": "8.63", "charge_ph7": "0.79", "gravy": "0.275", "instability": "7.5", "hydrophobic": "0.5", "boman": "-1.2525", "helix": "0.5", "turn_pct": "0.0", "sheet": "0.5" }, { "id": "aceip0025", "seq": "AKK", "length": "3", "detail": "Milk (bovine)", "source": "Milk", "ic50": "<20 mM", "reference": "Angiotensin I-converting enzyme inhibitory peptides in an alkaline protease hydrolyzate derived from sardine muscle.; Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Inhibition strength of short peptides derived from an ACE inhibitory peptide.; Review on the angiotensin-I-converting enzyme (ACE) inhibitor peptides from marine proteins.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1271\/bbb.58.2244; 10.1021\/jf051263l; 10.1021\/jf202902r; 10.1007\/s12010-012-0024-y; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "7765718 16448176 21923188 23271625 23871047", "mw": "345.44", "pi": "10.0", "charge_ph7": "1.79", "gravy": "-2.0", "instability": "6.67", "hydrophobic": "0.3333", "boman": "0.45", "helix": "1.0", "turn_pct": "0.0", "sheet": "0.0" }, { "id": "aceip0026", "seq": "AKLEK", "length": "5", "detail": "Loach", "source": "Fish", "ic50": "227.46 μM", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "23194537", "mw": "587.71", "pi": "8.64", "charge_ph7": "0.8", "gravy": "-1.14", "instability": "-8.98", "hydrophobic": "0.4", "boman": "-0.386", "helix": "1.0", "turn_pct": "0.0", "sheet": "0.2" }, { "id": "aceip0027", "seq": "AKYCY", "length": "5", "detail": "Fish (Cuttlefish)", "source": "Fish", "ic50": "19.95 μM", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "23194537", "mw": "646.75", "pi": "8.22", "charge_ph7": "0.78", "gravy": "-0.44", "instability": "8.0", "hydrophobic": "0.2", "boman": "-0.246", "helix": "0.4", "turn_pct": "0.0", "sheet": "0.4" }, { "id": "aceip0028", "seq": "AKYSY", "length": "5", "detail": "Cereals (Soybean+Wheat) | Soybean (Fermented) | Soybean Sauce | Pork", "source": "Cereal | Legume | Porcine", "ic50": "1.5 μM", "reference": "Antihypertensive peptides from food proteins: a review.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1039\/c2fo10192k; 10.1016\/j.foodchem.2012.09.092", "pubmedid": "22249830 23194537", "mw": "630.69", "pi": "8.54", "charge_ph7": "0.79", "gravy": "-1.1", "instability": "8.0", "hydrophobic": "0.2", "boman": "0.178", "helix": "0.4", "turn_pct": "0.2", "sheet": "0.4" }, { "id": "aceip0029", "seq": "AL", "length": "2", "detail": "Milk (bovine) | Milk | Milk (human) | Amaranth", "source": "Milk | Plants", "ic50": null, "reference": "Three-dimensional holograph vector of atomic interaction field (3D-HoVAIF): a novel rotation-translation invariant 3D structure descriptor and its applications to peptides.", "doi": "10.1002\/psc.892", "pubmedid": "17654623", "mw": "202.25", "pi": "5.57", "charge_ph7": "-0.2", "gravy": "2.8", "instability": "5.0", "hydrophobic": "1.0", "boman": "-3.365", "helix": "1.0", "turn_pct": "0.0", "sheet": "0.5" }, { "id": "aceip0030", "seq": "ALAFQ", "length": "5", "detail": "Milk (human)", "source": "Milk", "ic50": "165.96 μM", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "23194537", "mw": "548.63", "pi": "5.57", "charge_ph7": "-0.2", "gravy": "1.34", "instability": "8.0", "hydrophobic": "0.8", "boman": "-2.032", "helix": "0.6", "turn_pct": "0.0", "sheet": "0.4" }, { "id": "aceip0031", "seq": "ALEP", "length": "4", "detail": "Chicken", "source": "Chicken", "ic50": "6320 μM", "reference": "ACE inhibitory tetrapeptides from Amaranthus hypochondriacus 11S globulin.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1016\/j.phytochem.2009.04.006; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "19443002 23871047", "mw": "428.48", "pi": "4.05", "charge_ph7": "-1.2", "gravy": "0.125", "instability": "55.65", "hydrophobic": "0.75", "boman": "-1.2725", "helix": "0.75", "turn_pct": "0.25", "sheet": "0.25" }, { "id": "aceip0032", "seq": "ALKAWSVAR", "length": "9", "detail": "Wakame", "source": "Plants", "ic50": "3 μM", "reference": "Lactokinins: whey protein-derived ACE inhibitory peptides.; Temporal gene expression and probiotic attributes of Lactobacillus acidophilus during growth in milk.; QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.; Bioactive peptides derived from milk proteins and their health beneficial potentials: an update.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1002\/(SICI)1521-3803(19990601)43:3<165::AID-FOOD165>3.0.CO;2-2; 10.3168\/jds.2008-1457; 10.1007\/s00894-010-0862-x; 10.1039\/c0fo00016g; 10.1016\/j.foodchem.2012.09.092", "pubmedid": "10399349 19233780 20941517 21773582 23194537", "mw": "1001.18", "pi": "11.0", "charge_ph7": "1.79", "gravy": "0.3667", "instability": "-0.54", "hydrophobic": "0.6667", "boman": "-1.2867", "helix": "0.5556", "turn_pct": "0.1111", "sheet": "0.3333" }, { "id": "aceip0033", "seq": "ALNEINQFY", "length": "9", "detail": "Meat", "source": "Meat", "ic50": "219 μM", "reference": "Angiotensin converting enzyme inhibitory peptides derived from food proteins: biochemistry, bioactivity and production.; QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.2174\/138161207780363068; 10.1007\/s00894-010-0862-x; 10.1016\/j.foodchem.2012.09.092", "pubmedid": "17430180 20941517 23194537", "mw": "1111.2", "pi": "4.05", "charge_ph7": "-1.2", "gravy": "-0.2667", "instability": "49.76", "hydrophobic": "0.4444", "boman": "-0.9167", "helix": "0.3333", "turn_pct": "0.2222", "sheet": "0.4444" }, { "id": "aceip0034", "seq": "ALNEINQFYQK", "length": "11", "detail": "Milk", "source": "Milk", "ic50": "264 μM", "reference": "Angiotensin converting enzyme inhibitory peptides derived from food proteins: biochemistry, bioactivity and production.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.2174\/138161207780363068; 10.1016\/j.foodchem.2012.09.092", "pubmedid": "17430180 23194537", "mw": "1367.51", "pi": "6.05", "charge_ph7": "-0.2", "gravy": "-0.8909", "instability": "42.53", "hydrophobic": "0.3636", "boman": "-0.4827", "helix": "0.3636", "turn_pct": "0.1818", "sheet": "0.3636" }, { "id": "aceip0035", "seq": "ALP", "length": "3", "detail": "Milk (bovine) | Synthesized | Sardine | Chicken", "source": "Milk | Synthesized | Fish | Chicken", "ic50": "<20 mM", "reference": "Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.", "doi": "10.1021\/jf051263l", "pubmedid": "16448176", "mw": "299.37", "pi": "5.57", "charge_ph7": "-0.2", "gravy": "1.3333", "instability": "70.87", "hydrophobic": "1.0", "boman": "-2.2433", "helix": "0.6667", "turn_pct": "0.3333", "sheet": "0.3333" }, { "id": "aceip0036", "seq": "ALPHA", "length": "5", "detail": "ND", "source": "ND", "ic50": "10 μM", "reference": "Peptide inhibitors for angiotensin I-converting enzyme from thermolysin digest of dried bonito.; Isolation and characterization of angiotensin I-converting enzyme inhibitory peptides derived from bonito bowels.; Review on the angiotensin-I-converting enzyme (ACE) inhibitor peptides from marine proteins.", "doi": "10.1271\/bbb.56.1541; 10.1271\/bbb.57.1743; 10.1007\/s12010-012-0024-y", "pubmedid": "1369054 7764272 23271625", "mw": "507.58", "pi": "6.79", "charge_ph7": "-0.12", "gravy": "0.52", "instability": "46.52", "hydrophobic": "0.8", "boman": "-1.51", "helix": "0.6", "turn_pct": "0.2", "sheet": "0.2" }, { "id": "aceip0037", "seq": "ALPM", "length": "4", "detail": "Milk", "source": "Milk", "ic50": "928 μM", "reference": "Structural analysis of a new anti-hypertensive peptide (beta-lactosin B) isolated from a commercial whey product.; Antihypertensive peptides: production, bioavailability and incorporation into foods.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.3168\/jds.S0022-0302(04)70013-2; 10.1016\/j.cis.2010.11.001; 10.1016\/j.foodchem.2013.05.140; 10.1080\/10408398.2012.664829", "pubmedid": "15328207 21185549 23871047 24915368", "mw": "430.56", "pi": "5.57", "charge_ph7": "-0.2", "gravy": "1.475", "instability": "36.8", "hydrophobic": "1.0", "boman": "-2.27", "helix": "0.75", "turn_pct": "0.25", "sheet": "0.25" }, { "id": "aceip0038", "seq": "ALPMH", "length": "5", "detail": "Milk", "source": "Milk", "ic50": "521 μM", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "23194537", "mw": "567.7", "pi": "6.79", "charge_ph7": "-0.12", "gravy": "0.54", "instability": "146.0", "hydrophobic": "0.8", "boman": "-1.618", "helix": "0.6", "turn_pct": "0.2", "sheet": "0.2" }, { "id": "aceip0039", "seq": "ALPMHIR", "length": "7", "detail": "Milk", "source": "Milk", "ic50": "42.6 μM", "reference": "Identification of a novel angiotensin-I-converting enzyme inhibitory peptide corresponding to a tryptic fragment of bovine beta-lactoglobulin.; Milk peptides and blood pressure.; Quality and acceptability of a set-type yogurt made from camel milk.; Bioactive peptides derived from milk proteins and their health beneficial potentials: an update.; The potential role of milk-derived peptides in cardiovascular disease.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/s0014-5793(96)01503-7; 10.1093\/jn\/137.3.825S; 10.3168\/jds.2008-1408; 10.1039\/c0fo00016g; 10.1039\/c1fo10017c; 10.1016\/j.foodchem.2012.09.092", "pubmedid": "9037174 17311982 19233778 21773582 21779574 23194537", "mw": "837.04", "pi": "9.8", "charge_ph7": "0.88", "gravy": "0.3857", "instability": "169.91", "hydrophobic": "0.7143", "boman": "-1.47", "helix": "0.4286", "turn_pct": "0.1429", "sheet": "0.2857" }, { "id": "aceip0040", "seq": "ALPP", "length": "4", "detail": "ND", "source": "ND", "ic50": "1mM", "reference": "Bioactive peptides in amaranth (Amaranthus hypochondriacus) seed.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1016\/j.foodchem.2013.05.140", "pubmedid": "18211015 23871047", "mw": "396.48", "pi": "5.57", "charge_ph7": "-0.2", "gravy": "0.6", "instability": "103.8", "hydrophobic": "1.0", "boman": "-1.6825", "helix": "0.5", "turn_pct": "0.5", "sheet": "0.25" }, { "id": "aceip0041", "seq": "AMKPW", "length": "5", "detail": "Porphyra yezoensis", "source": "Plants", "ic50": "580 μM", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "23194537", "mw": "631.79", "pi": "8.8", "charge_ph7": "0.79", "gravy": "-0.54", "instability": "-12.84", "hydrophobic": "0.8", "boman": "-0.982", "helix": "0.6", "turn_pct": "0.2", "sheet": "0.2" }, { "id": "aceip0042", "seq": "AMKPWIQPK", "length": "9", "detail": "ND", "source": "ND", "ic50": "600 μM", "reference": "QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.", "doi": "10.1007\/s00894-010-0862-x", "pubmedid": "20941517", "mw": "1098.36", "pi": "10.0", "charge_ph7": "1.79", "gravy": "-0.8", "instability": "18.71", "hydrophobic": "0.6667", "boman": "-0.7656", "helix": "0.4444", "turn_pct": "0.2222", "sheet": "0.2222" }, { "id": "aceip0043", "seq": "AMPKPW", "length": "6", "detail": "Proteinase of L. helveticus CP790", "source": "Bacteria", "ic50": "580 μM", "reference": "Antihypertensive peptides: production, bioavailability and incorporation into foods.; Antihypertensive peptides from food proteins: a review.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.cis.2010.11.001; 10.1039\/c2fo10192k; 10.1016\/j.foodchem.2012.09.092", "pubmedid": "21185549 22249830 23194537", "mw": "728.9", "pi": "8.8", "charge_ph7": "0.79", "gravy": "-0.7167", "instability": "64.2", "hydrophobic": "0.8333", "boman": "-0.8183", "helix": "0.5", "turn_pct": "0.3333", "sheet": "0.1667" }, { "id": "aceip0044", "seq": "AMQS", "length": "4", "detail": "Seed (Brassica napus)", "source": "Plants", "ic50": ">1 mM", "reference": "New antihypertensive peptides isolated from rapeseed.", "doi": "10.1016\/s0196-9781(03)00174-8", "pubmedid": "12948830", "mw": "435.5", "pi": "5.57", "charge_ph7": "-0.2", "gravy": "-0.15", "instability": "98.5", "hydrophobic": "0.5", "boman": "-0.49", "helix": "0.5", "turn_pct": "0.25", "sheet": "0.0" }, { "id": "aceip0045", "seq": "ANPAVVRP", "length": "8", "detail": "Milk (bovine) | Milk (whey) | Bovine | Bovine blood", "source": "Milk | Bovine", "ic50": "25 μM", "reference": "Inhibition of angiotensin-converting enzyme by synthetic peptide fragments of human kappa-casein.", "doi": "10.1271\/bbb1961.54.835", "pubmedid": "1368540", "mw": "822.95", "pi": "9.8", "charge_ph7": "0.8", "gravy": "0.1", "instability": "53.3", "hydrophobic": "0.75", "boman": "-0.92", "helix": "0.25", "turn_pct": "0.375", "sheet": "0.25" }, { "id": "aceip0046", "seq": "ANSSIL", "length": "6", "detail": "Leg bone (chicken)", "source": "Birds", "ic50": null, "reference": "Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1080\/10408398.2012.664829", "pubmedid": "24915368", "mw": "603.67", "pi": "5.57", "charge_ph7": "-0.2", "gravy": "0.8333", "instability": "72.53", "hydrophobic": "0.5", "boman": "-1.3917", "helix": "0.3333", "turn_pct": "0.5", "sheet": "0.3333" }, { "id": "aceip0047", "seq": "AP", "length": "2", "detail": " Synthesized(1) | Anchovy, sardine, bonito(3) | Skin(Salmo salar)(6)", "source": "Synthesized | Fish", "ic50": "300 mM", "reference": "Binding of peptide substrates and inhibitors of angiotensin-converting enzyme. Importance of the COOH-terminal dipeptide sequence.;Angiotensin I-converting enzyme inhibitory activity and insulin secretion stimulative activity of fermented fish sauce.; Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Three-dimensional holograph vector of atomic interaction field (3D-HoVAIF): a novel rotation-translation invariant 3D structure descriptor and its applications to peptides.; Review on the angiotensin-I-converting enzyme (ACE) inhibitor peptides from marine proteins.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1002\/(SICI)1521-3803(19990601)43:3<159::AID-FOOD159>3.0.CO;2-R; 10.1021\/jf051263l; 10.1002\/psc.892; 10.1007\/s12010-012-0024-y; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "6243277 16233562 16448176 17654623 23271625 23871047", "mw": "186.21", "pi": "5.57", "charge_ph7": "-0.2", "gravy": "0.1", "instability": "101.3", "hydrophobic": "1.0", "boman": "-0.905", "helix": "0.5", "turn_pct": "0.5", "sheet": "0.0" }, { "id": "aceip0048", "seq": "APGAGVY", "length": "7", "detail": "Synthesized", "source": "Synthesized", "ic50": "5.1 μM", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "23194537", "mw": "633.69", "pi": "5.57", "charge_ph7": "-0.21", "gravy": "0.5857", "instability": "13.19", "hydrophobic": "0.5714", "boman": "-1.3429", "helix": "0.2857", "turn_pct": "0.4286", "sheet": "0.2857" }, { "id": "aceip0049", "seq": "APSAK", "length": "5", "detail": "Agaricus bisporus", "source": "Fungi", "ic50": "326 μM", "reference": "Novel angiotensin I-converting enzyme inhibitory peptides derived from edible mushroom Agaricus bisporus (J.E. Lange) Imbach identified by LC-MS\/MS.", "doi": "10.1016\/j.foodchem.2013.10.053", "pubmedid": "24262574", "mw": "472.54", "pi": "8.8", "charge_ph7": "0.79", "gravy": "-0.54", "instability": "85.04", "hydrophobic": "0.6", "boman": "-0.24", "helix": "0.6", "turn_pct": "0.4", "sheet": "0.0" }, { "id": "aceip0050", "seq": "APVPP", "length": "5", "detail": "ND", "source": "ND", "ic50": "630.96 μM", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "23194537", "mw": "479.57", "pi": "5.57", "charge_ph7": "-0.2", "gravy": "0.24", "instability": "162.08", "hydrophobic": "1.0", "boman": "-1.17", "helix": "0.2", "turn_pct": "0.6", "sheet": "0.2" }, { "id": "aceip0051", "seq": "AQK", "length": "3", "detail": "ND", "source": "ND", "ic50": "1820 mM", "reference": "Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.", "doi": "10.1021\/jf051263l", "pubmedid": "16448176", "mw": "345.39", "pi": "8.8", "charge_ph7": "0.79", "gravy": "-1.8667", "instability": "6.67", "hydrophobic": "0.3333", "boman": "0.3767", "helix": "0.6667", "turn_pct": "0.0", "sheet": "0.0" }, { "id": "aceip0052", "seq": "AQL", "length": "3", "detail": "ND", "source": "ND", "ic50": "57.5 mM", "reference": "Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.", "doi": "10.1021\/jf051263l", "pubmedid": "16448176", "mw": "330.38", "pi": "5.57", "charge_ph7": "-0.2", "gravy": "0.7", "instability": "6.67", "hydrophobic": "0.6667", "boman": "-1.79", "helix": "0.6667", "turn_pct": "0.0", "sheet": "0.3333" }, { "id": "aceip0053", "seq": "AQTQSL", "length": "6", "detail": "Milk (bovine) | Milk (human) | Amaranth", "source": "Milk | Plants", "ic50": null, "reference": "Enterococcus faecalis strains from food, environmental, and clinical origin produce ACE-inhibitory peptides and other bioactive peptides during growth in bovine skim milk.", "doi": "10.1016\/j.ijfoodmicro.2013.06.019", "pubmedid": "23845432", "mw": "646.69", "pi": "5.57", "charge_ph7": "-0.2", "gravy": "-0.4833", "instability": "69.0", "hydrophobic": "0.3333", "boman": "-0.485", "helix": "0.3333", "turn_pct": "0.1667", "sheet": "0.3333" }, { "id": "aceip0054", "seq": "AQTQSLVYP", "length": "9", "detail": "Milk (bovine β-caseins)", "source": "Milk", "ic50": "76 μM", "reference": "Inhibition of angiotensin-converting enzyme by synthetic peptide fragments of various beta-caseins.; Evaluation of the allergenicity of goat milk, cow milk, and their lactosera in a guinea pig model.", "doi": "10.3168\/jds.2008-1125", "pubmedid": "1368548 19233776", "mw": "1006.11", "pi": "5.57", "charge_ph7": "-0.21", "gravy": "-0.1778", "instability": "54.67", "hydrophobic": "0.4444", "boman": "-0.7567", "helix": "0.2222", "turn_pct": "0.2222", "sheet": "0.4444" }, { "id": "aceip0055", "seq": "AR", "length": "2", "detail": "ND", "source": "Milk", "ic50": "95.5 μM", "reference": "What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1016\/j.foodchem.2013.05.140", "pubmedid": "23871047", "mw": "245.28", "pi": "9.8", "charge_ph7": "0.8", "gravy": "-1.35", "instability": "5.0", "hydrophobic": "0.5", "boman": "0.455", "helix": "0.5", "turn_pct": "0.0", "sheet": "0.0" }, { "id": "aceip0056", "seq": "ARPAK", "length": "5", "detail": "ND", "source": "Milk | Bacteria", "ic50": "19.05 μM", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "23194537", "mw": "541.64", "pi": "11.0", "charge_ph7": "1.79", "gravy": "-1.28", "instability": "85.04", "hydrophobic": "0.6", "boman": "0.136", "helix": "0.6", "turn_pct": "0.2", "sheet": "0.0" }, { "id": "aceip0057", "seq": "ASP", "length": "3", "detail": "ND", "source": "Plants", "ic50": "240 μM", "reference": "What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1016\/j.foodchem.2013.05.140", "pubmedid": "23871047", "mw": "273.29", "pi": "5.57", "charge_ph7": "-0.2", "gravy": "-0.2", "instability": "153.13", "hydrophobic": "0.6667", "boman": "-0.3233", "helix": "0.3333", "turn_pct": "0.6667", "sheet": "0.0" }, { "id": "aceip0058", "seq": "AV", "length": "2", "detail": "Fermented sardine sauce", "source": "Fish", "ic50": "15 %(800μM)", "reference": "Angiotensin I-converting enzyme inhibitory activity and insulin secretion stimulative activity of fermented fish sauce.", "doi": "10.1016\/S1389-1723(03)70138-8", "pubmedid": "16233562", "mw": "188.22", "pi": "5.57", "charge_ph7": "-0.2", "gravy": "3.0", "instability": "5.0", "hydrophobic": "1.0", "boman": "-2.925", "helix": "0.5", "turn_pct": "0.0", "sheet": "0.5" }, { "id": "aceip0059", "seq": "AVF", "length": "3", "detail": "Spodoptera Insect", "source": "Insect", "ic50": "1374 μM", "reference": "Ala-Val-Phe and Val-Phe: ACE inhibitory peptides derived from insect protein with antihypertensive activity in spontaneously hypertensive rats.; Antihypertensive peptides from food proteins: a review.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1016\/j.peptides.2009.05.029; 10.1039\/c2fo10192k; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "19524628 22249830 23871047", "mw": "335.4", "pi": "5.57", "charge_ph7": "-0.2", "gravy": "2.9333", "instability": "6.67", "hydrophobic": "1.0", "boman": "-2.9433", "helix": "0.3333", "turn_pct": "0.0", "sheet": "0.6667" }, { "id": "aceip0060", "seq": "AVL", "length": "3", "detail": "Milk (bovine) | Salmon | Anchovy (sauce) | Fish (Sardine fermented sauce) | Fish Sauce | Cereals (Wheat) | Arachin | Chicken", "source": "Milk | Fish | Cereal | Legume | Chicken", "ic50": "<20 mM", "reference": "Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1021\/jf051263l; 10.1080\/10408398.2012.664829", "pubmedid": "16448176 24915368", "mw": "301.38", "pi": "5.57", "charge_ph7": "-0.2", "gravy": "3.2667", "instability": "6.67", "hydrophobic": "1.0", "boman": "-3.59", "helix": "0.6667", "turn_pct": "0.0", "sheet": "0.6667" }, { "id": "aceip0061", "seq": "AVNPIR", "length": "6", "detail": "ND", "source": "ND", "ic50": "13 μM", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "23194537", "mw": "668.79", "pi": "9.8", "charge_ph7": "0.8", "gravy": "0.15", "instability": "3.53", "hydrophobic": "0.6667", "boman": "-1.0717", "helix": "0.1667", "turn_pct": "0.3333", "sheet": "0.3333" }, { "id": "aceip0062", "seq": "AVP", "length": "3", "detail": "Fungi (Agaricus bisporus)", "source": "Fungi", "ic50": "<20 mM", "reference": "Bioactive peptides in amaranth (Amaranthus hypochondriacus) seed.; Evaluation of the allergenicity of goat milk, cow milk, and their lactosera in a guinea pig model.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1021\/jf072911z; 10.3168\/jds.2008-1125; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "18211015 19233776 23871047", "mw": "285.34", "pi": "5.57", "charge_ph7": "-0.2", "gravy": "1.4667", "instability": "70.87", "hydrophobic": "1.0", "boman": "-1.95", "helix": "0.3333", "turn_pct": "0.3333", "sheet": "0.3333" }, { "id": "aceip0063", "seq": "AVPYP", "length": "5", "detail": "ND", "source": "ND", "ic50": "80 μM", "reference": "Evaluation of the allergenicity of goat milk, cow milk, and their lactosera in a guinea pig model.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.3168\/jds.2008-1125; 10.1016\/j.foodchem.2012.09.092", "pubmedid": "19233776 23194537", "mw": "545.63", "pi": "5.57", "charge_ph7": "-0.21", "gravy": "0.3", "instability": "71.2", "hydrophobic": "0.8", "boman": "-1.142", "helix": "0.2", "turn_pct": "0.4", "sheet": "0.4" }, { "id": "aceip0064", "seq": "AVPYPQ", "length": "6", "detail": "ND", "source": "ND", "ic50": null, "reference": "Identification of angiotensin-I-converting enzyme inhibitory peptides derived from sodium caseinate hydrolysates produced by Lactobacillus helveticus NCC 2765.", "doi": "10.1021\/jf049510t", "pubmedid": "15537298", "mw": "673.76", "pi": "5.57", "charge_ph7": "-0.21", "gravy": "-0.3333", "instability": "93.1", "hydrophobic": "0.6667", "boman": "-0.725", "helix": "0.1667", "turn_pct": "0.3333", "sheet": "0.3333" }, { "id": "aceip0065", "seq": "AVPYPQP", "length": "7", "detail": "ND", "source": "ND", "ic50": "80 μM", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "23194537", "mw": "770.87", "pi": "5.57", "charge_ph7": "-0.21", "gravy": "-0.5143", "instability": "108.74", "hydrophobic": "0.7143", "boman": "-0.6214", "helix": "0.1429", "turn_pct": "0.4286", "sheet": "0.2857" }, { "id": "aceip0066", "seq": "AVPYPQR", "length": "7", "detail": "Milk (bovine)", "source": "Milk", "ic50": "15 μM", "reference": "Evaluation of the allergenicity of goat milk, cow milk, and their lactosera in a guinea pig model.; Antihypertensive peptides: production, bioavailability and incorporation into foods.; Bioactive peptides derived from milk proteins and their health beneficial potentials: an update.; Antihypertensive peptides from food proteins: a review.", "doi": "10.3168\/jds.2008-1125; 10.1016\/j.cis.2010.11.001; 10.1039\/c0fo00016g; 10.1039\/c2fo10192k", "pubmedid": "19233776 21185549 21773582 22249830", "mw": "829.94", "pi": "8.79", "charge_ph7": "0.79", "gravy": "-0.9286", "instability": "81.23", "hydrophobic": "0.5714", "boman": "-0.2329", "helix": "0.1429", "turn_pct": "0.2857", "sheet": "0.2857" }, { "id": "aceip0067", "seq": "AVV", "length": "3", "detail": "Milk (bovine, buffalo and ovine) | Chicken connectin", "source": "Milk | Chicken", "ic50": "66.6 μM", "reference": "Analysis of novel angiotensin I-converting enzyme inhibitory peptides from enzymatic hydrolysates of cuttlefish (Sepia officinalis) muscle proteins.; Review on the angiotensin-I-converting enzyme (ACE) inhibitor peptides from marine proteins.; What are the ideal properties for functional food peptides with antihypertensive effect? 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A computational peptidology approach.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1271\/bbb.60.661; 10.1021\/jf051263l; 10.1002\/psc.892; 10.1021\/jf0705670; 10.1021\/jf072911z; 10.1021\/jf903261h; 10.1016\/j.talanta.2012.12.041; 10.1016\/j.jprot.2013.06.023; 10.1016\/j.foodchem.2013.05.140; 10.1080\/10408398.2012.664829", "pubmedid": "8829536 16448176 17654623 17715987 18211015 19994857 23598136 23806758 23871047 24915368", "mw": "252.27", "pi": "5.57", "charge_ph7": "-0.21", "gravy": "0.25", "instability": "5.0", "hydrophobic": "0.5", "boman": "-0.835", "helix": "0.5", "turn_pct": "0.0", "sheet": "0.5" }, { "id": "aceip0072", "seq": "AYFTPE", "length": "6", "detail": "Milk (bovine)", "source": "Milk", "ic50": "104.71 μM", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "23194537", "mw": "726.77", "pi": "4.6", "charge_ph7": "-1.2", "gravy": "-0.4167", "instability": "37.3", "hydrophobic": "0.5", "boman": "-0.4583", "helix": "0.3333", "turn_pct": "0.1667", "sheet": "0.5" }, { "id": "aceip0073", "seq": "AYFYP", "length": "5", "detail": "Milk", "source": "Milk", "ic50": "500 μM", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "23194537", "mw": "659.73", "pi": "5.57", "charge_ph7": "-0.21", "gravy": "0.08", "instability": "97.88", "hydrophobic": "0.6", "boman": "-0.902", "helix": "0.2", "turn_pct": "0.2", "sheet": "0.6" }, { "id": "aceip0074", "seq": "AYFYPE", "length": "6", "detail": "ND", "source": "ND", "ic50": "106 μM", "reference": "Antihypertensive effect of the peptides derived from casein by an extracellular proteinase from Lactobacillus helveticus CP790.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.3168\/jds.S0022-0302(94)77026-0; 10.1016\/j.foodchem.2012.09.092", "pubmedid": "8201050 23194537", "mw": "788.84", "pi": "4.6", "charge_ph7": "-1.2", "gravy": "-0.5167", "instability": "112.2", "hydrophobic": "0.5", "boman": "-0.4783", "helix": "0.3333", "turn_pct": "0.1667", "sheet": "0.5" }, { "id": "aceip0075", "seq": "AYFYPEL", "length": "7", "detail": "Soybean", "source": "Legume", "ic50": "6.58 μM", "reference": "Antihypertensive peptides: production, bioavailability and incorporation into foods.; Antihypertensive peptides from food proteins: a review.; Glycinyl-histidinyl-serine (GHS), a novel rapeseed protein-derived peptide has blood pressure-lowering effect in spontaneously hypertensive rats.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1016\/j.cis.2010.11.001; 10.1039\/c2fo10192k; 10.1021\/jf400865m; 10.1080\/10408398.2012.664829", "pubmedid": "21185549 22249830 23919612 24915368", "mw": "902.0", "pi": "4.05", "charge_ph7": "-1.2", "gravy": "0.1", "instability": "97.6", "hydrophobic": "0.5714", "boman": "-1.1129", "helix": "0.4286", "turn_pct": "0.1429", "sheet": "0.5714" }, { "id": "aceip0076", "seq": "AYIASKGL", "length": "8", "detail": "Milk", "source": "Milk", "ic50": "34.67 μM", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "23194537", "mw": "821.96", "pi": "8.63", "charge_ph7": "0.79", "gravy": "0.6875", "instability": "-1.86", "hydrophobic": "0.5", "boman": "-1.48", "helix": "0.5", "turn_pct": "0.25", "sheet": "0.375" }, { "id": "aceip0077", "seq": "AYP", "length": "3", "detail": "Milk (bovine)", "source": "Milk", "ic50": null, "reference": "Isolation from alpha-zein of thermolysin peptides with angiotensin I-converting enzyme inhibitory activity.", "doi": "10.1271\/bbb.60.661", "pubmedid": "8829536", "mw": "349.38", "pi": "5.57", "charge_ph7": "-0.21", "gravy": "-0.3667", "instability": "47.8", "hydrophobic": "0.6667", "boman": "-0.5567", "helix": "0.3333", "turn_pct": "0.3333", "sheet": "0.3333" }, { "id": "aceip0078", "seq": "AYPQQ", "length": "5", "detail": "Flaxseed", "source": "Plants", "ic50": null, "reference": "Isolation from alpha-zein of thermolysin peptides with angiotensin I-converting enzyme inhibitory activity.", "doi": "10.1271\/bbb.60.661", "pubmedid": "8829536", "mw": "605.64", "pi": "5.57", "charge_ph7": "-0.21", "gravy": "-1.62", "instability": "109.72", "hydrophobic": "0.4", "boman": "0.21", "helix": "0.2", "turn_pct": "0.2", "sheet": "0.2" }, { "id": "aceip0079", "seq": "CF", "length": "2", "detail": "Meat", "source": "Meat", "ic50": "0.4 mg\/ml", "reference": "Review on the angiotensin-I-converting enzyme (ACE) inhibitor peptides from marine proteins.; Peptides with angiotensin I converting enzyme (ACE) inhibitory activity generated from porcine skeletal muscle proteins by the action of meat-borne Lactobacillus.; What are the ideal properties for functional food peptides with antihypertensive effect? 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A computational peptidology approach.", "doi": "10.1021\/jf051263l; 10.1002\/psc.892; 10.1021\/ic9001779; 10.1021\/ol900845g; 10.1007\/s00894-010-0862-x; 10.1016\/j.talanta.2012.12.041; 10.1016\/j.jprot.2013.06.023; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "16448176 17654623 19449891 19449894 20941517 23598136 23806758 23871047", "mw": "190.15", "pi": "4.05", "charge_ph7": "-1.24", "gravy": "-1.95", "instability": "5.0", "hydrophobic": "0.0", "boman": "0.37", "helix": "0.0", "turn_pct": "1.0", "sheet": "0.0" }, { "id": "aceip0092", "seq": "DGL", "length": "3", "detail": "Milk (human)", "source": "Milk", "ic50": "<20 mM", "reference": "Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1021\/jf051263l; 10.1080\/10408398.2012.664829", "pubmedid": "16448176 24915368", "mw": "303.31", "pi": "4.05", "charge_ph7": "-1.24", "gravy": "-0.0333", "instability": "6.67", "hydrophobic": "0.3333", "boman": "-1.3933", "helix": "0.3333", "turn_pct": "0.6667", "sheet": "0.3333" }, { "id": "aceip0093", "seq": "DHPFL", "length": "5", "detail": "Wakame | Synthesized | Cereals (Soybean+Wheat) | Cereals (Finnish) | Soybean | Soybean (Fermented) | Soybean Sauce | Chicken", "source": "Plants | Synthesized | Cereal | Legume | Chicken", "ic50": "6.2 μM", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "23194537", "mw": "627.69", "pi": "5.08", "charge_ph7": "-1.15", "gravy": "-0.34", "instability": "40.76", "hydrophobic": "0.6", "boman": "-1.046", "helix": "0.2", "turn_pct": "0.4", "sheet": "0.4" }, { "id": "aceip0094", "seq": "DIGYY", "length": "5", "detail": "Wine", "source": "Cereal", "ic50": "3.39 μM", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "23194537", "mw": "629.66", "pi": "4.05", "charge_ph7": "-1.24", "gravy": "-0.4", "instability": "15.7", "hydrophobic": "0.2", "boman": "-0.78", "helix": "0.0", "turn_pct": "0.4", "sheet": "0.6" }, { "id": "aceip0095", "seq": "DKIHP", "length": "5", "detail": "Cheese (Manchego cheese)", "source": "Milk", "ic50": "113 μM", "reference": "The potential role of milk-derived peptides in cardiovascular disease.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1039\/c1fo10017c; 10.1016\/j.foodchem.2012.09.092", "pubmedid": "21779574 23194537", "mw": "608.69", "pi": "6.74", "charge_ph7": "-0.15", "gravy": "-1.54", "instability": "-7.04", "hydrophobic": "0.4", "boman": "-0.134", "helix": "0.2", "turn_pct": "0.4", "sheet": "0.2" }, { "id": "aceip0096", "seq": "DKIHPF", "length": "6", "detail": "Soybean", "source": "Legume", "ic50": "256.8 μM", "reference": "Angiotensin-converting enzyme inhibitory activity of peptides derived from caprine kefir.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.3168\/jds.S0022-0302(05)73032-0; 10.1016\/j.foodchem.2012.09.092", "pubmedid": "16162521 23194537", "mw": "755.86", "pi": "6.74", "charge_ph7": "-0.15", "gravy": "-0.8167", "instability": "27.9", "hydrophobic": "0.5", "boman": "-0.6083", "helix": "0.1667", "turn_pct": "0.3333", "sheet": "0.3333" }, { "id": "aceip0097", "seq": "DKIYPSFQPQPLIYP", "length": "15", "detail": "Milk (bovine) | Amaranth | Cereals (Maize) | Maize | Cereals (Buckwheat) | Cereals (Soybean+Wheat) | Soybean | Soybean (Fermented) | Soybean Sauce | Pork | Chicken | Chicken connectin", "source": "Milk | Plants | Cereal | Legume | Porcine | Chicken", "ic50": "107 μM", "reference": "Inhibition of angiotensin-converting enzyme by synthetic peptide fragments of various beta-caseins.", "doi": "", "pubmedid": "1368548", "mw": "1806.06", "pi": "5.83", "charge_ph7": "-0.24", "gravy": "-0.5733", "instability": "65.83", "hydrophobic": "0.5333", "boman": "-0.7093", "helix": "0.1333", "turn_pct": "0.4", "sheet": "0.4" }, { "id": "aceip0098", "seq": "DKVGINY", "length": "7", "detail": "Meat", "source": "Meat", "ic50": "99.9 μM", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "23194537", "mw": "807.89", "pi": "5.83", "charge_ph7": "-0.24", "gravy": "-0.5571", "instability": "-39.94", "hydrophobic": "0.2857", "boman": "-0.6971", "helix": "0.1429", "turn_pct": "0.4286", "sheet": "0.4286" }, { "id": "aceip0099", "seq": "DKVGINYW", "length": "8", "detail": "ND", "source": "ND", "ic50": "25.4 μM", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "23194537", "mw": "994.1", "pi": "5.83", "charge_ph7": "-0.24", "gravy": "-0.6", "instability": "-46.66", "hydrophobic": "0.375", "boman": "-0.9013", "helix": "0.125", "turn_pct": "0.375", "sheet": "0.5" }, { "id": "aceip0100", "seq": "DL", "length": "2", "detail": "Milk-Cheese (Goat milk protein and cheeses)", "source": "Milk", "ic50": "<20 mM", "reference": "Angiotensin I-converting enzyme inhibitory activity and insulin secretion stimulative activity of fermented fish sauce.; Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.", "doi": "10.1016\/S1389-1723(03)70138-8; 10.1021\/jf051263l", "pubmedid": "16233562 16448176", "mw": "246.26", "pi": "4.05", "charge_ph7": "-1.24", "gravy": "0.15", "instability": "5.0", "hydrophobic": "0.5", "boman": "-1.62", "helix": "0.5", "turn_pct": "0.5", "sheet": "0.5" }, { "id": "aceip0101", "seq": "DLP", "length": "3", "detail": "Milk (bovine)", "source": "Milk", "ic50": "<20 mM", "reference": "Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; A molecular keypad lock based on the thiacalix[4]arene of 1,3-alternate conformation.; Vegetable foods: a cheap source of proteins and peptides with antihypertensive, antioxidant, and other less occurrence bioactivities.", "doi": "10.1021\/jf051263l; 10.1021\/ol900845g; 10.1016\/j.talanta.2012.12.041", "pubmedid": "16448176 19449894 23598136", "mw": "343.38", "pi": "4.05", "charge_ph7": "-1.24", "gravy": "-0.4333", "instability": "70.87", "hydrophobic": "0.6667", "boman": "-1.08", "helix": "0.3333", "turn_pct": "0.6667", "sheet": "0.3333" }, { "id": "aceip0102", "seq": "DLRPDNAKA", "length": "9", "detail": "Milk (bovine) | Milk", "source": "Milk", "ic50": null, "reference": "High throughput screening of bradykinin-potentiating peptides in Bothrops moojeni snake venom using precursor ion mass spectrometry.", "doi": "10.1016\/j.toxicon.2008.02.019", "pubmedid": "18471845", "mw": "999.08", "pi": "5.96", "charge_ph7": "-0.24", "gravy": "-1.4556", "instability": "43.31", "hydrophobic": "0.4444", "boman": "0.0822", "helix": "0.4444", "turn_pct": "0.4444", "sheet": "0.1111" }, { "id": "aceip0103", "seq": "DLTDY", "length": "5", "detail": "Milk (bovine) | Milk | Casein | Enzymatic-hydrolysis (Hydrolysis with pepsin) | Miso paste with casein", "source": "Milk | Synthesized | Legume", "ic50": "143 μM", "reference": "Antihypertensive peptides from food proteins: a review.", "doi": "10.1039\/c2fo10192k", "pubmedid": "22249830", "mw": "625.62", "pi": "4.05", "charge_ph7": "-2.24", "gravy": "-1.04", "instability": "8.0", "hydrophobic": "0.2", "boman": "-0.232", "helix": "0.2", "turn_pct": "0.4", "sheet": "0.6" }, { "id": "aceip0104", "seq": "DM", "length": "2", "detail": "ND", "source": "ND", "ic50": "<20 mM", "reference": "What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1016\/j.foodchem.2013.05.140", "pubmedid": "23871047", "mw": "264.3", "pi": "4.05", "charge_ph7": "-1.24", "gravy": "-0.8", "instability": "5.0", "hydrophobic": "0.5", "boman": "-0.335", "helix": "0.5", "turn_pct": "0.5", "sheet": "0.0" }, { "id": "aceip0105", "seq": "DMIPAQK", "length": "7", "detail": "Meat", "source": "Meat", "ic50": "45 μM", "reference": "Peptide inhibitors for angiotensin I-converting enzyme from thermolysin digest of dried bonito.", "doi": "10.1271\/bbb.56.1541", "pubmedid": "1369054", "mw": "801.95", "pi": "5.84", "charge_ph7": "-0.24", "gravy": "-0.6143", "instability": "31.97", "hydrophobic": "0.5714", "boman": "-0.6371", "helix": "0.4286", "turn_pct": "0.2857", "sheet": "0.1429" }, { "id": "aceip0106", "seq": "DMSVF", "length": "5", "detail": "Cereals (Maize)", "source": "Cereal", "ic50": null, "reference": "Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1080\/10408398.2012.664829", "pubmedid": "24915368", "mw": "597.68", "pi": "4.05", "charge_ph7": "-1.24", "gravy": "0.92", "instability": "95.88", "hydrophobic": "0.6", "boman": "-1.37", "helix": "0.2", "turn_pct": "0.4", "sheet": "0.4" }, { "id": "aceip0107", "seq": "DP", "length": "2", "detail": "Cereals (Maize)", "source": "Cereal", "ic50": "2.15 μM", "reference": "Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1080\/10408398.2012.664829", "pubmedid": "24915368", "mw": "230.22", "pi": "4.05", "charge_ph7": "-1.24", "gravy": "-2.55", "instability": "5.0", "hydrophobic": "0.5", "boman": "0.84", "helix": "0.0", "turn_pct": "1.0", "sheet": "0.0" }, { "id": "aceip0108", "seq": "DQVFPMNPPK", "length": "10", "detail": "Cotton leafworm", "source": "Insect", "ic50": null, "reference": "Angiotensin I-converting enzyme inhibitory peptides generated from in vitro gastrointestinal digestion of pork meat.", "doi": "10.1021\/jf904204n", "pubmedid": "20151679", "mw": "1172.35", "pi": "5.84", "charge_ph7": "-0.24", "gravy": "-1.03", "instability": "29.56", "hydrophobic": "0.6", "boman": "-0.313", "helix": "0.2", "turn_pct": "0.5", "sheet": "0.2" }, { "id": "aceip0109", "seq": "DRVYIHPFHL", "length": "10", "detail": "Meat", "source": "Meat", "ic50": "75.86 μM", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.; VPPIPP and IPPVPP: two hexapeptides innovated to exert antihypertensive activity.", "doi": "10.1016\/j.foodchem.2012.09.092; 10.1371\/journal.pone.0062384", "pubmedid": "23194537 23638059", "mw": "1296.48", "pi": "6.92", "charge_ph7": "-0.07", "gravy": "-0.2", "instability": "22.64", "hydrophobic": "0.5", "boman": "-1.034", "helix": "0.1", "turn_pct": "0.2", "sheet": "0.5" }, { "id": "aceip0110", "seq": "DV", "length": "2", "detail": "Soybean", "source": "Legume", "ic50": null, "reference": "Quantitative structure-activity relationship study of bitter di- and tri-peptides including relationship with angiotensin I-converting enzyme inhibitory activity.", "doi": "10.1002\/psc.800", "pubmedid": "17117396", "mw": "232.23", "pi": "4.05", "charge_ph7": "-1.24", "gravy": "0.35", "instability": "5.0", "hydrophobic": "0.5", "boman": "-1.18", "helix": "0.0", "turn_pct": "0.5", "sheet": "0.5" }, { "id": "aceip0111", "seq": "DVENLHLPLPLLQSW", "length": "15", "detail": "Fish (Shark) | Pork", "source": "Fish | Porcine", "ic50": null, "reference": "Identification of angiotensin-I-converting enzyme inhibitory peptides derived from sodium caseinate hydrolysates produced by Lactobacillus helveticus NCC 2765.", "doi": "10.1021\/jf049510t", "pubmedid": "15537298", "mw": "1774.02", "pi": "4.35", "charge_ph7": "-2.15", "gravy": "0.0733", "instability": "86.04", "hydrophobic": "0.6", "boman": "-1.5227", "helix": "0.4", "turn_pct": "0.3333", "sheet": "0.4667" }, { "id": "aceip0112", "seq": "DW", "length": "2", "detail": "Sweet-potato", "source": "Potato", "ic50": "13 μM", "reference": "Inhibition strength of short peptides derived from an ACE inhibitory peptide.", "doi": "10.1021\/jf202902r", "pubmedid": "21923188", "mw": "319.31", "pi": "4.05", "charge_ph7": "-1.24", "gravy": "-2.2", "instability": "5.0", "hydrophobic": "0.5", "boman": "-0.325", "helix": "0.0", "turn_pct": "0.5", "sheet": "0.5" }, { "id": "aceip0113", "seq": "DWGP", "length": "4", "detail": "Milk | Milk (whey)", "source": "Milk", "ic50": null, "reference": "Antihypertensive peptides: production, bioavailability and incorporation into foods.", "doi": "10.1016\/j.cis.2010.11.001", "pubmedid": "21185549", "mw": "473.48", "pi": "4.05", "charge_ph7": "-1.24", "gravy": "-1.6", "instability": "-18.42", "hydrophobic": "0.5", "boman": "-0.3975", "helix": "0.0", "turn_pct": "0.75", "sheet": "0.25" }, { "id": "aceip0114", "seq": "DY", "length": "2", "detail": "Legume (Peanut)", "source": "Legume", "ic50": "<20 mM", "reference": "Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Antihypertensive peptides from food proteins: a review.", "doi": "10.1021\/jf051263l; 10.1039\/c2fo10192k", "pubmedid": "16448176 22249830", "mw": "296.28", "pi": "4.05", "charge_ph7": "-1.24", "gravy": "-2.4", "instability": "5.0", "hydrophobic": "0.0", "boman": "0.91", "helix": "0.0", "turn_pct": "0.5", "sheet": "0.5" }, { "id": "aceip0115", "seq": "DYG", "length": "3", "detail": "Fish (Alaska pollack) | Fish (Skipjack tuna)", "source": "Fish", "ic50": "<20 mM", "reference": "Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.", "doi": "10.1021\/jf051263l", "pubmedid": "16448176", "mw": "353.33", "pi": "4.05", "charge_ph7": "-1.24", "gravy": "-1.7333", "instability": "-21.63", "hydrophobic": "0.0", "boman": "0.2933", "helix": "0.0", "turn_pct": "0.6667", "sheet": "0.3333" }, { "id": "aceip0116", "seq": "DYGLYP", "length": "6", "detail": "Milk (bovine) | Carp | Cereals | Pork | Chicken", "source": "Milk | Fish | Cereal | Porcine | Chicken", "ic50": "62 μM", "reference": "Peptide inhibitors for angiotensin I-converting enzyme from thermolysin digest of dried bonito.; Review on the angiotensin-I-converting enzyme (ACE) inhibitor peptides from marine proteins.", "doi": "10.1271\/bbb.56.1541; 10.1007\/s12010-012-0024-y", "pubmedid": "1369054 23271625", "mw": "726.77", "pi": "4.05", "charge_ph7": "-1.24", "gravy": "-0.7167", "instability": "14.75", "hydrophobic": "0.3333", "boman": "-0.65", "helix": "0.1667", "turn_pct": "0.5", "sheet": "0.5" }, { "id": "aceip0117", "seq": "DYVGN", "length": "5", "detail": "Milk (whey)", "source": "Milk", "ic50": "0.72 μM", "reference": "Inhibition strength of short peptides derived from an ACE inhibitory peptide.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1021\/jf202902r; 10.1016\/j.foodchem.2012.09.092", "pubmedid": "21923188 23194537", "mw": "566.56", "pi": "4.05", "charge_ph7": "-1.24", "gravy": "-0.9", "instability": "-25.96", "hydrophobic": "0.2", "boman": "-0.308", "helix": "0.0", "turn_pct": "0.6", "sheet": "0.4" }, { "id": "aceip0118", "seq": "EA", "length": "2", "detail": "Milk (bovine)", "source": "Milk", "ic50": "10000 μM", "reference": "Binding of peptide substrates and inhibitors of angiotensin-converting enzyme. Importance of the COOH-terminal dipeptide sequence.; Three-dimensional holograph vector of atomic interaction field (3D-HoVAIF): a novel rotation-translation invariant 3D structure descriptor and its applications to peptides.; QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.; Peptides with angiotensin I converting enzyme (ACE) inhibitory activity generated from porcine skeletal muscle proteins by the action of meat-borne Lactobacillus.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1002\/psc.892; 10.1007\/s00894-010-0862-x; 10.1016\/j.jprot.2013.06.023; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "6243277 17654623 20941517 23806758 23871047", "mw": "218.21", "pi": "4.05", "charge_ph7": "-1.16", "gravy": "-0.85", "instability": "5.0", "hydrophobic": "0.5", "boman": "-0.085", "helix": "1.0", "turn_pct": "0.0", "sheet": "0.0" }, { "id": "aceip0119", "seq": "EAP", "length": "3", "detail": "Milk (bovine) | Milk | Milk (Digested milk products)", "source": "Milk", "ic50": "<20 mM", "reference": "Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.", "doi": "10.1021\/jf051263l", "pubmedid": "16448176", "mw": "315.32", "pi": "4.05", "charge_ph7": "-1.16", "gravy": "-1.1", "instability": "70.87", "hydrophobic": "0.6667", "boman": "-0.0567", "helix": "0.6667", "turn_pct": "0.3333", "sheet": "0.0" }, { "id": "aceip0120", "seq": "EG", "length": "2", "detail": "Marine Rotifer", "source": "Animal", "ic50": "<20 mM", "reference": "Binding of peptide substrates and inhibitors of angiotensin-converting enzyme. Importance of the COOH-terminal dipeptide sequence.; Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Three-dimensional holograph vector of atomic interaction field (3D-HoVAIF): a novel rotation-translation invariant 3D structure descriptor and its applications to peptides.; QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.; Peptides with angiotensin I converting enzyme (ACE) inhibitory activity generated from porcine skeletal muscle proteins by the action of meat-borne Lactobacillus.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1021\/jf051263l; 10.1002\/psc.892; 10.1007\/s00894-010-0862-x; 10.1016\/j.jprot.2013.06.023; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "6243277 16448176 17654623 20941517 23806758 23871047", "mw": "204.18", "pi": "4.05", "charge_ph7": "-1.16", "gravy": "-1.95", "instability": "5.0", "hydrophobic": "0.0", "boman": "0.35", "helix": "0.5", "turn_pct": "0.5", "sheet": "0.0" }, { "id": "aceip0121", "seq": "EGEPR", "length": "5", "detail": "Bovine", "source": "Bovine", "ic50": "728.2 ± 6.6 μM", "reference": "Novel angiotensin I-converting enzyme inhibitory peptides derived from edible mushroom Agaricus bisporus (J.E. Lange) Imbach identified by LC-MS\/MS.", "doi": "10.1016\/j.foodchem.2013.10.053", "pubmedid": "24262574", "mw": "586.6", "pi": "4.53", "charge_ph7": "-1.16", "gravy": "-2.7", "instability": "16.36", "hydrophobic": "0.2", "boman": "1.012", "helix": "0.4", "turn_pct": "0.4", "sheet": "0.0" }, { "id": "aceip0122", "seq": "EGGPKP", "length": "6", "detail": "Milk", "source": "Milk", "ic50": null, "reference": "Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1080\/10408398.2012.664829", "pubmedid": "24915368", "mw": "583.63", "pi": "6.1", "charge_ph7": "-0.16", "gravy": "-1.9", "instability": "16.33", "hydrophobic": "0.3333", "boman": "0.2233", "helix": "0.3333", "turn_pct": "0.6667", "sheet": "0.0" }, { "id": "aceip0123", "seq": "EIAKLM", "length": "6", "detail": "Anchovy (sauce)", "source": "Fish", "ic50": null, "reference": "Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1080\/10408398.2012.664829", "pubmedid": "24915368", "mw": "703.89", "pi": "6.1", "charge_ph7": "-0.16", "gravy": "0.7667", "instability": "26.28", "hydrophobic": "0.6667", "boman": "-1.7967", "helix": "0.8333", "turn_pct": "0.0", "sheet": "0.3333" }, { "id": "aceip0124", "seq": "EK", "length": "2", "detail": "Cuttle Fish", "source": "Fish", "ic50": "0 0", "reference": "Application of at-line two-dimensional liquid chromatography-mass spectrometry for identification of small hydrophilic angiotensin I-inhibiting peptides in milk hydrolysates.", "doi": "10.1007\/s00216-008-1990-3", "pubmedid": "18392815", "mw": "275.3", "pi": "6.1", "charge_ph7": "-0.16", "gravy": "-3.7", "instability": "5.0", "hydrophobic": "0.0", "boman": "1.61", "helix": "1.0", "turn_pct": "0.0", "sheet": "0.0" }, { "id": "aceip0125", "seq": "EKDERF", "length": "6", "detail": "Synthesized | Bovine", "source": "Synthesized | Bovine", "ic50": "10.0-848.0 μM", "reference": "Identification of novel angiotensin-converting enzyme-inhibitory peptides from ovine milk proteins by CE-MS and chromatographic techniques.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1002\/elps.200700324; 10.1080\/10408398.2012.664829", "pubmedid": "17948260 24915368", "mw": "822.86", "pi": "4.68", "charge_ph7": "-1.16", "gravy": "-2.6833", "instability": "8.33", "hydrophobic": "0.1667", "boman": "1.0467", "helix": "0.5", "turn_pct": "0.1667", "sheet": "0.1667" }, { "id": "aceip0126", "seq": "EKERERQ", "length": "7", "detail": "Milk", "source": "Milk", "ic50": "552.5 552.5", "reference": "Porcine skeletal muscle troponin is a good source of peptides with Angiotensin-I converting enzyme inhibitory activity and antihypertensive effects in spontaneously hypertensive rats.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1021\/jf071408j; 10.1080\/10408398.2012.664829", "pubmedid": "18163567 24915368", "mw": "974.03", "pi": "6.33", "charge_ph7": "-0.16", "gravy": "-3.8429", "instability": "36.09", "hydrophobic": "0.0", "boman": "1.9", "helix": "0.5714", "turn_pct": "0.0", "sheet": "0.0" }, { "id": "aceip0127", "seq": "EKV", "length": "3", "detail": "Milk (bovine) | Cereals | Soybean | pea | Pork | Chicken", "source": "Milk | Cereal | Legume | Porcine | Chicken", "ic50": null, "reference": "Hot topic: Changes in angiotensin-converting enzyme inhibition and concentrations of the tripeptides Val-Pro-Pro and Ile-Pro-Pro during ripening of different Swiss cheese varieties.", "doi": "10.3168\/jds.2008-1531", "pubmedid": "19233775", "mw": "374.43", "pi": "6.1", "charge_ph7": "-0.16", "gravy": "-1.0667", "instability": "-21.63", "hydrophobic": "0.3333", "boman": "-0.2733", "helix": "0.6667", "turn_pct": "0.0", "sheet": "0.3333" }, { "id": "aceip0128", "seq": "ELEELNVPGE", "length": "10", "detail": "Royal jelly", "source": "Insect", "ic50": null, "reference": "Casein fermentate of Lactobacillus animalis DPC6134 contains a range of novel propeptide angiotensin-converting enzyme inhibitors.", "doi": "10.1128\/AEM.00096-07", "pubmedid": "17483275", "mw": "1128.19", "pi": "4.05", "charge_ph7": "-4.15", "gravy": "-0.77", "instability": "53.32", "hydrophobic": "0.4", "boman": "-0.664", "helix": "0.6", "turn_pct": "0.3", "sheet": "0.3" }, { "id": "aceip0129", "seq": "EMPFPK", "length": "6", "detail": "ND", "source": "ND", "ic50": "423 mg\/ml", "reference": "Evaluation of the allergenicity of goat milk, cow milk, and their lactosera in a guinea pig model.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.3168\/jds.2008-1125; 10.1016\/j.foodchem.2012.09.092", "pubmedid": "19233776 23194537", "mw": "747.9", "pi": "6.1", "charge_ph7": "-0.16", "gravy": "-0.9833", "instability": "145.77", "hydrophobic": "0.6667", "boman": "-0.3517", "helix": "0.5", "turn_pct": "0.3333", "sheet": "0.1667" }, { "id": "aceip0130", "seq": "EMPFPKYPVEP", "length": "11", "detail": "Egg (Ovalbumin)", "source": "Egg", "ic50": null, "reference": "Casein fermentate of Lactobacillus animalis DPC6134 contains a range of novel propeptide angiotensin-converting enzyme inhibitors.", "doi": "10.1128\/AEM.00096-07", "pubmedid": "17483275", "mw": "1333.55", "pi": "4.53", "charge_ph7": "-1.16", "gravy": "-0.8818", "instability": "130.29", "hydrophobic": "0.6364", "boman": "-0.3973", "helix": "0.3636", "turn_pct": "0.3636", "sheet": "0.2727" }, { "id": "aceip0131", "seq": "ENLHLP", "length": "6", "detail": "ND", "source": "ND", "ic50": ">1000 μM", "reference": "Inhibition of angiotensin-converting enzyme by synthetic peptide fragments of various beta-caseins.", "doi": "", "pubmedid": "1368548", "mw": "721.8", "pi": "5.24", "charge_ph7": "-1.08", "gravy": "-0.7", "instability": "40.43", "hydrophobic": "0.5", "boman": "-0.9317", "helix": "0.5", "turn_pct": "0.3333", "sheet": "0.3333" }, { "id": "aceip0132", "seq": "ENLHLPLPLL", "length": "10", "detail": "Milk (bovine)", "source": "Milk", "ic50": "250 μM", "reference": "Identification of angiotensin-I-converting enzyme inhibitory peptides derived from sodium caseinate hydrolysates produced by Lactobacillus helveticus NCC 2765.", "doi": "10.1021\/jf049510t", "pubmedid": "15537298", "mw": "1158.39", "pi": "5.24", "charge_ph7": "-1.08", "gravy": "0.56", "instability": "47.52", "hydrophobic": "0.7", "boman": "-2.035", "helix": "0.6", "turn_pct": "0.3", "sheet": "0.5" }, { "id": "aceip0133", "seq": "ENLLRF", "length": "6", "detail": "Synthesized", "source": "Synthesized", "ic50": "82.4 μM", "reference": "Angiotensin-converting enzyme inhibitory activity of peptides derived from caprine kefir.", "doi": "10.3168\/jds.S0022-0302(05)73032-0", "pubmedid": "16162521", "mw": "790.91", "pi": "6.1", "charge_ph7": "-0.16", "gravy": "-0.1833", "instability": "40.43", "hydrophobic": "0.5", "boman": "-1.14", "helix": "0.5", "turn_pct": "0.1667", "sheet": "0.5" }, { "id": "aceip0134", "seq": "ENLLRFFVAPFPEVFG", "length": "16", "detail": "Milk-Cheese (Goat milk protein and cheeses) | Cheese (Manchego cheese) | Milk-Cheese (Sheep milk and cheeses proteins)", "source": "Milk", "ic50": "250 μM", "reference": "Identification of angiotensin-I-converting enzyme inhibitory peptides derived from sodium caseinate hydrolysates produced by Lactobacillus helveticus NCC 2765.", "doi": "10.1021\/jf049510t", "pubmedid": "15537298", "mw": "1882.16", "pi": "4.53", "charge_ph7": "-1.16", "gravy": "0.65", "instability": "68.39", "hydrophobic": "0.6875", "boman": "-1.5606", "helix": "0.3125", "turn_pct": "0.25", "sheet": "0.5" }, { "id": "aceip0135", "seq": "EP", "length": "2", "detail": "Milk (bovine) | Milk (whey) | Milk (Fermented Milk) | Milk-Cheese (Goat milk protein and cheeses) | Milk-Cheese (Sheep milk and cheeses proteins) | Milk (caprine kefir)", "source": "Milk", "ic50": "1200 μM", "reference": "Angiotensin I-converting enzyme inhibitory activity and insulin secretion stimulative activity of fermented fish sauce.; ACE inhibitory tetrapeptides from Amaranthus hypochondriacus 11S globulin.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1016\/S1389-1723(03)70138-8; 10.1016\/j.phytochem.2009.04.006; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "16233562 19443002 23871047", "mw": "244.24", "pi": "4.05", "charge_ph7": "-1.16", "gravy": "-2.55", "instability": "101.3", "hydrophobic": "0.5", "boman": "0.82", "helix": "0.5", "turn_pct": "0.5", "sheet": "0.0" }, { "id": "aceip0136", "seq": "EPIPYGFLP", "length": "9", "detail": "Milk (human)", "source": "Milk", "ic50": "180 μM", "reference": "Inhibition of angiotensin-converting enzyme by synthetic peptide fragments of various beta-caseins.", "doi": "", "pubmedid": "1368548", "mw": "1032.19", "pi": "4.05", "charge_ph7": "-1.16", "gravy": "0.1222", "instability": "39.06", "hydrophobic": "0.6667", "boman": "-1.3311", "helix": "0.2222", "turn_pct": "0.4444", "sheet": "0.4444" }, { "id": "aceip0137", "seq": "EPR", "length": "3", "detail": "Milk (whey)", "source": "Milk", "ic50": "382->1000 μM", "reference": "Angiotensin I-converting enzyme inhibitory peptides generated from in vitro gastrointestinal digestion of pork meat.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1021\/jf904204n; 10.1080\/10408398.2012.664829", "pubmedid": "20151679 24915368", "mw": "400.43", "pi": "6.1", "charge_ph7": "-0.16", "gravy": "-3.2", "instability": "45.73", "hydrophobic": "0.3333", "boman": "1.4533", "helix": "0.3333", "turn_pct": "0.3333", "sheet": "0.0" }, { "id": "aceip0138", "seq": "EPVLGPVRGPFP", "length": "12", "detail": "Milk (whey)", "source": "Milk", "ic50": "790 μM", "reference": "Casein fermentate of Lactobacillus animalis DPC6134 contains a range of novel propeptide angiotensin-converting enzyme inhibitors.", "doi": "10.1128\/AEM.00096-07", "pubmedid": "17483275", "mw": "1264.47", "pi": "6.1", "charge_ph7": "-0.16", "gravy": "-0.0167", "instability": "82.34", "hydrophobic": "0.6667", "boman": "-1.125", "helix": "0.1667", "turn_pct": "0.5", "sheet": "0.3333" }, { "id": "aceip0139", "seq": "ER", "length": "2", "detail": "Fish (Sardine fermented sauce)", "source": "Fish", "ic50": "667 μM", "reference": "Angiotensin I-converting enzyme inhibitory peptides generated from in vitro gastrointestinal digestion of pork meat.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1021\/jf904204n; 10.1016\/j.foodchem.2013.05.140; 10.1080\/10408398.2012.664829", "pubmedid": "20151679 23871047 24915368", "mw": "303.31", "pi": "6.1", "charge_ph7": "-0.16", "gravy": "-4.0", "instability": "5.0", "hydrophobic": "0.0", "boman": "2.18", "helix": "0.5", "turn_pct": "0.0", "sheet": "0.0" }, { "id": "aceip0140", "seq": "ERKIKVYL", "length": "8", "detail": "Cereals (Finnish) | Soybean", "source": "Cereal | Legume", "ic50": "1.2 μM", "reference": "Angiotensin I converting enzyme inhibitory peptides from simulated in vitro gastrointestinal digestion of cooked eggs.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1021\/jf8028557; 10.1016\/j.foodchem.2012.09.092; 10.1080\/10408398.2012.664829", "pubmedid": "19154160 23194537 24915368", "mw": "1048.28", "pi": "9.7", "charge_ph7": "1.83", "gravy": "-0.575", "instability": "-32.51", "hydrophobic": "0.375", "boman": "-0.7775", "helix": "0.5", "turn_pct": "0.0", "sheet": "0.5" }, { "id": "aceip0141", "seq": "ERYPI", "length": "5", "detail": "Egg (Ovalbumin)", "source": "Egg", "ic50": "6.59-27.38 μM", "reference": "Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1080\/10408398.2012.664829", "pubmedid": "24915368", "mw": "676.76", "pi": "6.1", "charge_ph7": "-0.16", "gravy": "-1.28", "instability": "17.6", "hydrophobic": "0.4", "boman": "-0.084", "helix": "0.2", "turn_pct": "0.2", "sheet": "0.4" }, { "id": "aceip0142", "seq": "ESIINF", "length": "6", "detail": "Brazilian lancehead", "source": "Animal", "ic50": null, "reference": "Antihypertensive peptides from food proteins: a review.", "doi": "10.1039\/c2fo10192k", "pubmedid": "22249830", "mw": "721.8", "pi": "4.05", "charge_ph7": "-1.16", "gravy": "0.6667", "instability": "15.38", "hydrophobic": "0.5", "boman": "-1.4533", "helix": "0.1667", "turn_pct": "0.3333", "sheet": "0.5" }, { "id": "aceip0143", "seq": "EV", "length": "2", "detail": "Oyster", "source": "Animal", "ic50": "0 0", "reference": "Quantitative structure-activity relationship study of bitter di- and tri-peptides including relationship with angiotensin I-converting enzyme inhibitory activity.; Application of at-line two-dimensional liquid chromatography-mass spectrometry for identification of small hydrophilic angiotensin I-inhibiting peptides in milk hydrolysates.; Peptides with angiotensin I converting enzyme (ACE) inhibitory activity generated from porcine skeletal muscle proteins by the action of meat-borne Lactobacillus.", "doi": "10.1002\/psc.800; 10.1007\/s00216-008-1990-3; 10.1016\/j.jprot.2013.06.023", "pubmedid": "17117396 18392815 23806758", "mw": "246.26", "pi": "4.05", "charge_ph7": "-1.16", "gravy": "0.35", "instability": "5.0", "hydrophobic": "0.5", "boman": "-1.2", "helix": "0.5", "turn_pct": "0.0", "sheet": "0.5" }, { "id": "aceip0144", "seq": "EVLP", "length": "4", "detail": "ND", "source": "ND", "ic50": ">1000 μM", "reference": "Inhibition of angiotensin-converting enzyme by synthetic peptide fragments of various beta-caseins.", "doi": "", "pubmedid": "1368548", "mw": "456.53", "pi": "4.05", "charge_ph7": "-1.16", "gravy": "0.725", "instability": "55.65", "hydrophobic": "0.75", "boman": "-1.83", "helix": "0.5", "turn_pct": "0.25", "sheet": "0.5" }, { "id": "aceip0145", "seq": "EVMAGNLYPG", "length": "10", "detail": "Bonito", "source": "Fish", "ic50": "18.4 μM", "reference": "Angiotensin I converting enzyme (ACE) inhibitory peptide derived from the sauce of fermented blue mussel, Mytilus edulis.; Review on the angiotensin-I-converting enzyme (ACE) inhibitor peptides from marine proteins.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1016\/j.biortech.2005.01.001; 10.1007\/s12010-012-0024-y; 10.1080\/10408398.2012.664829", "pubmedid": "15978996 23271625 24915368", "mw": "1050.19", "pi": "4.05", "charge_ph7": "-1.16", "gravy": "0.1", "instability": "25.19", "hydrophobic": "0.5", "boman": "-1.16", "helix": "0.4", "turn_pct": "0.4", "sheet": "0.3" }, { "id": "aceip0146", "seq": "EVMAGNYLPG", "length": "10", "detail": "Chicken", "source": "Chicken", "ic50": "2.98 μM", "reference": "Angiotensin converting enzyme inhibitory peptides derived from food proteins: biochemistry, bioactivity and production.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.2174\/138161207780363068; 10.1016\/j.foodchem.2012.09.092", "pubmedid": "17430180 23194537", "mw": "1050.19", "pi": "4.05", "charge_ph7": "-1.16", "gravy": "0.1", "instability": "32.11", "hydrophobic": "0.5", "boman": "-1.16", "helix": "0.4", "turn_pct": "0.4", "sheet": "0.3" }, { "id": "aceip0147", "seq": "EW", "length": "2", "detail": "Shrimp", "source": "Shrimp", "ic50": "0 0", "reference": "Application of at-line two-dimensional liquid chromatography-mass spectrometry for identification of small hydrophilic angiotensin I-inhibiting peptides in milk hydrolysates.", "doi": "10.1007\/s00216-008-1990-3", "pubmedid": "18392815", "mw": "333.34", "pi": "4.05", "charge_ph7": "-1.16", "gravy": "-2.2", "instability": "-70.15", "hydrophobic": "0.5", "boman": "-0.345", "helix": "0.5", "turn_pct": "0.0", "sheet": "0.5" }, { "id": "aceip0148", "seq": "EWPRPQIPP", "length": "9", "detail": "Pork", "source": "Porcine", "ic50": null, "reference": "QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.", "doi": "10.1007\/s00894-010-0862-x", "pubmedid": "20941517", "mw": "1119.27", "pi": "6.1", "charge_ph7": "-0.16", "gravy": "-1.5889", "instability": "44.81", "hydrophobic": "0.6667", "boman": "-0.17", "helix": "0.1111", "turn_pct": "0.4444", "sheet": "0.2222" }, { "id": "aceip0149", "seq": "EY", "length": "2", "detail": "Pork", "source": "Porcine", "ic50": "0.4 mg\/ml", "reference": "Review on the angiotensin-I-converting enzyme (ACE) inhibitor peptides from marine proteins.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1007\/s12010-012-0024-y; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "23271625 23871047", "mw": "310.3", "pi": "4.05", "charge_ph7": "-1.16", "gravy": "-2.4", "instability": "5.0", "hydrophobic": "0.0", "boman": "0.89", "helix": "0.5", "turn_pct": "0.0", "sheet": "0.5" }, { "id": "aceip0150", "seq": "FAL", "length": "3", "detail": "ND", "source": "ND", "ic50": "<20 mM", "reference": "Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Angiotensin converting enzyme inhibitory peptides derived from food proteins: biochemistry, bioactivity and production.; Review on the angiotensin-I-converting enzyme (ACE) inhibitor peptides from marine proteins.; Vegetable foods: a cheap source of proteins and peptides with antihypertensive, antioxidant, and other less occurrence bioactivities.", "doi": "10.1021\/jf051263l; 10.2174\/138161207780363068; 10.1007\/s12010-012-0024-y; 10.1016\/j.talanta.2012.12.041", "pubmedid": "16448176 17430180 23271625 23598136", "mw": "349.42", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "2.8", "instability": "6.67", "hydrophobic": "1.0", "boman": "-3.2367", "helix": "0.6667", "turn_pct": "0.0", "sheet": "0.6667" }, { "id": "aceip0151", "seq": "FALPC", "length": "5", "detail": "Milk (bovine)", "source": "Milk", "ic50": "690.9 ± 5.3 μM", "reference": "Novel angiotensin I-converting enzyme inhibitory peptides derived from edible mushroom Agaricus bisporus (J.E. Lange) Imbach identified by LC-MS\/MS.", "doi": "10.1016\/j.foodchem.2013.10.053", "pubmedid": "24262574", "mw": "549.68", "pi": "5.52", "charge_ph7": "-0.25", "gravy": "1.86", "instability": "31.44", "hydrophobic": "0.8", "boman": "-2.198", "helix": "0.4", "turn_pct": "0.2", "sheet": "0.4" }, { "id": "aceip0152", "seq": "FALPQY", "length": "6", "detail": "Cheese (Manchego cheese)", "source": "Milk", "ic50": "4.3 μM", "reference": "Randomized controlled trial of sour milk on blood pressure in borderline hypertensive men.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.amjhyper.2004.03.674; 10.1016\/j.foodchem.2012.09.092", "pubmedid": "15288885 23194537", "mw": "737.84", "pi": "5.52", "charge_ph7": "-0.24", "gravy": "0.3333", "instability": "59.97", "hydrophobic": "0.6667", "boman": "-1.3683", "helix": "0.3333", "turn_pct": "0.1667", "sheet": "0.5" }, { "id": "aceip0153", "seq": "FALPQYLK", "length": "8", "detail": "Cheese (Manchego cheese)", "source": "Milk", "ic50": "4.3 μM", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "23194537", "mw": "979.17", "pi": "8.59", "charge_ph7": "0.76", "gravy": "0.2375", "instability": "36.86", "hydrophobic": "0.625", "boman": "-1.4438", "helix": "0.5", "turn_pct": "0.125", "sheet": "0.5" }, { "id": "aceip0154", "seq": "FAP", "length": "3", "detail": "Synthesized", "source": "Synthesized", "ic50": "<20 mM", "reference": "Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; What are the ideal properties for functional food peptides with antihypertensive effect? 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A computational peptidology approach.", "doi": "10.1016\/j.foodchem.2013.05.140", "pubmedid": "23871047", "mw": "432.51", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "1.8", "instability": "55.65", "hydrophobic": "1.0", "boman": "-2.2075", "helix": "0.25", "turn_pct": "0.25", "sheet": "0.5" }, { "id": "aceip0158", "seq": "FCF", "length": "3", "detail": "Bonito", "source": "Fish", "ic50": "11 μM", "reference": "Angiotensin I converting enzyme inhibitory peptides from simulated in vitro gastrointestinal digestion of cooked eggs.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1021\/jf8028557; 10.1080\/10408398.2012.664829", "pubmedid": "19154160 24915368", "mw": "415.51", "pi": "5.52", "charge_ph7": "-0.25", "gravy": "2.7", "instability": "6.67", "hydrophobic": "0.6667", "boman": "-2.4133", "helix": "0.0", "turn_pct": "0.0", "sheet": "0.6667" }, { "id": "aceip0159", "seq": "FCVLRP", "length": "6", "detail": "Flaxseed", "source": "Plants", "ic50": "12.3 μM", "reference": "Analysis of novel angiotensin-I-converting enzyme inhibitory peptides from protease-hydrolyzed marine shrimp Acetes chinensis.; Review on the angiotensin-I-converting enzyme (ACE) inhibitor peptides from marine proteins.", "doi": "10.1002\/psc.789; 10.1007\/s12010-012-0024-y", "pubmedid": "16981241 23271625", "mw": "733.92", "pi": "8.25", "charge_ph7": "0.75", "gravy": "1.2", "instability": "59.97", "hydrophobic": "0.6667", "boman": "-1.75", "helix": "0.1667", "turn_pct": "0.1667", "sheet": "0.5" }, { "id": "aceip0160", "seq": "FDK", "length": "3", "detail": "Synthesized", "source": "Synthesized", "ic50": "<20 mM", "reference": "Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.", "doi": "10.1021\/jf051263l", "pubmedid": "16448176", "mw": "408.45", "pi": "5.84", "charge_ph7": "-0.24", "gravy": "-1.5333", "instability": "19.5", "hydrophobic": "0.3333", "boman": "0.0933", "helix": "0.3333", "turn_pct": "0.3333", "sheet": "0.3333" }, { "id": "aceip0161", "seq": "FDKPVSPL", "length": "8", "detail": "Milk (bovine) | Cereals (Wheat) | Pork | Chicken", "source": "Milk | Cereal | Porcine | Chicken", "ic50": null, "reference": "Angiotensin I-converting enzyme inhibitory peptides generated from in vitro gastrointestinal digestion of pork meat.", "doi": "10.1021\/jf904204n", "pubmedid": "20151679", "mw": "902.05", "pi": "5.84", "charge_ph7": "-0.24", "gravy": "-0.075", "instability": "83.14", "hydrophobic": "0.625", "boman": "-0.98", "helix": "0.25", "turn_pct": "0.5", "sheet": "0.375" }, { "id": "aceip0162", "seq": "FE", "length": "2", "detail": "ND", "source": "ND", "ic50": "0.4 mg\/ml", "reference": "Review on the angiotensin-I-converting enzyme (ACE) inhibitor peptides from marine proteins.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1007\/s12010-012-0024-y; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "23271625 23871047", "mw": "294.3", "pi": "4.6", "charge_ph7": "-1.23", "gravy": "-0.35", "instability": "5.0", "hydrophobic": "0.5", "boman": "-0.67", "helix": "0.5", "turn_pct": "0.0", "sheet": "0.5" }, { "id": "aceip0163", "seq": "FEP", "length": "3", "detail": "Soybean", "source": "Legume", "ic50": "<20 mM", "reference": "Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.", "doi": "10.1021\/jf051263l", "pubmedid": "16448176", "mw": "391.42", "pi": "4.05", "charge_ph7": "-1.24", "gravy": "-0.7667", "instability": "70.87", "hydrophobic": "0.6667", "boman": "-0.4467", "helix": "0.3333", "turn_pct": "0.3333", "sheet": "0.3333" }, { "id": "aceip0164", "seq": "FF", "length": "2", "detail": "Fish", "source": "Fish", "ic50": null, "reference": "Quantitative structure-activity relationship study of bitter di- and tri-peptides including relationship with angiotensin I-converting enzyme inhibitory activity.; Three-dimensional holograph vector of atomic interaction field (3D-HoVAIF): a novel rotation-translation invariant 3D structure descriptor and its applications to peptides.", "doi": "10.1002\/psc.800; 10.1002\/psc.892", "pubmedid": "17117396 17654623", "mw": "312.36", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "2.8", "instability": "5.0", "hydrophobic": "1.0", "boman": "-2.98", "helix": "0.0", "turn_pct": "0.0", "sheet": "1.0" }, { "id": "aceip0165", "seq": "FFF", "length": "3", "detail": "Milk (bovine) | Cereals | Pork | Chicken", "source": "Milk | Cereal | Porcine | Chicken", "ic50": null, "reference": "Quantitative structure-activity relationship study of bitter di- and tri-peptides including relationship with angiotensin I-converting enzyme inhibitory activity.; QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.; What are the ideal properties for functional food peptides with antihypertensive effect? 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A computational peptidology approach.", "doi": "10.1002\/psc.800; 10.1007\/s00894-010-0862-x; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "17117396 20941517 23871047", "mw": "369.41", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "1.7333", "instability": "6.67", "hydrophobic": "0.6667", "boman": "-2.3", "helix": "0.0", "turn_pct": "0.3333", "sheet": "0.6667" }, { "id": "aceip0167", "seq": "FFGRCVSP", "length": "8", "detail": "Chicken", "source": "Chicken", "ic50": "0.4 μM", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1016\/j.foodchem.2012.09.092; 10.1080\/10408398.2012.664829", "pubmedid": "23194537 24915368", "mw": "912.07", "pi": "8.25", "charge_ph7": "0.75", "gravy": "0.625", "instability": "54.25", "hydrophobic": "0.5", "boman": "-1.0825", "helix": "0.0", "turn_pct": "0.375", "sheet": "0.375" }, { "id": "aceip0168", "seq": "FFL", "length": "3", "detail": "Milk (Sheep raw milk cheese (synthesised))", "source": "Milk", "ic50": "<20 mM", "reference": "Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Vegetable foods: a cheap source of proteins and peptides with antihypertensive, antioxidant, and other less occurrence bioactivities.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1021\/jf051263l; 10.1016\/j.talanta.2012.12.041; 10.1080\/10408398.2012.664829", "pubmedid": "16448176 23598136 24915368", "mw": "425.52", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "3.1333", "instability": "6.67", "hydrophobic": "1.0", "boman": "-3.6267", "helix": "0.3333", "turn_pct": "0.0", "sheet": "1.0" }, { "id": "aceip0169", "seq": "FFVAP", "length": "5", "detail": "Milk (bovine) | Cereals | Chicken", "source": "Milk | Cereal | Chicken", "ic50": "6 μM", "reference": "Randomized controlled trial of sour milk on blood pressure in borderline hypertensive men.; Bioactive peptides derived from milk proteins and their health beneficial potentials: an update.; The potential role of milk-derived peptides in cardiovascular disease.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.amjhyper.2004.03.674; 10.1039\/c0fo00016g; 10.1039\/c1fo10017c; 10.1016\/j.foodchem.2012.09.092", "pubmedid": "15288885 21773582 21779574 23194537", "mw": "579.69", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "2.0", "instability": "46.52", "hydrophobic": "1.0", "boman": "-2.362", "helix": "0.2", "turn_pct": "0.2", "sheet": "0.6" }, { "id": "aceip0170", "seq": "FFVAPFEVFGK", "length": "11", "detail": "Chicken", "source": "Chicken", "ic50": "77 μM", "reference": "The potential role of milk-derived peptides in cardiovascular disease.", "doi": "10.1039\/c1fo10017c", "pubmedid": "21779574", "mw": "1287.5", "pi": "6.0", "charge_ph7": "-0.24", "gravy": "1.0909", "instability": "36.39", "hydrophobic": "0.7273", "boman": "-1.7755", "helix": "0.2727", "turn_pct": "0.1818", "sheet": "0.5455" }, { "id": "aceip0171", "seq": "FFVAPFPEVFGK", "length": "12", "detail": "Milk (bovine) | Milk | Cereals | Chicken", "source": "Milk | Cereal | Chicken", "ic50": "18 μM", "reference": "Angiotensin-I-converting enzyme inhibitory peptides from tryptic hydrolysate of bovine alphaS2-casein.; The potential role of milk-derived peptides in cardiovascular disease.; The impact of milk proteins and peptides on blood pressure and vascular function: a review of evidence from human intervention studies.", "doi": "10.1016\/s0014-5793(02)03576-7; 10.1039\/c1fo10017c; 10.1017\/S0954422413000139", "pubmedid": "12417344 21779574 24135454", "mw": "1384.62", "pi": "6.0", "charge_ph7": "-0.24", "gravy": "0.8667", "instability": "64.73", "hydrophobic": "0.75", "boman": "-1.6275", "helix": "0.25", "turn_pct": "0.25", "sheet": "0.5" }, { "id": "aceip0172", "seq": "FFVAPFPGVFGK", "length": "12", "detail": "Milk | Milk-Cheese (Sheep milk and cheeses proteins) | Egg (Ovalbumin)", "source": "Milk | Egg", "ic50": "77 μM", "reference": "Antihypertensive peptides: production, bioavailability and incorporation into foods.; Antihypertensive peptides from food proteins: a review.", "doi": "10.1016\/j.cis.2010.11.001; 10.1039\/c2fo10192k", "pubmedid": "21185549 22249830", "mw": "1312.56", "pi": "8.75", "charge_ph7": "0.76", "gravy": "1.125", "instability": "50.24", "hydrophobic": "0.75", "boman": "-1.8425", "helix": "0.1667", "turn_pct": "0.3333", "sheet": "0.5" }, { "id": "aceip0173", "seq": "FFYY", "length": "4", "detail": "Pork", "source": "Porcine", "ic50": null, "reference": "What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1016\/j.foodchem.2013.05.140", "pubmedid": "23871047", "mw": "638.71", "pi": "5.52", "charge_ph7": "-0.24", "gravy": "0.75", "instability": "119.85", "hydrophobic": "0.5", "boman": "-1.42", "helix": "0.0", "turn_pct": "0.0", "sheet": "1.0" }, { "id": "aceip0174", "seq": "FG", "length": "2", "detail": "Milk", "source": "Milk", "ic50": "<20 mM", "reference": "Binding of peptide substrates and inhibitors of angiotensin-converting enzyme. Importance of the COOH-terminal dipeptide sequence.; Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Quantitative structure-activity relationship study of bitter di- and tri-peptides including relationship with angiotensin I-converting enzyme inhibitory activity.; Three-dimensional holograph vector of atomic interaction field (3D-HoVAIF): a novel rotation-translation invariant 3D structure descriptor and its applications to peptides.; Model of the exofacial substrate-binding site and helical folding of the human Glut1 glucose transporter based on scanning mutagenesis.; QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.; Peptides with angiotensin I converting enzyme (ACE) inhibitory activity generated from porcine skeletal muscle proteins by the action of meat-borne Lactobacillus.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1021\/jf051263l; 10.1002\/psc.800; 10.1002\/psc.892; 10.1021\/bi900521n; 10.1007\/s00894-010-0862-x; 10.1016\/j.jprot.2013.06.023; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "6243277 16448176 17117396 17654623 19449892 20941517 23806758 23871047", "mw": "222.24", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "1.2", "instability": "5.0", "hydrophobic": "0.5", "boman": "-1.96", "helix": "0.0", "turn_pct": "0.5", "sheet": "0.5" }, { "id": "aceip0175", "seq": "FGASTRGA", "length": "8", "detail": "Milk (bovine)", "source": "Milk", "ic50": "14.7 μM", "reference": "A novel angiotensin I converting enzyme inhibitory peptide from Alaska pollack (Theragra chalcogramma) frame protein hydrolysate.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1021\/jf0494027; 10.1016\/j.foodchem.2012.09.092", "pubmedid": "15612765 23194537", "mw": "765.81", "pi": "9.75", "charge_ph7": "0.76", "gravy": "-0.05", "instability": "-23.09", "hydrophobic": "0.375", "boman": "-0.5825", "helix": "0.25", "turn_pct": "0.375", "sheet": "0.25" }, { "id": "aceip0176", "seq": "FGF", "length": "3", "detail": "Milk (bovine) | Milk (Goat milk protein)", "source": "Milk", "ic50": null, "reference": "Quantitative structure-activity relationship study of bitter di- and tri-peptides including relationship with angiotensin I-converting enzyme inhibitory activity.; QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.; What are the ideal properties for functional food peptides with antihypertensive effect? 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A computational peptidology approach.", "doi": "10.1271\/bbb.60.661; 10.1021\/jf072911z; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "8829536 18211015 23871047", "mw": "407.42", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "-1.4", "instability": "-18.47", "hydrophobic": "0.3333", "boman": "0.0", "helix": "0.0", "turn_pct": "0.3333", "sheet": "0.3333" }, { "id": "aceip0192", "seq": "FP", "length": "2", "detail": "Milk", "source": "Milk", "ic50": "<20 mM", "reference": "Structural analysis of new antihypertensive peptides derived from cheese whey protein by proteinase K digestion.; Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Quantitative structure-activity relationship study of bitter di- and tri-peptides including relationship with angiotensin I-converting enzyme inhibitory activity.; Three-dimensional holograph vector of atomic interaction field (3D-HoVAIF): a novel rotation-translation invariant 3D structure descriptor and its applications to peptides.; Bioactive peptides in amaranth (Amaranthus hypochondriacus) seed.; Antihypertensive peptides from food proteins: a review.; What are the ideal properties for functional food peptides with antihypertensive effect? 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A computational peptidology approach.", "doi": "10.1002\/psc.800; 10.1007\/s00894-010-0862-x; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "17117396 20941517 23871047", "mw": "359.42", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "-0.1333", "instability": "135.07", "hydrophobic": "1.0", "boman": "-0.9933", "helix": "0.0", "turn_pct": "0.6667", "sheet": "0.3333" }, { "id": "aceip0197", "seq": "FPQYLQY", "length": "7", "detail": "Milk (bovine) | Milk | Cereals | Pork | Chicken", "source": "Milk | Cereal | Porcine | Chicken", "ic50": "14 μM", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "23194537", "mw": "958.07", "pi": "5.52", "charge_ph7": "-0.24", "gravy": "-0.6571", "instability": "88.63", "hydrophobic": "0.4286", "boman": "-0.7", "helix": "0.1429", "turn_pct": "0.1429", "sheet": "0.5714" }, { "id": "aceip0198", "seq": "FQ", "length": "2", "detail": "Cheese (Fresco)", "source": "Milk", "ic50": "<20 mM", "reference": "Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.", "doi": "10.1021\/jf051263l", "pubmedid": "16448176", "mw": "293.32", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "-0.35", "instability": "5.0", "hydrophobic": "0.5", "boman": "-0.81", "helix": "0.0", "turn_pct": "0.0", "sheet": "0.5" }, { "id": "aceip0199", "seq": "FQKPKR", "length": "6", "detail": "Milk (human)", "source": "Milk", "ic50": "0.32-14 μM", "reference": "Angiotensin I-converting enzyme-inhibitory peptides obtained from chicken collagen hydrolysate.; Temporal gene expression and probiotic attributes of Lactobacillus acidophilus during growth in milk.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1021\/jf072669w; 10.3168\/jds.2008-1457; 10.1016\/j.foodchem.2012.09.092; 10.1080\/10408398.2012.664829", "pubmedid": "18808143 19233780 23194537 24915368", "mw": "802.96", "pi": "11.17", "charge_ph7": "2.76", "gravy": "-2.4333", "instability": "50.1", "hydrophobic": "0.3333", "boman": "0.71", "helix": "0.3333", "turn_pct": "0.1667", "sheet": "0.1667" }, { "id": "aceip0200", "seq": "FQKVVA", "length": "6", "detail": "Blue mussel", "source": "Animal", "ic50": "5.8 μM", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "23194537", "mw": "690.83", "pi": "8.75", "charge_ph7": "0.76", "gravy": "0.9333", "instability": "-5.82", "hydrophobic": "0.6667", "boman": "-1.655", "helix": "0.3333", "turn_pct": "0.0", "sheet": "0.5" }, { "id": "aceip0201", "seq": "FQKVVAG", "length": "7", "detail": "ND", "source": "ND", "ic50": "7.4 μM", "reference": "Antihypertensive effect of angiotensin I-converting enzyme inhibitory peptides derived from hemoglobin.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/0014-2999(96)00146-x; 10.1016\/j.foodchem.2012.09.092", "pubmedid": "8813589 23194537", "mw": "747.88", "pi": "8.75", "charge_ph7": "0.76", "gravy": "0.7429", "instability": "-3.56", "hydrophobic": "0.5714", "boman": "-1.5529", "helix": "0.2857", "turn_pct": "0.1429", "sheet": "0.4286" }, { "id": "aceip0202", "seq": "FQKVVAK", "length": "7", "detail": "Sweet-potato", "source": "Potato", "ic50": "2.1 μM", "reference": "Antihypertensive effect of angiotensin I-converting enzyme inhibitory peptides derived from hemoglobin.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/0014-2999(96)00146-x; 10.1016\/j.foodchem.2012.09.092", "pubmedid": "8813589 23194537", "mw": "819.0", "pi": "10.0", "charge_ph7": "1.76", "gravy": "0.2429", "instability": "-3.56", "hydrophobic": "0.5714", "boman": "-1.1929", "helix": "0.4286", "turn_pct": "0.0", "sheet": "0.4286" }, { "id": "aceip0203", "seq": "FQP", "length": "3", "detail": "Milk (bovine) | Milk | Cereals | Chicken", "source": "Milk | Cereal | Chicken", "ic50": "0 μM", "reference": "Peptide inhibitors for angiotensin I-converting enzyme from thermolysin digest of dried bonito.; Bioactive peptides in amaranth (Amaranthus hypochondriacus) seed.; Rational design of angiotensin-I-converting enzyme inhibitory peptides by integrating in silico modeling and an in vitro assay.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1271\/bbb.56.1541; 10.1021\/jf072911z; 10.1002\/cmdc.201300132; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "1369054 18211015 23740817 23871047", "mw": "390.43", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "-0.7667", "instability": "70.87", "hydrophobic": "0.6667", "boman": "-0.54", "helix": "0.0", "turn_pct": "0.3333", "sheet": "0.3333" }, { "id": "aceip0204", "seq": "FQPQPLIYP", "length": "9", "detail": "ND", "source": "ND", "ic50": "1.8 μM", "reference": "Inhibition of angiotensin-converting enzyme by synthetic peptide fragments of various beta-caseins.", "doi": "", "pubmedid": "1368548", "mw": "1102.28", "pi": "5.52", "charge_ph7": "-0.24", "gravy": "-0.2222", "instability": "86.8", "hydrophobic": "0.6667", "boman": "-1.1067", "helix": "0.1111", "turn_pct": "0.3333", "sheet": "0.4444" }, { "id": "aceip0205", "seq": "FR", "length": "2", "detail": "Milk (bovine) | Fish (Shark) | Cereals | Chicken", "source": "Milk | Fish | Cereal | Chicken", "ic50": "920 μM", "reference": "Three-dimensional holograph vector of atomic interaction field (3D-HoVAIF): a novel rotation-translation invariant 3D structure descriptor and its applications to peptides.; QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1002\/psc.892; 10.1007\/s00894-010-0862-x; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "17654623 20941517 23871047", "mw": "321.37", "pi": "9.75", "charge_ph7": "0.76", "gravy": "-0.85", "instability": "5.0", "hydrophobic": "0.5", "boman": "-0.13", "helix": "0.0", "turn_pct": "0.0", "sheet": "0.5" }, { "id": "aceip0206", "seq": "FRADHPFL", "length": "8", "detail": "Milk (bovine) | Cereals | Algae (Chlorella vulgaris) | Microalgae", "source": "Milk | Cereal | Bacteria", "ic50": "3.2 μM", "reference": "Antihypertensive peptides: production, bioavailability and incorporation into foods.; Antihypertensive peptides from food proteins: a review.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.cis.2010.11.001; 10.1039\/c2fo10192k; 10.1016\/j.foodchem.2012.09.092", "pubmedid": "21185549 22249830 23194537", "mw": "1002.13", "pi": "6.74", "charge_ph7": "-0.15", "gravy": "-0.2", "instability": "18.61", "hydrophobic": "0.625", "boman": "-0.9125", "helix": "0.25", "turn_pct": "0.25", "sheet": "0.375" }, { "id": "aceip0207", "seq": "FRADHPPL", "length": "8", "detail": "Fungi (Agaricus bisporus)", "source": "Fungi", "ic50": null, "reference": "Antihypertensive peptides derived from egg proteins.", "doi": "10.1093\/jn\/136.6.1457", "pubmedid": "16702303", "mw": "952.07", "pi": "6.74", "charge_ph7": "-0.15", "gravy": "-0.75", "instability": "18.61", "hydrophobic": "0.625", "boman": "-0.54", "helix": "0.25", "turn_pct": "0.375", "sheet": "0.25" }, { "id": "aceip0208", "seq": "FRQF", "length": "4", "detail": "Milk (bovine)", "source": "Milk", "ic50": null, "reference": "Enterococcus faecalis strains from food, environmental, and clinical origin produce ACE-inhibitory peptides and other bioactive peptides during growth in bovine skim milk.", "doi": "10.1016\/j.ijfoodmicro.2013.06.019", "pubmedid": "23845432", "mw": "596.68", "pi": "9.75", "charge_ph7": "0.76", "gravy": "-0.6", "instability": "36.8", "hydrophobic": "0.5", "boman": "-0.47", "helix": "0.0", "turn_pct": "0.0", "sheet": "0.5" }, { "id": "aceip0209", "seq": "FRVPTPN", "length": "7", "detail": "Milk (bovine) | Casein", "source": "Milk", "ic50": "9.55 μM", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "23194537", "mw": "829.94", "pi": "9.75", "charge_ph7": "0.76", "gravy": "-0.7", "instability": "36.09", "hydrophobic": "0.5714", "boman": "-0.3457", "helix": "0.0", "turn_pct": "0.4286", "sheet": "0.4286" }, { "id": "aceip0210", "seq": "FSQ", "length": "3", "detail": "Milk (bovine) | Casein | Cereals", "source": "Milk | Cereal", "ic50": null, "reference": "Isolation from alpha-zein of thermolysin peptides with angiotensin I-converting enzyme inhibitory activity.", "doi": "10.1271\/bbb.60.661", "pubmedid": "8829536", "mw": "380.4", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "-0.5", "instability": "70.87", "hydrophobic": "0.3333", "boman": "-0.26", "helix": "0.0", "turn_pct": "0.3333", "sheet": "0.3333" }, { "id": "aceip0211", "seq": "FTESQS", "length": "6", "detail": "Milk (bovine)", "source": "Milk", "ic50": null, "reference": "Enterococcus faecalis strains from food, environmental, and clinical origin produce ACE-inhibitory peptides and other bioactive peptides during growth in bovine skim milk.", "doi": "10.1016\/j.ijfoodmicro.2013.06.019", "pubmedid": "23845432", "mw": "697.69", "pi": "4.05", "charge_ph7": "-1.24", "gravy": "-1.0833", "instability": "177.87", "hydrophobic": "0.1667", "boman": "0.3267", "helix": "0.1667", "turn_pct": "0.3333", "sheet": "0.3333" }, { "id": "aceip0212", "seq": "FV", "length": "2", "detail": "Milk (bovine, buffalo and ovine)", "source": "Milk", "ic50": null, "reference": "Quantitative structure-activity relationship study of bitter di- and tri-peptides including relationship with angiotensin I-converting enzyme inhibitory activity.", "doi": "10.1002\/psc.800", "pubmedid": "17117396", "mw": "264.32", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "3.5", "instability": "5.0", "hydrophobic": "1.0", "boman": "-3.51", "helix": "0.0", "turn_pct": "0.0", "sheet": "1.0" }, { "id": "aceip0213", "seq": "FVAP", "length": "4", "detail": "ND", "source": "ND", "ic50": "10 μM", "reference": "What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1016\/j.foodchem.2013.05.140", "pubmedid": "23871047", "mw": "432.51", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "1.8", "instability": "55.65", "hydrophobic": "1.0", "boman": "-2.2075", "helix": "0.25", "turn_pct": "0.25", "sheet": "0.5" }, { "id": "aceip0214", "seq": "FVAPFP", "length": "6", "detail": "Egg (Ovalbumin)", "source": "Egg", "ic50": null, "reference": "Enterococcus faecalis strains from food, environmental, and clinical origin produce ACE-inhibitory peptides and other bioactive peptides during growth in bovine skim milk.", "doi": "10.1016\/j.ijfoodmicro.2013.06.019", "pubmedid": "23845432", "mw": "676.8", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "1.4", "instability": "104.63", "hydrophobic": "1.0", "boman": "-1.9683", "helix": "0.1667", "turn_pct": "0.3333", "sheet": "0.5" }, { "id": "aceip0215", "seq": "FVAPFPEV", "length": "8", "detail": "Shrimp", "source": "Shrimp", "ic50": "475.89 ± 41.73 μM", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "23194537", "mw": "905.05", "pi": "4.05", "charge_ph7": "-1.24", "gravy": "1.1375", "instability": "102.7", "hydrophobic": "0.875", "boman": "-1.7763", "helix": "0.25", "turn_pct": "0.25", "sheet": "0.5" }, { "id": "aceip0216", "seq": "FVAPFPEVFGKEKVNELSKDIGS", "length": "23", "detail": "ND", "source": "ND", "ic50": null, "reference": "Identification of angiotensin-I-converting enzyme inhibitory peptides derived from sodium caseinate hydrolysates produced by Lactobacillus helveticus NCC 2765.", "doi": "10.1021\/jf049510t", "pubmedid": "15537298", "mw": "2537.86", "pi": "4.87", "charge_ph7": "-1.23", "gravy": "-0.1609", "instability": "34.86", "hydrophobic": "0.4783", "boman": "-0.8674", "helix": "0.3478", "turn_pct": "0.3478", "sheet": "0.3478" }, { "id": "aceip0217", "seq": "FVAPFPEVFGKEKVNELSKDIGSE", "length": "24", "detail": "Milk (caprine)", "source": "Milk", "ic50": null, "reference": "Angiotensin I-converting-enzyme-inhibitory and antibacterial peptides from Lactobacillus helveticus PR4 proteinase-hydrolyzed caseins of milk from six species.", "doi": "10.1128\/AEM.69.9.5297-5305.2003", "pubmedid": "12957917", "mw": "2666.97", "pi": "4.75", "charge_ph7": "-2.23", "gravy": "-0.3", "instability": "41.85", "hydrophobic": "0.4583", "boman": "-0.7629", "helix": "0.375", "turn_pct": "0.3333", "sheet": "0.3333" }, { "id": "aceip0218", "seq": "FVEPIP", "length": "6", "detail": "Pork", "source": "Porcine", "ic50": ">1000 μM", "reference": "Inhibition of angiotensin-converting enzyme by synthetic peptide fragments of various beta-caseins.", "doi": "", "pubmedid": "1368548", "mw": "700.82", "pi": "4.05", "charge_ph7": "-1.24", "gravy": "0.8", "instability": "35.63", "hydrophobic": "0.8333", "boman": "-1.7167", "helix": "0.1667", "turn_pct": "0.3333", "sheet": "0.5" }, { "id": "aceip0219", "seq": "FVNPQAGS", "length": "8", "detail": "Fish (Shark)", "source": "Fish", "ic50": "6.9 μM", "reference": "Purification of an ACE inhibitory peptide after hydrolysis of sunflower (Helianthus annuus L.) protein isolates.; Vegetable foods: a cheap source of proteins and peptides with antihypertensive, antioxidant, and other less occurrence bioactivities.", "doi": "10.1021\/jf034707r; 10.1016\/j.talanta.2012.12.041", "pubmedid": "15053531 23598136", "mw": "818.87", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "-0.125", "instability": "29.23", "hydrophobic": "0.5", "boman": "-0.7437", "helix": "0.125", "turn_pct": "0.5", "sheet": "0.25" }, { "id": "aceip0220", "seq": "FWN", "length": "3", "detail": "Salmon", "source": "Fish", "ic50": "18.3 μM", "reference": "Structure and activity of angiotensin I converting enzyme inhibitory peptides from sake and sake lees.; Vegetable foods: a cheap source of proteins and peptides with antihypertensive, antioxidant, and other less occurrence bioactivities.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1271\/bbb.58.1767; 10.1016\/j.talanta.2012.12.041; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "7765503 23598136 23871047", "mw": "465.5", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "-0.5333", "instability": "47.8", "hydrophobic": "0.6667", "boman": "-1.23", "helix": "0.0", "turn_pct": "0.3333", "sheet": "0.6667" }, { "id": "aceip0221", "seq": "FY", "length": "2", "detail": "ND", "source": "ND", "ic50": "<20 mM", "reference": "Structures and activity of angiotensin-converting enzyme inhibitors in an alpha-zein hydrolysate.; Isolation from alpha-zein of thermolysin peptides with angiotensin I-converting enzyme inhibitory activity.; Antihypertensive effects of Undaria pinnatifida (wakame) peptide on blood pressure in spontaneously hypertensive rats.; Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Three-dimensional holograph vector of atomic interaction field (3D-HoVAIF): a novel rotation-translation invariant 3D structure descriptor and its applications to peptides.; Max-E47, a designed minimalist protein that targets the E-box DNA site in vivo and in vitro.; Cellular membrane disruption by amyloid fibrils involved intermolecular disulfide cross-linking.; Antihypertensive peptides from food proteins: a review.; Vegetable foods: a cheap source of proteins and peptides with antihypertensive, antioxidant, and other less occurrence bioactivities.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1271\/bbb.60.661; 10.1016\/j.jnutbio.2003.11.004; 10.1021\/jf051263l; 10.1002\/psc.892; 10.1021\/ja901306q; 10.1021\/bi900219c; 10.1039\/c2fo10192k; 10.1016\/j.talanta.2012.12.041; 10.1016\/j.foodchem.2013.05.140; 10.1080\/10408398.2012.664829", "pubmedid": "1368684 8829536 15135150 16448176 17654623 19449889 19449893 22249830 23598136 23871047 24915368", "mw": "328.36", "pi": "5.52", "charge_ph7": "-0.24", "gravy": "0.75", "instability": "168.0", "hydrophobic": "0.5", "boman": "-1.42", "helix": "0.0", "turn_pct": "0.0", "sheet": "1.0" }, { "id": "aceip0222", "seq": "FYN", "length": "3", "detail": "Previously publish reports", "source": "ND", "ic50": "<20 mM", "reference": "Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.", "doi": "10.1021\/jf051263l", "pubmedid": "16448176", "mw": "442.46", "pi": "5.52", "charge_ph7": "-0.24", "gravy": "-0.6667", "instability": "115.34", "hydrophobic": "0.3333", "boman": "-0.4067", "helix": "0.0", "turn_pct": "0.3333", "sheet": "0.6667" }, { "id": "aceip0223", "seq": "FYQLDA", "length": "6", "detail": "ND", "source": "ND", "ic50": null, "reference": "Hot topic: Changes in angiotensin-converting enzyme inhibition and concentrations of the tripeptides Val-Pro-Pro and Ile-Pro-Pro during ripening of different Swiss cheese varieties.", "doi": "10.3168\/jds.2008-1531", "pubmedid": "19233775", "mw": "755.81", "pi": "4.05", "charge_ph7": "-1.24", "gravy": "0.0167", "instability": "62.67", "hydrophobic": "0.5", "boman": "-1.0883", "helix": "0.3333", "turn_pct": "0.1667", "sheet": "0.5" }, { "id": "aceip0224", "seq": "FYQQ", "length": "4", "detail": "ND", "source": "ND", "ic50": "25 μM", "reference": "Isolation from alpha-zein of thermolysin peptides with angiotensin I-converting enzyme inhibitory activity.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1271\/bbb.60.661; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "8829536 23871047", "mw": "584.62", "pi": "5.52", "charge_ph7": "-0.24", "gravy": "-1.375", "instability": "137.15", "hydrophobic": "0.25", "boman": "-0.03", "helix": "0.0", "turn_pct": "0.0", "sheet": "0.5" }, { "id": "aceip0225", "seq": "GA", "length": "2", "detail": "Egg (Ovalbumin)", "source": "Egg", "ic50": "<20 mM", "reference": "Binding of peptide substrates and inhibitors of angiotensin-converting enzyme. Importance of the COOH-terminal dipeptide sequence.; Three-dimensional holograph vector of atomic interaction field (3D-HoVAIF): a novel rotation-translation invariant 3D structure descriptor and its applications to peptides.; QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.; Peptides with angiotensin I converting enzyme (ACE) inhibitory activity generated from porcine skeletal muscle proteins by the action of meat-borne Lactobacillus.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1002\/psc.892; 10.1007\/s00894-010-0862-x; 10.1016\/j.jprot.2013.06.023; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "6243277 17654623 20941517 23806758 23871047", "mw": "146.14", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "0.7", "instability": "-37.45", "hydrophobic": "0.5", "boman": "-1.375", "helix": "0.5", "turn_pct": "0.5", "sheet": "0.0" }, { "id": "aceip0226", "seq": "GAAELPCSADWW", "length": "12", "detail": "Egg (Ovalbumin)", "source": "Egg", "ic50": "0.95 μM", "reference": "Antihypertensive peptides from food proteins: a review.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1039\/c2fo10192k; 10.1016\/j.foodchem.2012.09.092; 10.1080\/10408398.2012.664829", "pubmedid": "22249830 23194537 24915368", "mw": "1305.41", "pi": "4.05", "charge_ph7": "-2.25", "gravy": "0.0083", "instability": "4.78", "hydrophobic": "0.5833", "boman": "-1.0892", "helix": "0.4167", "turn_pct": "0.3333", "sheet": "0.25" }, { "id": "aceip0227", "seq": "GAP", "length": "3", "detail": "Cereals | Soybean", "source": "Cereal | Legume", "ic50": "9.3 μM", "reference": "Rational design of angiotensin-I-converting enzyme inhibitory peptides by integrating in silico modeling and an in vitro assay.", "doi": "10.1002\/cmdc.201300132", "pubmedid": "23740817", "mw": "243.26", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "-0.0667", "instability": "42.57", "hydrophobic": "0.6667", "boman": "-0.9167", "helix": "0.3333", "turn_pct": "0.6667", "sheet": "0.0" }, { "id": "aceip0228", "seq": "GAPGLPGP", "length": "8", "detail": "Milk (bovine) | Milk (human)", "source": "Milk", "ic50": "29.4 μM", "reference": "Angiotensin I-converting enzyme-inhibitory peptides obtained from chicken collagen hydrolysate.", "doi": "10.1021\/jf072669w", "pubmedid": "18808143", "mw": "664.75", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "-0.05", "instability": "46.29", "hydrophobic": "0.625", "boman": "-1.1937", "helix": "0.25", "turn_pct": "0.75", "sheet": "0.125" }, { "id": "aceip0229", "seq": "GAPGPAGPGGIPGERG", "length": "16", "detail": "Casein", "source": "Milk", "ic50": "45.6 μM", "reference": "Angiotensin I-converting enzyme-inhibitory peptides obtained from chicken collagen hydrolysate.", "doi": "10.1021\/jf072669w", "pubmedid": "18808143", "mw": "1346.45", "pi": "6.0", "charge_ph7": "-0.24", "gravy": "-0.5687", "instability": "18.73", "hydrophobic": "0.4375", "boman": "-0.6725", "helix": "0.1875", "turn_pct": "0.6875", "sheet": "0.0625" }, { "id": "aceip0230", "seq": "GAVGPSG", "length": "7", "detail": "Milk (bovine) | Casein | Milk (Goat milk protein)", "source": "Milk", "ic50": null, "reference": "Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1080\/10408398.2012.664829", "pubmedid": "24915368", "mw": "543.57", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "0.3429", "instability": "11.83", "hydrophobic": "0.4286", "boman": "-1.1186", "helix": "0.1429", "turn_pct": "0.7143", "sheet": "0.1429" }, { "id": "aceip0231", "seq": "GD", "length": "2", "detail": "Casein", "source": "Milk", "ic50": "<20 mM", "reference": "Binding of peptide substrates and inhibitors of angiotensin-converting enzyme. Importance of the COOH-terminal dipeptide sequence.; Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Three-dimensional holograph vector of atomic interaction field (3D-HoVAIF): a novel rotation-translation invariant 3D structure descriptor and its applications to peptides.; QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.; Peptides with angiotensin I converting enzyme (ACE) inhibitory activity generated from porcine skeletal muscle proteins by the action of meat-borne Lactobacillus.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1021\/jf051263l; 10.1002\/psc.892; 10.1007\/s00894-010-0862-x; 10.1016\/j.jprot.2013.06.023; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "6243277 16448176 17654623 20941517 23806758 23871047", "mw": "190.15", "pi": "4.3", "charge_ph7": "-1.24", "gravy": "-1.95", "instability": "5.0", "hydrophobic": "0.0", "boman": "0.37", "helix": "0.0", "turn_pct": "1.0", "sheet": "0.0" }, { "id": "aceip0232", "seq": "GDAP", "length": "4", "detail": "Milk | Hydrolysis", "source": "Milk | Synthesized", "ic50": "11.6 μM\/L", "reference": "Analysis of novel angiotensin I-converting enzyme inhibitory peptides from enzymatic hydrolysates of cuttlefish (Sepia officinalis) muscle proteins.; Review on the angiotensin-I-converting enzyme (ACE) inhibitor peptides from marine proteins.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1021\/jf904300q; 10.1007\/s12010-012-0024-y; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "20180574 23271625 23871047", "mw": "358.35", "pi": "4.05", "charge_ph7": "-1.24", "gravy": "-0.925", "instability": "55.65", "hydrophobic": "0.5", "boman": "-0.2675", "helix": "0.25", "turn_pct": "0.75", "sheet": "0.0" }, { "id": "aceip0233", "seq": "GDLGKTTTVSNWSPPKYKDTP", "length": "21", "detail": "Casein", "source": "Milk", "ic50": "11.28 μM", "reference": "Antihypertensive peptides from food proteins: a review.; Review on the angiotensin-I-converting enzyme (ACE) inhibitor peptides from marine proteins.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1039\/c2fo10192k; 10.1007\/s12010-012-0024-y; 10.1080\/10408398.2012.664829", "pubmedid": "22249830 23271625 24915368", "mw": "2292.5", "pi": "8.43", "charge_ph7": "0.76", "gravy": "-1.2571", "instability": "23.48", "hydrophobic": "0.2857", "boman": "-0.0281", "helix": "0.1905", "turn_pct": "0.4762", "sheet": "0.381" }, { "id": "aceip0234", "seq": "GE", "length": "2", "detail": "ND", "source": "ND", "ic50": "<20 mM", "reference": "Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Three-dimensional holograph vector of atomic interaction field (3D-HoVAIF): a novel rotation-translation invariant 3D structure descriptor and its applications to peptides.; QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.; Peptides with angiotensin I converting enzyme (ACE) inhibitory activity generated from porcine skeletal muscle proteins by the action of meat-borne Lactobacillus.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1021\/jf051263l; 10.1002\/psc.892; 10.1007\/s00894-010-0862-x; 10.1016\/j.jprot.2013.06.023; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "16448176 17654623 20941517 23806758 23871047", "mw": "204.18", "pi": "4.6", "charge_ph7": "-1.23", "gravy": "-1.95", "instability": "-32.7", "hydrophobic": "0.0", "boman": "0.35", "helix": "0.5", "turn_pct": "0.5", "sheet": "0.0" }, { "id": "aceip0235", "seq": "GEG", "length": "3", "detail": "Milk (bovine) | Cereals | pea | Pork | Chicken", "source": "Milk | Cereal | Legume | Porcine | Chicken", "ic50": null, "reference": "QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1007\/s00894-010-0862-x; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "20941517 23871047", "mw": "261.23", "pi": "4.05", "charge_ph7": "-1.24", "gravy": "-1.4333", "instability": "-18.47", "hydrophobic": "0.0", "boman": "-0.08", "helix": "0.3333", "turn_pct": "0.6667", "sheet": "0.0" }, { "id": "aceip0236", "seq": "GEGGP", "length": "5", "detail": "Bulfrog | Fish (Alaska pollack)", "source": "Amphibian | Fish", "ic50": "0.044 mg\/ml", "reference": "Characterization of an antihypertensive angiotensin I-converting enzyme inhibitory peptide from the edible mushroom Hypsizygus marmoreus.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1155\/2013\/283964; 10.1080\/10408398.2012.664829", "pubmedid": "24380081 24915368", "mw": "415.4", "pi": "4.05", "charge_ph7": "-1.24", "gravy": "-1.26", "instability": "17.6", "hydrophobic": "0.2", "boman": "-0.236", "helix": "0.2", "turn_pct": "0.8", "sheet": "0.0" }, { "id": "aceip0237", "seq": "GEP", "length": "3", "detail": "ND", "source": "ND", "ic50": "<10 μM", "reference": "Isolation and characterization of a novel angiotensin I-converting enzyme inhibitory peptide derived from the edible mushroom Tricholoma giganteum.; Angiotensin converting enzyme inhibitory peptides derived from food proteins: biochemistry, bioactivity and production.; Langmuir monolayers of a hydrogenated\/fluorinated catanionic surfactant: from the macroscopic to the nanoscopic size scale.; Vegetable foods: a cheap source of proteins and peptides with antihypertensive, antioxidant, and other less occurrence bioactivities.; Novel angiotensin I-converting enzyme inhibitory peptides derived from an edible mushroom, Pleurotus cystidiosus O.K. Miller identified by LC-MS\/MS.; Characterization of an antihypertensive angiotensin I-converting enzyme inhibitory peptide from the edible mushroom Hypsizygus marmoreus.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1016\/j.peptides.2004.01.015; 10.2174\/138161207780363068; 10.1021\/la900593c; 10.1016\/j.talanta.2012.12.041; 10.1186\/1472-6882-13-313; 10.1155\/2013\/283964; 10.1080\/10408398.2012.664829", "pubmedid": "15165718 17430180 19449890 23598136 24215325 24380081 24915368", "mw": "301.3", "pi": "4.05", "charge_ph7": "-1.24", "gravy": "-1.8333", "instability": "45.73", "hydrophobic": "0.3333", "boman": "0.2333", "helix": "0.3333", "turn_pct": "0.6667", "sheet": "0.0" }, { "id": "aceip0238", "seq": "GF", "length": "2", "detail": "Fish (Cuttlefish)", "source": "Fish", "ic50": "<20 mM", "reference": "Binding of peptide substrates and inhibitors of angiotensin-converting enzyme. Importance of the COOH-terminal dipeptide sequence.; Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Quantitative structure-activity relationship study of bitter di- and tri-peptides including relationship with angiotensin I-converting enzyme inhibitory activity.; Three-dimensional holograph vector of atomic interaction field (3D-HoVAIF): a novel rotation-translation invariant 3D structure descriptor and its applications to peptides.; QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.; Antihypertensive peptides from food proteins: a review.; Review on the angiotensin-I-converting enzyme (ACE) inhibitor peptides from marine proteins.; Peptides with angiotensin I converting enzyme (ACE) inhibitory activity generated from porcine skeletal muscle proteins by the action of meat-borne Lactobacillus.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1021\/jf051263l; 10.1002\/psc.800; 10.1002\/psc.892; 10.1007\/s00894-010-0862-x; 10.1039\/c2fo10192k; 10.1007\/s12010-012-0024-y; 10.1016\/j.jprot.2013.06.023; 10.1016\/j.foodchem.2013.05.140; 10.1080\/10408398.2012.664829", "pubmedid": "6243277 16448176 17117396 17654623 20941517 22249830 23271625 23806758 23871047 24915368", "mw": "222.24", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "1.2", "instability": "5.0", "hydrophobic": "0.5", "boman": "-1.96", "helix": "0.0", "turn_pct": "0.5", "sheet": "0.5" }, { "id": "aceip0239", "seq": "GFF", "length": "3", "detail": "Nomura Jellyfish", "source": "Animal", "ic50": null, "reference": "Quantitative structure-activity relationship study of bitter di- and tri-peptides including relationship with angiotensin I-converting enzyme inhibitory activity.; QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1002\/psc.800; 10.1007\/s00894-010-0862-x; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "17117396 20941517 23871047", "mw": "369.41", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "1.7333", "instability": "6.67", "hydrophobic": "0.6667", "boman": "-2.3", "helix": "0.0", "turn_pct": "0.3333", "sheet": "0.6667" }, { "id": "aceip0240", "seq": "GFG", "length": "3", "detail": "Milk (bovine) | Casein | Milk (Digested milk products)", "source": "Milk", "ic50": null, "reference": "Quantitative structure-activity relationship study of bitter di- and tri-peptides including relationship with angiotensin I-converting enzyme inhibitory activity.; QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1002\/psc.800; 10.1007\/s00894-010-0862-x; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "17117396 20941517 23871047", "mw": "279.29", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "0.6667", "instability": "6.67", "hydrophobic": "0.3333", "boman": "-1.62", "helix": "0.0", "turn_pct": "0.6667", "sheet": "0.3333" }, { "id": "aceip0241", "seq": "GFHI", "length": "4", "detail": "Egg (Ovalbumin)", "source": "Egg", "ic50": "64.0 mg\/ml", "reference": "Antihypertensive peptides: production, bioavailability and incorporation into foods.", "doi": "10.1016\/j.cis.2010.11.001", "pubmedid": "21185549", "mw": "472.54", "pi": "6.74", "charge_ph7": "-0.15", "gravy": "0.925", "instability": "117.35", "hydrophobic": "0.5", "boman": "-1.9625", "helix": "0.0", "turn_pct": "0.25", "sheet": "0.5" }, { "id": "aceip0242", "seq": "GFPGTPGLPGF", "length": "11", "detail": "Bonito", "source": "Fish", "ic50": "436 μM", "reference": "Angiotensin I-converting enzyme inhibitory peptides in a hydrolyzed chicken breast muscle extract.", "doi": "10.1021\/jf020604h", "pubmedid": "12617616", "mw": "1046.18", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "0.2091", "instability": "36.39", "hydrophobic": "0.5455", "boman": "-1.3073", "helix": "0.0909", "turn_pct": "0.6364", "sheet": "0.3636" }, { "id": "aceip0243", "seq": "GG", "length": "2", "detail": "Synthesized | Bovine", "source": "Synthesized | Bovine", "ic50": "<20 mM", "reference": "Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Three-dimensional holograph vector of atomic interaction field (3D-HoVAIF): a novel rotation-translation invariant 3D structure descriptor and its applications to peptides.; QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.; Peptides with angiotensin I converting enzyme (ACE) inhibitory activity generated from porcine skeletal muscle proteins by the action of meat-borne Lactobacillus.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1021\/jf051263l; 10.1002\/psc.892; 10.1007\/s00894-010-0862-x; 10.1016\/j.jprot.2013.06.023; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "16448176 17654623 20941517 23806758 23871047", "mw": "132.12", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "-0.4", "instability": "66.7", "hydrophobic": "0.0", "boman": "-0.94", "helix": "0.0", "turn_pct": "1.0", "sheet": "0.0" }, { "id": "aceip0244", "seq": "GGF", "length": "3", "detail": "Soybean Sauce", "source": "Legume", "ic50": null, "reference": "Quantitative structure-activity relationship study of bitter di- and tri-peptides including relationship with angiotensin I-converting enzyme inhibitory activity.; QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1002\/psc.800; 10.1007\/s00894-010-0862-x; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "17117396 20941517 23871047", "mw": "279.29", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "0.6667", "instability": "47.8", "hydrophobic": "0.3333", "boman": "-1.62", "helix": "0.0", "turn_pct": "0.6667", "sheet": "0.3333" }, { "id": "aceip0245", "seq": "GGG", "length": "3", "detail": "ND", "source": "ND", "ic50": null, "reference": "Quantitative structure-activity relationship study of bitter di- and tri-peptides including relationship with angiotensin I-converting enzyme inhibitory activity.; QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1002\/psc.800; 10.1007\/s00894-010-0862-x; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "17117396 20941517 23871047", "mw": "189.17", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "-0.4", "instability": "88.93", "hydrophobic": "0.0", "boman": "-0.94", "helix": "0.0", "turn_pct": "1.0", "sheet": "0.0" }, { "id": "aceip0246", "seq": "GGL", "length": "3", "detail": "Sweet-potato", "source": "Potato", "ic50": null, "reference": "Quantitative structure-activity relationship study of bitter di- and tri-peptides including relationship with angiotensin I-converting enzyme inhibitory activity.; QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1002\/psc.800; 10.1007\/s00894-010-0862-x; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "17117396 20941517 23871047", "mw": "245.28", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "1.0", "instability": "47.8", "hydrophobic": "0.3333", "boman": "-2.2667", "helix": "0.3333", "turn_pct": "0.6667", "sheet": "0.3333" }, { "id": "aceip0247", "seq": "GGP", "length": "3", "detail": "Milk", "source": "Milk", "ic50": null, "reference": "Quantitative structure-activity relationship study of bitter di- and tri-peptides including relationship with angiotensin I-converting enzyme inhibitory activity.; QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1002\/psc.800; 10.1007\/s00894-010-0862-x; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "17117396 20941517 23871047", "mw": "229.23", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "-0.8", "instability": "47.8", "hydrophobic": "0.3333", "boman": "-0.6267", "helix": "0.0", "turn_pct": "1.0", "sheet": "0.0" }, { "id": "aceip0248", "seq": "GGV", "length": "3", "detail": "Creatine kinase | Chicken", "source": "Chicken", "ic50": null, "reference": "Quantitative structure-activity relationship study of bitter di- and tri-peptides including relationship with angiotensin I-converting enzyme inhibitory activity.; QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1002\/psc.800; 10.1007\/s00894-010-0862-x; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "17117396 20941517 23871047", "mw": "231.25", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "1.1333", "instability": "47.8", "hydrophobic": "0.3333", "boman": "-1.9733", "helix": "0.0", "turn_pct": "0.6667", "sheet": "0.3333" }, { "id": "aceip0249", "seq": "GGVIPN", "length": "6", "detail": "Milk", "source": "Milk", "ic50": "0.74 μM", "reference": "Inhibition strength of short peptides derived from an ACE inhibitory peptide.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1021\/jf202902r; 10.1016\/j.foodchem.2012.09.092", "pubmedid": "21923188 23194537", "mw": "555.62", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "0.4667", "instability": "24.1", "hydrophobic": "0.5", "boman": "-1.5367", "helix": "0.0", "turn_pct": "0.6667", "sheet": "0.3333" }, { "id": "aceip0250", "seq": "GGY", "length": "3", "detail": "Rapeseed", "source": "Plants", "ic50": "<20 mM", "reference": "Structure and activity of angiotensin I converting enzyme inhibitory peptides from sake and sake lees.; Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Quantitative structure-activity relationship study of bitter di- and tri-peptides including relationship with angiotensin I-converting enzyme inhibitory activity.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1271\/bbb.58.1767; 10.1021\/jf051263l; 10.1002\/psc.800; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "7765503 16448176 17117396 23871047", "mw": "295.29", "pi": "5.52", "charge_ph7": "-0.24", "gravy": "-0.7", "instability": "19.5", "hydrophobic": "0.0", "boman": "-0.58", "helix": "0.0", "turn_pct": "0.6667", "sheet": "0.3333" }, { "id": "aceip0251", "seq": "GH", "length": "2", "detail": "Cereals (Maize)", "source": "Cereal", "ic50": "<20 mM", "reference": "Binding of peptide substrates and inhibitors of angiotensin-converting enzyme. Importance of the COOH-terminal dipeptide sequence.; Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Three-dimensional holograph vector of atomic interaction field (3D-HoVAIF): a novel rotation-translation invariant 3D structure descriptor and its applications to peptides.; QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.; Peptides with angiotensin I converting enzyme (ACE) inhibitory activity generated from porcine skeletal muscle proteins by the action of meat-borne Lactobacillus.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1021\/jf051263l; 10.1002\/psc.892; 10.1007\/s00894-010-0862-x; 10.1016\/j.jprot.2013.06.023; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "6243277 16448176 17654623 20941517 23806758 23871047", "mw": "212.21", "pi": "6.74", "charge_ph7": "-0.15", "gravy": "-1.8", "instability": "5.0", "hydrophobic": "0.0", "boman": "0.025", "helix": "0.0", "turn_pct": "0.5", "sheet": "0.0" }, { "id": "aceip0252", "seq": "GHF", "length": "3", "detail": "Cereals (Maize)", "source": "Cereal", "ic50": "1001 μM", "reference": "Angiotensin I-converting enzyme inhibitory peptides derived from bonito bowels autolysate.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1271\/bbb.57.695; 10.1016\/j.foodchem.2013.05.140; 10.1080\/10408398.2012.664829", "pubmedid": "7763772 23871047 24915368", "mw": "359.38", "pi": "6.74", "charge_ph7": "-0.15", "gravy": "-0.2667", "instability": "-27.9", "hydrophobic": "0.3333", "boman": "-0.9767", "helix": "0.0", "turn_pct": "0.3333", "sheet": "0.3333" }, { "id": "aceip0253", "seq": "GHG", "length": "3", "detail": "Milk (Casein)", "source": "Milk", "ic50": "122 μM", "reference": "What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1016\/j.foodchem.2013.05.140", "pubmedid": "23871047", "mw": "269.26", "pi": "6.74", "charge_ph7": "-0.15", "gravy": "-1.3333", "instability": "-27.9", "hydrophobic": "0.0", "boman": "-0.2967", "helix": "0.0", "turn_pct": "0.6667", "sheet": "0.0" }, { "id": "aceip0254", "seq": "GHKIATFQER", "length": "10", "detail": "ND", "source": "ND", "ic50": "0.4 μM", "reference": "Production of angiotensin-converting enzyme inhibitors from baker's yeast glyceraldehyde-3-phosphate dehydrogenase.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1248\/bpb1978.13.766; 10.1016\/j.foodchem.2012.09.092", "pubmedid": "2098549 23194537", "mw": "1186.32", "pi": "8.76", "charge_ph7": "0.85", "gravy": "-1.06", "instability": "55.79", "hydrophobic": "0.3", "boman": "-0.21", "helix": "0.3", "turn_pct": "0.1", "sheet": "0.3" }, { "id": "aceip0255", "seq": "GHKIATFQQR", "length": "10", "detail": "ND", "source": "ND", "ic50": "0.4 μM", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "23194537", "mw": "1185.34", "pi": "11.0", "charge_ph7": "1.85", "gravy": "-1.06", "instability": "55.79", "hydrophobic": "0.3", "boman": "-0.238", "helix": "0.2", "turn_pct": "0.1", "sheet": "0.3" }, { "id": "aceip0256", "seq": "GHS", "length": "3", "detail": "Royal jelly", "source": "Insect", "ic50": "0.52 ± 0.01 mg\/ml", "reference": "Review on the angiotensin-I-converting enzyme (ACE) inhibitor peptides from marine proteins.; Glycinyl-histidinyl-serine (GHS), a novel rapeseed protein-derived peptide has blood pressure-lowering effect in spontaneously hypertensive rats.", "doi": "10.1007\/s12010-012-0024-y; 10.1021\/jf400865m", "pubmedid": "23271625 23919612", "mw": "299.28", "pi": "6.74", "charge_ph7": "-0.15", "gravy": "-1.4667", "instability": "6.67", "hydrophobic": "0.0", "boman": "0.2967", "helix": "0.0", "turn_pct": "0.6667", "sheet": "0.0" }, { "id": "aceip0257", "seq": "GI", "length": "2", "detail": "Amaranth | Cereals (Maize) | Cereals (Wheat) | Maize", "source": "Plants | Cereal", "ic50": "<20 mM", "reference": "Binding of peptide substrates and inhibitors of angiotensin-converting enzyme. Importance of the COOH-terminal dipeptide sequence.; Angiotensin I-converting enzyme inhibitory activity and insulin secretion stimulative activity of fermented fish sauce.; Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Three-dimensional holograph vector of atomic interaction field (3D-HoVAIF): a novel rotation-translation invariant 3D structure descriptor and its applications to peptides.; QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.; Peptides with angiotensin I converting enzyme (ACE) inhibitory activity generated from porcine skeletal muscle proteins by the action of meat-borne Lactobacillus.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1016\/S1389-1723(03)70138-8; 10.1021\/jf051263l; 10.1002\/psc.892; 10.1007\/s00894-010-0862-x; 10.1016\/j.jprot.2013.06.023; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "6243277 16233562 16448176 17654623 20941517 23806758 23871047", "mw": "188.22", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "2.05", "instability": "-37.45", "hydrophobic": "0.5", "boman": "-2.93", "helix": "0.0", "turn_pct": "0.5", "sheet": "0.5" }, { "id": "aceip0258", "seq": "GIPGERGPVGPSG", "length": "13", "detail": "Salmon", "source": "Fish", "ic50": "43.4 μM", "reference": "Angiotensin I-converting enzyme-inhibitory peptides obtained from chicken collagen hydrolysate.", "doi": "10.1021\/jf072669w", "pubmedid": "18808143", "mw": "1179.28", "pi": "6.0", "charge_ph7": "-0.24", "gravy": "-0.5308", "instability": "11.25", "hydrophobic": "0.3846", "boman": "-0.6508", "helix": "0.0769", "turn_pct": "0.6923", "sheet": "0.1538" }, { "id": "aceip0259", "seq": "GK", "length": "2", "detail": "Salmon", "source": "Fish", "ic50": "<20 mM", "reference": "Binding of peptide substrates and inhibitors of angiotensin-converting enzyme. Importance of the COOH-terminal dipeptide sequence.; Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Three-dimensional holograph vector of atomic interaction field (3D-HoVAIF): a novel rotation-translation invariant 3D structure descriptor and its applications to peptides.; Assessing the dependence of (51)V A(z) value on the aromatic ring orientation of V(IV)O(2+) pyridine complexes.; Model of the exofacial substrate-binding site and helical folding of the human Glut1 glucose transporter based on scanning mutagenesis.; QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.; Peptides with angiotensin I converting enzyme (ACE) inhibitory activity generated from porcine skeletal muscle proteins by the action of meat-borne Lactobacillus.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1021\/jf051263l; 10.1002\/psc.892; 10.1021\/ic9001779; 10.1021\/bi900521n; 10.1007\/s00894-010-0862-x; 10.1016\/j.jprot.2013.06.023; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "6243277 16448176 17654623 19449891 19449892 20941517 23806758 23871047", "mw": "203.24", "pi": "8.75", "charge_ph7": "0.76", "gravy": "-2.15", "instability": "-37.45", "hydrophobic": "0.0", "boman": "0.32", "helix": "0.5", "turn_pct": "0.5", "sheet": "0.0" }, { "id": "aceip0260", "seq": "GKEIIVKAQR", "length": "10", "detail": "Meat", "source": "Meat", "ic50": "66.07 μM", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "23194537", "mw": "1141.36", "pi": "9.99", "charge_ph7": "1.76", "gravy": "-0.47", "instability": "8.4", "hydrophobic": "0.4", "boman": "-0.775", "helix": "0.4", "turn_pct": "0.1", "sheet": "0.3" }, { "id": "aceip0261", "seq": "GKEKV", "length": "5", "detail": "Milk (bovine) | Casein | Milk (whey) | Cheese (Manchego cheese) | Milk (cheese whey) | Amaranth | Cereals (Wheat) | Soybean | Chicken", "source": "Milk | Plants | Cereal | Legume | Chicken", "ic50": null, "reference": "Hot topic: Changes in angiotensin-converting enzyme inhibition and concentrations of the tripeptides Val-Pro-Pro and Ile-Pro-Pro during ripening of different Swiss cheese varieties.", "doi": "10.3168\/jds.2008-1531", "pubmedid": "19233775", "mw": "559.66", "pi": "8.59", "charge_ph7": "0.76", "gravy": "-1.5", "instability": "-25.96", "hydrophobic": "0.2", "boman": "-0.036", "helix": "0.6", "turn_pct": "0.2", "sheet": "0.2" }, { "id": "aceip0262", "seq": "GKEKVNELSKDI", "length": "12", "detail": "Cheese (Manchego cheese)", "source": "Milk", "ic50": null, "reference": "Hot topic: Changes in angiotensin-converting enzyme inhibition and concentrations of the tripeptides Val-Pro-Pro and Ile-Pro-Pro during ripening of different Swiss cheese varieties.", "doi": "10.3168\/jds.2008-1531", "pubmedid": "19233775", "mw": "1359.52", "pi": "6.18", "charge_ph7": "-0.24", "gravy": "-1.2", "instability": "-4.98", "hydrophobic": "0.25", "boman": "-0.2217", "helix": "0.5", "turn_pct": "0.3333", "sheet": "0.25" }, { "id": "aceip0263", "seq": "GKKIATYQER", "length": "10", "detail": "Milk (bovine) | Milk (whey) | Milk (Digested milk products)", "source": "Milk", "ic50": "2 μM", "reference": "Production of angiotensin-converting enzyme inhibitors from baker's yeast glyceraldehyde-3-phosphate dehydrogenase.", "doi": "10.1248\/bpb1978.13.766", "pubmedid": "2098549", "mw": "1193.35", "pi": "9.7", "charge_ph7": "1.76", "gravy": "-1.54", "instability": "11.28", "hydrophobic": "0.2", "boman": "0.161", "helix": "0.4", "turn_pct": "0.1", "sheet": "0.3" }, { "id": "aceip0264", "seq": "GKKVLQ", "length": "6", "detail": "ND", "source": "ND", "ic50": "1.9 μM", "reference": "Antihypertensive effect of angiotensin I-converting enzyme inhibitory peptides derived from hemoglobin.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/0014-2999(96)00146-x; 10.1016\/j.foodchem.2012.09.092", "pubmedid": "8813589 23194537", "mw": "671.83", "pi": "10.0", "charge_ph7": "1.76", "gravy": "-0.6167", "instability": "34.37", "hydrophobic": "0.3333", "boman": "-0.8967", "helix": "0.5", "turn_pct": "0.1667", "sheet": "0.3333" }, { "id": "aceip0265", "seq": "GKMVKVVSWY", "length": "10", "detail": "ND", "source": "ND", "ic50": "6.76 μM", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "23194537", "mw": "1196.46", "pi": "9.7", "charge_ph7": "1.76", "gravy": "0.33", "instability": "21.74", "hydrophobic": "0.5", "boman": "-1.36", "helix": "0.3", "turn_pct": "0.2", "sheet": "0.5" }, { "id": "aceip0266", "seq": "GKP", "length": "3", "detail": "Pork", "source": "Porcine", "ic50": "<20 mM", "reference": "Structural analysis of new antihypertensive peptides derived from cheese whey protein by proteinase K digestion.; Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Bioactive peptides in amaranth (Amaranthus hypochondriacus) seed.; Inhibition strength of short peptides derived from an ACE inhibitory peptide.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.3168\/jds.S0022-0302(98)75878-3; 10.1021\/jf051263l; 10.1021\/jf072911z; 10.1021\/jf202902r; 10.1016\/j.foodchem.2013.05.140; 10.1080\/10408398.2012.664829", "pubmedid": "9891260 16448176 18211015 21923188 23871047 24915368", "mw": "300.35", "pi": "8.75", "charge_ph7": "0.76", "gravy": "-1.9667", "instability": "-46.77", "hydrophobic": "0.3333", "boman": "0.2133", "helix": "0.3333", "turn_pct": "0.6667", "sheet": "0.0" }, { "id": "aceip0267", "seq": "GKV", "length": "3", "detail": "Pork", "source": "Porcine", "ic50": "<20 mM", "reference": "Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.", "doi": "10.1021\/jf051263l", "pubmedid": "16448176", "mw": "302.37", "pi": "8.75", "charge_ph7": "0.76", "gravy": "-0.0333", "instability": "-49.93", "hydrophobic": "0.3333", "boman": "-1.1333", "helix": "0.3333", "turn_pct": "0.3333", "sheet": "0.3333" }, { "id": "aceip0268", "seq": "GL", "length": "2", "detail": "ND", "source": "ND", "ic50": "<20 mM", "reference": "Binding of peptide substrates and inhibitors of angiotensin-converting enzyme. Importance of the COOH-terminal dipeptide sequence.; Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Three-dimensional holograph vector of atomic interaction field (3D-HoVAIF): a novel rotation-translation invariant 3D structure descriptor and its applications to peptides.; QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.; Peptides with angiotensin I converting enzyme (ACE) inhibitory activity generated from porcine skeletal muscle proteins by the action of meat-borne Lactobacillus.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1021\/jf051263l; 10.1002\/psc.892; 10.1007\/s00894-010-0862-x; 10.1016\/j.jprot.2013.06.023; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "6243277 16448176 17654623 20941517 23806758 23871047", "mw": "188.22", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "1.7", "instability": "5.0", "hydrophobic": "0.5", "boman": "-2.93", "helix": "0.5", "turn_pct": "0.5", "sheet": "0.5" }, { "id": "aceip0269", "seq": "GLDIQK", "length": "6", "detail": "Casein", "source": "Milk", "ic50": "580 μM", "reference": "Quality and acceptability of a set-type yogurt made from camel milk.", "doi": "10.3168\/jds.2008-1408", "pubmedid": "19233778", "mw": "672.77", "pi": "5.84", "charge_ph7": "-0.24", "gravy": "-0.5", "instability": "8.33", "hydrophobic": "0.3333", "boman": "-1.0267", "helix": "0.3333", "turn_pct": "0.3333", "sheet": "0.3333" }, { "id": "aceip0270", "seq": "GLG", "length": "3", "detail": "Milk (bovine) | Casein", "source": "Milk", "ic50": null, "reference": "Quantitative structure-activity relationship study of bitter di- and tri-peptides including relationship with angiotensin I-converting enzyme inhibitory activity.; QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1002\/psc.800; 10.1007\/s00894-010-0862-x; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "17117396 20941517 23871047", "mw": "245.28", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "1.0", "instability": "6.67", "hydrophobic": "0.3333", "boman": "-2.2667", "helix": "0.3333", "turn_pct": "0.6667", "sheet": "0.3333" }, { "id": "aceip0271", "seq": "GLL", "length": "3", "detail": "ND", "source": "ND", "ic50": null, "reference": "Quantitative structure-activity relationship study of bitter di- and tri-peptides including relationship with angiotensin I-converting enzyme inhibitory activity.; QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1002\/psc.800; 10.1007\/s00894-010-0862-x; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "17117396 20941517 23871047", "mw": "301.38", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "2.4", "instability": "6.67", "hydrophobic": "0.6667", "boman": "-3.5933", "helix": "0.6667", "turn_pct": "0.3333", "sheet": "0.6667" }, { "id": "aceip0272", "seq": "GLP", "length": "3", "detail": "Food-protein | chicken", "source": "Synthesized | Chicken", "ic50": "1.62 μM", "reference": "Structure and activity of angiotensin I converting enzyme inhibitory peptides derived from Alaskan pollack skin.", "doi": "10.5483\/bmbrep.2002.35.2.239", "pubmedid": "12297036", "mw": "285.34", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "0.6", "instability": "70.87", "hydrophobic": "0.6667", "boman": "-1.9533", "helix": "0.3333", "turn_pct": "0.6667", "sheet": "0.3333" }, { "id": "aceip0273", "seq": "GLPGSRGERGLPG", "length": "13", "detail": "ND", "source": "ND", "ic50": "60.8 μM", "reference": "Angiotensin I-converting enzyme-inhibitory peptides obtained from chicken collagen hydrolysate.", "doi": "10.1021\/jf072669w", "pubmedid": "18808143", "mw": "1252.38", "pi": "9.6", "charge_ph7": "0.76", "gravy": "-0.8385", "instability": "34.82", "hydrophobic": "0.3077", "boman": "-0.5092", "helix": "0.2308", "turn_pct": "0.6154", "sheet": "0.1538" }, { "id": "aceip0274", "seq": "GLSDGEWQ", "length": "8", "detail": "Pork", "source": "Porcine", "ic50": "117.6 mg\/ml", "reference": "Antihypertensive peptides: production, bioavailability and incorporation into foods.", "doi": "10.1016\/j.cis.2010.11.001", "pubmedid": "21185549", "mw": "890.89", "pi": "4.05", "charge_ph7": "-2.24", "gravy": "-1.15", "instability": "-19.46", "hydrophobic": "0.25", "boman": "-0.4512", "helix": "0.25", "turn_pct": "0.5", "sheet": "0.25" }, { "id": "aceip0275", "seq": "GLY", "length": "3", "detail": "Hemoglobulin | Pork", "source": "Synthesized | Porcine", "ic50": "<20 mM", "reference": "Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1021\/jf051263l; 10.1080\/10408398.2012.664829", "pubmedid": "16448176 24915368", "mw": "351.4", "pi": "5.52", "charge_ph7": "-0.24", "gravy": "0.7", "instability": "6.67", "hydrophobic": "0.3333", "boman": "-1.9067", "helix": "0.3333", "turn_pct": "0.3333", "sheet": "0.6667" }, { "id": "aceip0276", "seq": "GM", "length": "2", "detail": "Hemoglobulin", "source": "Synthesized", "ic50": "<20 mM", "reference": "Binding of peptide substrates and inhibitors of angiotensin-converting enzyme. Importance of the COOH-terminal dipeptide sequence.; Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Three-dimensional holograph vector of atomic interaction field (3D-HoVAIF): a novel rotation-translation invariant 3D structure descriptor and its applications to peptides.; QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.; Peptides with angiotensin I converting enzyme (ACE) inhibitory activity generated from porcine skeletal muscle proteins by the action of meat-borne Lactobacillus.", "doi": "10.1021\/jf051263l; 10.1002\/psc.892; 10.1007\/s00894-010-0862-x; 10.1016\/j.jprot.2013.06.023", "pubmedid": "6243277 16448176 17654623 20941517 23806758", "mw": "206.26", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "0.75", "instability": "5.0", "hydrophobic": "0.5", "boman": "-1.645", "helix": "0.5", "turn_pct": "0.5", "sheet": "0.0" }, { "id": "aceip0277", "seq": "GP", "length": "2", "detail": "Amaranth | Bonito | Actin | Cereals | Cereals (Wheat)", "source": "Plants | Fish | Cereal", "ic50": "<20 mM", "reference": "Structure and activity of angiotensin I converting enzyme inhibitory peptides derived from Alaskan pollack skin.; Angiotensin I-converting enzyme inhibitory activity and insulin secretion stimulative activity of fermented fish sauce.; Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Quantitative structure-activity relationship study of bitter di- and tri-peptides including relationship with angiotensin I-converting enzyme inhibitory activity.; Three-dimensional holograph vector of atomic interaction field (3D-HoVAIF): a novel rotation-translation invariant 3D structure descriptor and its applications to peptides.; Assessing the dependence of (51)V A(z) value on the aromatic ring orientation of V(IV)O(2+) pyridine complexes.; QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.5483\/bmbrep.2002.35.2.239; 10.1016\/S1389-1723(03)70138-8; 10.1021\/jf051263l; 10.1002\/psc.800; 10.1002\/psc.892; 10.1021\/ic9001779; 10.1007\/s00894-010-0862-x; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "12297036 16233562 16448176 17117396 17654623 19449891 20941517 23871047", "mw": "172.18", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "-1.0", "instability": "5.0", "hydrophobic": "0.5", "boman": "-0.47", "helix": "0.0", "turn_pct": "1.0", "sheet": "0.0" }, { "id": "aceip0278", "seq": "GPA", "length": "3", "detail": "Milk (human)", "source": "Milk", "ic50": "405 μM", "reference": "Peptide inhibitors of angiotensin I-converting enzyme in digests of gelatin by bacterial collagenase.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1016\/0005-2744(79)90255-9; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "215231 23871047", "mw": "243.26", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "-0.0667", "instability": "70.87", "hydrophobic": "0.6667", "boman": "-0.9167", "helix": "0.3333", "turn_pct": "0.6667", "sheet": "0.0" }, { "id": "aceip0279", "seq": "GPAGAP", "length": "6", "detail": "Milk (bovine) | Cereals", "source": "Milk | Cereal", "ic50": "8.3 mM", "reference": "Peptide inhibitors of angiotensin I-converting enzyme in digests of gelatin by bacterial collagenase.", "doi": "10.1016\/0005-2744(79)90255-9", "pubmedid": "215231", "mw": "468.5", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "-0.0667", "instability": "58.38", "hydrophobic": "0.6667", "boman": "-0.9167", "helix": "0.3333", "turn_pct": "0.6667", "sheet": "0.0" }, { "id": "aceip0280", "seq": "GPAGAPGAA", "length": "9", "detail": "Egg (Ovalbumin)", "source": "Egg", "ic50": "37 μM", "reference": "Peptide inhibitors of angiotensin I-converting enzyme in digests of gelatin by bacterial collagenase.; QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.", "doi": "10.1016\/0005-2744(79)90255-9; 10.1007\/s00894-010-0862-x", "pubmedid": "215231 20941517", "mw": "667.71", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "0.3111", "instability": "32.82", "hydrophobic": "0.6667", "boman": "-1.1178", "helix": "0.4444", "turn_pct": "0.5556", "sheet": "0.0" }, { "id": "aceip0281", "seq": "GPCSR", "length": "5", "detail": "Egg (Ovalbumin)", "source": "Egg", "ic50": "61.67 μM", "reference": "Novel angiotensin I-converting enzyme inhibitory peptides derived from an edible mushroom, Pleurotus cystidiosus O.K. Miller identified by LC-MS\/MS.", "doi": "10.1186\/1472-6882-13-313", "pubmedid": "24215325", "mw": "518.59", "pi": "8.25", "charge_ph7": "0.75", "gravy": "-0.96", "instability": "31.44", "hydrophobic": "0.2", "boman": "0.268", "helix": "0.0", "turn_pct": "0.6", "sheet": "0.0" }, { "id": "aceip0282", "seq": "GPFPIIV", "length": "7", "detail": "ND", "source": "ND", "ic50": "0 0", "reference": "Putting microbes to work: dairy fermentation, cell factories and bioactive peptides. Part I: overview.", "doi": "10.1002\/biot.200600246", "pubmedid": "17407210", "mw": "741.92", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "1.7714", "instability": "51.47", "hydrophobic": "0.8571", "boman": "-2.5429", "helix": "0.0", "turn_pct": "0.4286", "sheet": "0.5714" }, { "id": "aceip0283", "seq": "GPG", "length": "3", "detail": "Egg (Ovalbumin)", "source": "Egg", "ic50": null, "reference": "Quantitative structure-activity relationship study of bitter di- and tri-peptides including relationship with angiotensin I-converting enzyme inhibitory activity.; QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1002\/psc.800; 10.1007\/s00894-010-0862-x; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "17117396 20941517 23871047", "mw": "229.23", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "-0.8", "instability": "6.67", "hydrophobic": "0.3333", "boman": "-0.6267", "helix": "0.0", "turn_pct": "1.0", "sheet": "0.0" }, { "id": "aceip0284", "seq": "GPIGPP", "length": "6", "detail": "Legume (Pea proteins)", "source": "Legume", "ic50": "123.4 μM", "reference": "Peptide inhibitors of angiotensin I-converting enzyme in digests of gelatin by bacterial collagenase.", "doi": "10.1016\/0005-2744(79)90255-9", "pubmedid": "215231", "mw": "536.62", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "-0.1833", "instability": "40.43", "hydrophobic": "0.6667", "boman": "-1.1333", "helix": "0.0", "turn_pct": "0.8333", "sheet": "0.1667" }, { "id": "aceip0285", "seq": "GPIGSVGAP", "length": "9", "detail": "Soybean", "source": "Legume", "ic50": "31.8 mM", "reference": "Peptide inhibitors of angiotensin I-converting enzyme in digests of gelatin by bacterial collagenase.", "doi": "10.1016\/0005-2744(79)90255-9", "pubmedid": "215231", "mw": "753.84", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "0.5889", "instability": "11.42", "hydrophobic": "0.5556", "boman": "-1.4167", "helix": "0.1111", "turn_pct": "0.6667", "sheet": "0.2222" }, { "id": "aceip0286", "seq": "GPL", "length": "3", "detail": "Sardine", "source": "Fish", "ic50": "<20 mM", "reference": "Structure and activity of angiotensin I converting enzyme inhibitory peptides derived from Alaskan pollack skin.; Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Review on the angiotensin-I-converting enzyme (ACE) inhibitor peptides from marine proteins.; Rational design of angiotensin-I-converting enzyme inhibitory peptides by integrating in silico modeling and an in vitro assay.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.; Glycinyl-histidinyl-serine (GHS), a novel rapeseed protein-derived peptide has blood pressure-lowering effect in spontaneously hypertensive rats.", "doi": "10.5483\/bmbrep.2002.35.2.239; 10.1021\/jf051263l; 10.1007\/s12010-012-0024-y; 10.1002\/cmdc.201300132; 10.1016\/j.foodchem.2013.05.140; 10.1021\/jf400865m", "pubmedid": "12297036 16448176 23271625 23740817 23871047 23919612", "mw": "285.34", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "0.6", "instability": "6.67", "hydrophobic": "0.6667", "boman": "-1.9533", "helix": "0.3333", "turn_pct": "0.6667", "sheet": "0.3333" }, { "id": "aceip0287", "seq": "GPLGLLGFLGPLGLS", "length": "15", "detail": "Cereals (Barley)", "source": "Cereal", "ic50": "90.03 μM", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.; Review on the angiotensin-I-converting enzyme (ACE) inhibitor peptides from marine proteins.", "doi": "10.1016\/j.foodchem.2012.09.092; 10.1007\/s12010-012-0024-y", "pubmedid": "23194537 23271625", "mw": "1410.7", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "1.3067", "instability": "9.33", "hydrophobic": "0.6", "boman": "-2.424", "helix": "0.4", "turn_pct": "0.5333", "sheet": "0.4667" }, { "id": "aceip0288", "seq": "GPM", "length": "3", "detail": "Milk (bovine) | Casein", "source": "Milk", "ic50": "<20 mM", "reference": "Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Review on the angiotensin-I-converting enzyme (ACE) inhibitor peptides from marine proteins.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.; Glycinyl-histidinyl-serine (GHS), a novel rapeseed protein-derived peptide has blood pressure-lowering effect in spontaneously hypertensive rats.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1021\/jf051263l; 10.1007\/s12010-012-0024-y; 10.1016\/j.foodchem.2013.05.140; 10.1021\/jf400865m; 10.1080\/10408398.2012.664829", "pubmedid": "16448176 23271625 23871047 23919612 24915368", "mw": "303.38", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "-0.0333", "instability": "-18.47", "hydrophobic": "0.6667", "boman": "-1.0967", "helix": "0.3333", "turn_pct": "0.6667", "sheet": "0.0" }, { "id": "aceip0289", "seq": "GPP", "length": "3", "detail": "Casein", "source": "Milk", "ic50": "<20 mM", "reference": "Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Angiotensin converting enzyme inhibitory peptides derived from food proteins: biochemistry, bioactivity and production.; Sex pheromone of the longtailed mealybug: a new class of monoterpene structure.; Vegetable foods: a cheap source of proteins and peptides with antihypertensive, antioxidant, and other less occurrence bioactivities.", "doi": "10.1021\/jf051263l; 10.2174\/138161207780363068; 10.1021\/ol802164v; 10.1016\/j.talanta.2012.12.041", "pubmedid": "16448176 17430180 19449888 23598136", "mw": "269.3", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "-1.2", "instability": "70.87", "hydrophobic": "0.6667", "boman": "-0.3133", "helix": "0.0", "turn_pct": "1.0", "sheet": "0.0" }, { "id": "aceip0290", "seq": "GPPGAP", "length": "6", "detail": "ND", "source": "ND", "ic50": "8.6 mM", "reference": "Peptide inhibitors of angiotensin I-converting enzyme in digests of gelatin by bacterial collagenase.", "doi": "10.1016\/0005-2744(79)90255-9", "pubmedid": "215231", "mw": "494.54", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "-0.6333", "instability": "58.38", "hydrophobic": "0.6667", "boman": "-0.615", "helix": "0.1667", "turn_pct": "0.8333", "sheet": "0.0" }, { "id": "aceip0291", "seq": "GPPGPP", "length": "6", "detail": "Casein", "source": "Milk", "ic50": "11.3 mM", "reference": "Peptide inhibitors of angiotensin I-converting enzyme in digests of gelatin by bacterial collagenase.", "doi": "10.1016\/0005-2744(79)90255-9", "pubmedid": "215231", "mw": "520.58", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "-1.2", "instability": "72.53", "hydrophobic": "0.6667", "boman": "-0.3133", "helix": "0.0", "turn_pct": "1.0", "sheet": "0.0" }, { "id": "aceip0292", "seq": "GPPGTDGAP", "length": "9", "detail": "Cereals (Maize)", "source": "Cereal", "ic50": "10.5 mM", "reference": "Peptide inhibitors of angiotensin I-converting enzyme in digests of gelatin by bacterial collagenase.", "doi": "10.1016\/0005-2744(79)90255-9", "pubmedid": "215231", "mw": "767.78", "pi": "4.05", "charge_ph7": "-1.24", "gravy": "-0.9333", "instability": "32.82", "hydrophobic": "0.4444", "boman": "-0.2989", "helix": "0.1111", "turn_pct": "0.7778", "sheet": "0.1111" }, { "id": "aceip0293", "seq": "GPR", "length": "3", "detail": "Shrimp", "source": "Shrimp", "ic50": "382->1000 μM", "reference": "Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1080\/10408398.2012.664829", "pubmedid": "24915368", "mw": "328.37", "pi": "9.75", "charge_ph7": "0.76", "gravy": "-2.1667", "instability": "-18.47", "hydrophobic": "0.3333", "boman": "0.5933", "helix": "0.0", "turn_pct": "0.6667", "sheet": "0.0" }, { "id": "aceip0294", "seq": "GPSMR", "length": "5", "detail": "Sweet-potato", "source": "Potato", "ic50": "277.5 μM", "reference": "Novel angiotensin I-converting enzyme inhibitory peptides derived from an edible mushroom, Pleurotus cystidiosus O.K. Miller identified by LC-MS\/MS.", "doi": "10.1186\/1472-6882-13-313", "pubmedid": "24215325", "mw": "546.64", "pi": "9.75", "charge_ph7": "0.76", "gravy": "-1.08", "instability": "31.44", "hydrophobic": "0.4", "boman": "0.054", "helix": "0.2", "turn_pct": "0.6", "sheet": "0.0" }, { "id": "aceip0295", "seq": "GPV", "length": "3", "detail": "Milk (bovine)", "source": "Milk", "ic50": "<20 mM", "reference": "Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.", "doi": "10.1021\/jf051263l", "pubmedid": "16448176", "mw": "271.31", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "0.7333", "instability": "70.87", "hydrophobic": "0.6667", "boman": "-1.66", "helix": "0.0", "turn_pct": "0.6667", "sheet": "0.3333" }, { "id": "aceip0296", "seq": "GPVGPA", "length": "6", "detail": "Shrimp", "source": "Shrimp", "ic50": "123.4 μM", "reference": "Peptide inhibitors of angiotensin I-converting enzyme in digests of gelatin by bacterial collagenase.", "doi": "10.1016\/0005-2744(79)90255-9", "pubmedid": "215231", "mw": "496.56", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "0.3333", "instability": "58.38", "hydrophobic": "0.6667", "boman": "-1.2883", "helix": "0.1667", "turn_pct": "0.6667", "sheet": "0.1667" }, { "id": "aceip0297", "seq": "GPVRGPFPII", "length": "10", "detail": "ND", "source": "ND", "ic50": "0 0", "reference": "Angiotensin converting enzyme inhibitory activity in commercial fermented products. Formation of peptides under simulated gastrointestinal digestion.", "doi": "10.1021\/jf034997b", "pubmedid": "15030202", "mw": "1052.27", "pi": "9.75", "charge_ph7": "0.76", "gravy": "0.59", "instability": "58.29", "hydrophobic": "0.7", "boman": "-1.602", "helix": "0.0", "turn_pct": "0.5", "sheet": "0.4" }, { "id": "aceip0298", "seq": "GQ", "length": "2", "detail": "Milk (bovine) | Casein | Milk (Digested milk products)", "source": "Milk", "ic50": "<20 mM", "reference": "Binding of peptide substrates and inhibitors of angiotensin-converting enzyme. Importance of the COOH-terminal dipeptide sequence.; Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Three-dimensional holograph vector of atomic interaction field (3D-HoVAIF): a novel rotation-translation invariant 3D structure descriptor and its applications to peptides.; QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.; Peptides with angiotensin I converting enzyme (ACE) inhibitory activity generated from porcine skeletal muscle proteins by the action of meat-borne Lactobacillus.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1021\/jf051263l; 10.1002\/psc.892; 10.1007\/s00894-010-0862-x; 10.1016\/j.jprot.2013.06.023; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "6243277 16448176 17654623 20941517 23806758 23871047", "mw": "203.2", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "-1.95", "instability": "5.0", "hydrophobic": "0.0", "boman": "0.21", "helix": "0.0", "turn_pct": "0.5", "sheet": "0.0" }, { "id": "aceip0299", "seq": "GQP", "length": "3", "detail": "Milk (bovine)", "source": "Milk", "ic50": "<20 mM", "reference": "Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.", "doi": "10.1021\/jf051263l", "pubmedid": "16448176", "mw": "300.31", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "-1.8333", "instability": "70.87", "hydrophobic": "0.3333", "boman": "0.14", "helix": "0.0", "turn_pct": "0.6667", "sheet": "0.0" }, { "id": "aceip0300", "seq": "GR", "length": "2", "detail": "Casein", "source": "Milk", "ic50": "<20 mM", "reference": "Binding of peptide substrates and inhibitors of angiotensin-converting enzyme. Importance of the COOH-terminal dipeptide sequence.; Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Quantitative structure-activity relationship study of bitter di- and tri-peptides including relationship with angiotensin I-converting enzyme inhibitory activity.; Three-dimensional holograph vector of atomic interaction field (3D-HoVAIF): a novel rotation-translation invariant 3D structure descriptor and its applications to peptides.; QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.; Peptides with angiotensin I converting enzyme (ACE) inhibitory activity generated from porcine skeletal muscle proteins by the action of meat-borne Lactobacillus.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1021\/jf051263l; 10.1002\/psc.800; 10.1002\/psc.892; 10.1007\/s00894-010-0862-x; 10.1016\/j.jprot.2013.06.023; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "6243277 16448176 17117396 17654623 20941517 23806758 23871047", "mw": "231.25", "pi": "9.75", "charge_ph7": "0.76", "gravy": "-2.45", "instability": "5.0", "hydrophobic": "0.0", "boman": "0.89", "helix": "0.0", "turn_pct": "0.5", "sheet": "0.0" }, { "id": "aceip0301", "seq": "GRP", "length": "3", "detail": "Cheese", "source": "Milk", "ic50": "<20 mM", "reference": "Angiotensin I-converting enzyme inhibitory peptides in an alkaline protease hydrolyzate derived from sardine muscle.; Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Quantitative structure-activity relationship study of bitter di- and tri-peptides including relationship with angiotensin I-converting enzyme inhibitory activity.; Bioactive peptides in amaranth (Amaranthus hypochondriacus) seed.; QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.; Review on the angiotensin-I-converting enzyme (ACE) inhibitor peptides from marine proteins.; Rational design of angiotensin-I-converting enzyme inhibitory peptides by integrating in silico modeling and an in vitro assay.; Peptides with angiotensin I converting enzyme (ACE) inhibitory activity generated from porcine skeletal muscle proteins by the action of meat-borne Lactobacillus.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1271\/bbb.58.2244; 10.1021\/jf051263l; 10.1002\/psc.800; 10.1021\/jf072911z; 10.1007\/s00894-010-0862-x; 10.1007\/s12010-012-0024-y; 10.1002\/cmdc.201300132; 10.1016\/j.jprot.2013.06.023; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "7765718 16448176 17117396 18211015 20941517 23271625 23740817 23806758 23871047", "mw": "328.37", "pi": "9.75", "charge_ph7": "0.76", "gravy": "-2.1667", "instability": "70.87", "hydrophobic": "0.3333", "boman": "0.5933", "helix": "0.0", "turn_pct": "0.6667", "sheet": "0.0" }, { "id": "aceip0302", "seq": "GRVMP", "length": "5", "detail": "Casein", "source": "Milk", "ic50": "179.67 μM", "reference": "Inhibition of angiotensin-converting enzyme by synthetic peptide fragments of various beta-caseins.", "doi": "", "pubmedid": "1368548", "mw": "558.69", "pi": "9.75", "charge_ph7": "0.76", "gravy": "-0.08", "instability": "95.88", "hydrophobic": "0.6", "boman": "-0.922", "helix": "0.2", "turn_pct": "0.4", "sheet": "0.2" }, { "id": "aceip0303", "seq": "GS", "length": "2", "detail": "Cheese (Fresco) | Cheese (Cheddar (with probiotics))", "source": "Milk", "ic50": "<20 mM", "reference": "Binding of peptide substrates and inhibitors of angiotensin-converting enzyme. Importance of the COOH-terminal dipeptide sequence.; Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Assessing the dependence of (51)V A(z) value on the aromatic ring orientation of V(IV)O(2+) pyridine complexes.; QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.; Peptides with angiotensin I converting enzyme (ACE) inhibitory activity generated from porcine skeletal muscle proteins by the action of meat-borne Lactobacillus.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1021\/jf051263l; 10.1021\/ic9001779; 10.1007\/s00894-010-0862-x; 10.1016\/j.jprot.2013.06.023; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "6243277 16448176 19449891 20941517 23806758 23871047", "mw": "162.14", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "-0.6", "instability": "5.0", "hydrophobic": "0.0", "boman": "-0.05", "helix": "0.0", "turn_pct": "1.0", "sheet": "0.0" }, { "id": "aceip0304", "seq": "GSH", "length": "3", "detail": "Casein", "source": "Milk", "ic50": "<20 mM", "reference": "Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.", "doi": "10.1021\/jf051263l", "pubmedid": "16448176", "mw": "299.28", "pi": "6.74", "charge_ph7": "-0.15", "gravy": "-1.4667", "instability": "6.67", "hydrophobic": "0.0", "boman": "0.2967", "helix": "0.0", "turn_pct": "0.6667", "sheet": "0.0" }, { "id": "aceip0305", "seq": "GT", "length": "2", "detail": "Milk (Casein)", "source": "Milk", "ic50": "<20 mM", "reference": "Binding of peptide substrates and inhibitors of angiotensin-converting enzyme. Importance of the COOH-terminal dipeptide sequence.; Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Three-dimensional holograph vector of atomic interaction field (3D-HoVAIF): a novel rotation-translation invariant 3D structure descriptor and its applications to peptides.; QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.; Peptides with angiotensin I converting enzyme (ACE) inhibitory activity generated from porcine skeletal muscle proteins by the action of meat-borne Lactobacillus.", "doi": "10.1021\/jf051263l; 10.1002\/psc.892; 10.1007\/s00894-010-0862-x; 10.1016\/j.jprot.2013.06.023", "pubmedid": "6243277 16448176 17654623 20941517 23806758", "mw": "176.17", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "-0.55", "instability": "-37.45", "hydrophobic": "0.0", "boman": "-0.34", "helix": "0.0", "turn_pct": "0.5", "sheet": "0.5" }, { "id": "aceip0306", "seq": "GTEKC", "length": "5", "detail": "Milk (Casein)", "source": "Milk", "ic50": "61.67 μM", "reference": "Novel angiotensin I-converting enzyme inhibitory peptides derived from an edible mushroom, Pleurotus cystidiosus O.K. Miller identified by LC-MS\/MS.", "doi": "10.1186\/1472-6882-13-313", "pubmedid": "24215325", "mw": "536.6", "pi": "5.99", "charge_ph7": "-0.25", "gravy": "-1.2", "instability": "29.54", "hydrophobic": "0.0", "boman": "0.252", "helix": "0.4", "turn_pct": "0.2", "sheet": "0.2" }, { "id": "aceip0307", "seq": "GTG", "length": "3", "detail": "Milk (human)", "source": "Milk", "ic50": "5.54 μM", "reference": "Review on the angiotensin-I-converting enzyme (ACE) inhibitor peptides from marine proteins.; Glycinyl-histidinyl-serine (GHS), a novel rapeseed protein-derived peptide has blood pressure-lowering effect in spontaneously hypertensive rats.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1007\/s12010-012-0024-y; 10.1021\/jf400865m; 10.1080\/10408398.2012.664829", "pubmedid": "23271625 23919612 24915368", "mw": "233.22", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "-0.5", "instability": "-49.93", "hydrophobic": "0.0", "boman": "-0.54", "helix": "0.0", "turn_pct": "0.6667", "sheet": "0.3333" }, { "id": "aceip0308", "seq": "GTW", "length": "3", "detail": "Sunflower", "source": "Plants", "ic50": "464 μM", "reference": "Antihypertensive peptides from food proteins: a review.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1039\/c2fo10192k; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "22249830 23871047", "mw": "362.38", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "-0.6667", "instability": "-71.73", "hydrophobic": "0.3333", "boman": "-1.0033", "helix": "0.0", "turn_pct": "0.3333", "sheet": "0.6667" }, { "id": "aceip0309", "seq": "GV", "length": "2", "detail": "Milk (Goat milk protein)", "source": "Milk", "ic50": "<20 mM", "reference": "Binding of peptide substrates and inhibitors of angiotensin-converting enzyme. Importance of the COOH-terminal dipeptide sequence.; Angiotensin I-converting enzyme inhibitory activity and insulin secretion stimulative activity of fermented fish sauce.; Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Quantitative structure-activity relationship study of bitter di- and tri-peptides including relationship with angiotensin I-converting enzyme inhibitory activity.; Three-dimensional holograph vector of atomic interaction field (3D-HoVAIF): a novel rotation-translation invariant 3D structure descriptor and its applications to peptides.; QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.; Peptides with angiotensin I converting enzyme (ACE) inhibitory activity generated from porcine skeletal muscle proteins by the action of meat-borne Lactobacillus.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1016\/S1389-1723(03)70138-8; 10.1021\/jf051263l; 10.1002\/psc.800; 10.1002\/psc.892; 10.1007\/s00894-010-0862-x; 10.1016\/j.jprot.2013.06.023; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "6243277 16233562 16448176 17117396 17654623 20941517 23806758 23871047", "mw": "174.2", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "1.9", "instability": "5.0", "hydrophobic": "0.5", "boman": "-2.49", "helix": "0.0", "turn_pct": "0.5", "sheet": "0.5" }, { "id": "aceip0310", "seq": "GVGAGY", "length": "6", "detail": "Cereals (Barley) | Legume (Pea proteins) | Egg (Ovalbumin)", "source": "Cereal | Legume | Egg", "ic50": "4.07 μM", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "23194537", "mw": "522.55", "pi": "5.52", "charge_ph7": "-0.24", "gravy": "0.5833", "instability": "-34.12", "hydrophobic": "0.3333", "boman": "-1.4217", "helix": "0.1667", "turn_pct": "0.5", "sheet": "0.3333" }, { "id": "aceip0311", "seq": "GVGY", "length": "4", "detail": "Sake", "source": "Cereal", "ic50": "35 μM", "reference": "What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1016\/j.foodchem.2013.05.140", "pubmedid": "23871047", "mw": "394.42", "pi": "5.52", "charge_ph7": "-0.24", "gravy": "0.525", "instability": "-34.95", "hydrophobic": "0.25", "boman": "-1.445", "helix": "0.0", "turn_pct": "0.5", "sheet": "0.5" }, { "id": "aceip0312", "seq": "GVHGV", "length": "5", "detail": "Wakame | Garlic | Cereals (Maize) | Maize | Cereals (Buckwheat)", "source": "Plants | Cereal", "ic50": "2 μM", "reference": "Angiotensin converting enzyme inhibitory peptides derived from food proteins: biochemistry, bioactivity and production.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.2174\/138161207780363068; 10.1016\/j.foodchem.2012.09.092", "pubmedid": "17430180 23194537", "mw": "467.52", "pi": "6.74", "charge_ph7": "-0.15", "gravy": "0.88", "instability": "-12.74", "hydrophobic": "0.4", "boman": "-1.794", "helix": "0.0", "turn_pct": "0.4", "sheet": "0.4" }, { "id": "aceip0313", "seq": "GVHHA", "length": "5", "detail": "ND", "source": "ND", "ic50": "71.8 μM", "reference": "Analysis of novel angiotensin I-converting enzyme inhibitory peptides from enzymatic hydrolysates of cuttlefish (Sepia officinalis) muscle proteins.", "doi": "10.1021\/jf904300q", "pubmedid": "20180574", "mw": "519.55", "pi": "6.92", "charge_ph7": "-0.07", "gravy": "-0.16", "instability": "8.0", "hydrophobic": "0.4", "boman": "-0.962", "helix": "0.2", "turn_pct": "0.2", "sheet": "0.2" }, { "id": "aceip0314", "seq": "GVNGEEGVPG", "length": "10", "detail": "Milk", "source": "Milk", "ic50": null, "reference": "Angiotensin I-converting enzyme inhibitory peptides in a hydrolyzed chicken breast muscle extract.", "doi": "10.1021\/jf020604h", "pubmedid": "12617616", "mw": "913.93", "pi": "4.05", "charge_ph7": "-2.23", "gravy": "-0.53", "instability": "38.29", "hydrophobic": "0.3", "boman": "-0.694", "helix": "0.2", "turn_pct": "0.6", "sheet": "0.2" }, { "id": "aceip0315", "seq": "GVPKVKETMVPK", "length": "12", "detail": "Milk", "source": "Milk", "ic50": "376.1 μM", "reference": "Angiotensin-converting enzyme inhibitory activity of peptides derived from caprine kefir.", "doi": "10.3168\/jds.S0022-0302(05)73032-0", "pubmedid": "16162521", "mw": "1312.62", "pi": "9.7", "charge_ph7": "1.76", "gravy": "-0.4167", "instability": "31.79", "hydrophobic": "0.5", "boman": "-0.7308", "helix": "0.4167", "turn_pct": "0.25", "sheet": "0.3333" }, { "id": "aceip0316", "seq": "GVPKVKETMVPKH", "length": "13", "detail": "Cereals (Maize)", "source": "Cereal", "ic50": "223.2 μM", "reference": "Angiotensin-converting enzyme inhibitory activity of peptides derived from caprine kefir.", "doi": "10.3168\/jds.S0022-0302(05)73032-0", "pubmedid": "16162521", "mw": "1449.76", "pi": "9.7", "charge_ph7": "1.85", "gravy": "-0.6308", "instability": "30.12", "hydrophobic": "0.4615", "boman": "-0.5985", "helix": "0.3846", "turn_pct": "0.2308", "sheet": "0.3077" }, { "id": "aceip0317", "seq": "GVQGPM", "length": "6", "detail": "Egg (Ovalbumin)", "source": "Egg", "ic50": "736.7 ± 4.8 μM", "reference": "Novel angiotensin I-converting enzyme inhibitory peptides derived from edible mushroom Agaricus bisporus (J.E. Lange) Imbach identified by LC-MS\/MS.", "doi": "10.1016\/j.foodchem.2013.10.053", "pubmedid": "24262574", "mw": "587.69", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "0.0333", "instability": "-4.23", "hydrophobic": "0.5", "boman": "-1.1517", "helix": "0.1667", "turn_pct": "0.5", "sheet": "0.1667" }, { "id": "aceip0318", "seq": "GVV", "length": "3", "detail": "Milk (bovine) | Carp | Cereals | Pork | Chicken", "source": "Milk | Fish | Cereal | Porcine | Chicken", "ic50": null, "reference": "Quantitative structure-activity relationship study of bitter di- and tri-peptides including relationship with angiotensin I-converting enzyme inhibitory activity.; QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1002\/psc.800; 10.1007\/s00894-010-0862-x; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "17117396 20941517 23871047", "mw": "273.33", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "2.6667", "instability": "6.67", "hydrophobic": "0.6667", "boman": "-3.0067", "helix": "0.0", "turn_pct": "0.3333", "sheet": "0.6667" }, { "id": "aceip0319", "seq": "GVW", "length": "3", "detail": "Bulfrog", "source": "Amphibian", "ic50": "240 μM", "reference": "Antihypertensive peptides from food proteins: a review.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1039\/c2fo10192k; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "22249830 23871047", "mw": "360.41", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "0.9667", "instability": "6.67", "hydrophobic": "0.6667", "boman": "-2.4367", "helix": "0.0", "turn_pct": "0.3333", "sheet": "0.6667" }, { "id": "aceip0320", "seq": "GVY", "length": "3", "detail": "ND", "source": "ND", "ic50": "<20 mM", "reference": "Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.", "doi": "10.1021\/jf051263l", "pubmedid": "16448176", "mw": "337.37", "pi": "5.52", "charge_ph7": "-0.24", "gravy": "0.8333", "instability": "-18.47", "hydrophobic": "0.3333", "boman": "-1.6133", "helix": "0.0", "turn_pct": "0.3333", "sheet": "0.6667" }, { "id": "aceip0321", "seq": "GVYPH", "length": "5", "detail": "Chicken", "source": "Chicken", "ic50": "2511.89 μM", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "23194537", "mw": "571.63", "pi": "6.74", "charge_ph7": "-0.15", "gravy": "-0.46", "instability": "17.6", "hydrophobic": "0.4", "boman": "-0.77", "helix": "0.0", "turn_pct": "0.4", "sheet": "0.4" }, { "id": "aceip0322", "seq": "GVYPHK", "length": "6", "detail": "Chicken", "source": "Chicken", "ic50": "1.6 μM", "reference": "Isolation and characterization of angiotensin I-converting enzyme inhibitory peptides derived from bonito bowels.", "doi": "10.1271\/bbb.57.1743", "pubmedid": "7764272", "mw": "699.8", "pi": "8.6", "charge_ph7": "0.85", "gravy": "-1.0333", "instability": "55.8", "hydrophobic": "0.3333", "boman": "-0.3783", "helix": "0.1667", "turn_pct": "0.3333", "sheet": "0.3333" }, { "id": "aceip0323", "seq": "GW", "length": "2", "detail": "Chicken", "source": "Chicken", "ic50": "<20 mM", "reference": "Binding of peptide substrates and inhibitors of angiotensin-converting enzyme. Importance of the COOH-terminal dipeptide sequence.; Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Three-dimensional holograph vector of atomic interaction field (3D-HoVAIF): a novel rotation-translation invariant 3D structure descriptor and its applications to peptides.; Antihypertensive effect of peptide-enriched soy sauce-like seasoning and identification of its angiotensin I-converting enzyme inhibitory substances.; QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.; Inhibition strength of short peptides derived from an ACE inhibitory peptide.; Vegetable foods: a cheap source of proteins and peptides with antihypertensive, antioxidant, and other less occurrence bioactivities.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1021\/jf051263l; 10.1002\/psc.892; 10.1021\/jf903261h; 10.1007\/s00894-010-0862-x; 10.1021\/jf202902r; 10.1016\/j.talanta.2012.12.041; 10.1080\/10408398.2012.664829", "pubmedid": "6243277 16448176 17654623 19994857 20941517 21923188 23598136 24915368", "mw": "261.28", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "-0.65", "instability": "66.7", "hydrophobic": "0.5", "boman": "-1.635", "helix": "0.0", "turn_pct": "0.5", "sheet": "0.5" }, { "id": "aceip0324", "seq": "GWAP", "length": "4", "detail": "Milk | Casein", "source": "Milk", "ic50": "3.86 μM", "reference": "Angiotensin I-converting enzyme inhibitory peptides in an alkaline protease hydrolyzate derived from sardine muscle.; Review on the angiotensin-I-converting enzyme (ACE) inhibitor peptides from marine proteins.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1271\/bbb.58.2244; 10.1007\/s12010-012-0024-y; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "7765718 23271625 23871047", "mw": "429.47", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "-0.275", "instability": "48.92", "hydrophobic": "0.75", "boman": "-1.27", "helix": "0.25", "turn_pct": "0.5", "sheet": "0.25" }, { "id": "aceip0325", "seq": "GY", "length": "2", "detail": "Soybean", "source": "Legume", "ic50": "<20 mM", "reference": "The inhibitory actions of dopamine, hydroxyamphetamine and phenylephrine on aqueous humor formation.; Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Quantitative structure-activity relationship study of bitter di- and tri-peptides including relationship with angiotensin I-converting enzyme inhibitory activity.; Three-dimensional holograph vector of atomic interaction field (3D-HoVAIF): a novel rotation-translation invariant 3D structure descriptor and its applications to peptides.; Bioactive peptides in amaranth (Amaranthus hypochondriacus) seed.; Max-E47, a designed minimalist protein that targets the E-box DNA site in vivo and in vitro.; Antihypertensive effect of peptide-enriched soy sauce-like seasoning and identification of its angiotensin I-converting enzyme inhibitory substances.; QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.; Antihypertensive peptides from food proteins: a review.; Review on the angiotensin-I-converting enzyme (ACE) inhibitor peptides from marine proteins.; Vegetable foods: a cheap source of proteins and peptides with antihypertensive, antioxidant, and other less occurrence bioactivities.; Peptides with angiotensin I converting enzyme (ACE) inhibitory activity generated from porcine skeletal muscle proteins by the action of meat-borne Lactobacillus.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1016\/0014-4835(78)90155-0; 10.1021\/jf051263l; 10.1002\/psc.800; 10.1002\/psc.892; 10.1021\/jf072911z; 10.1021\/ja901306q; 10.1021\/jf903261h; 10.1007\/s00894-010-0862-x; 10.1039\/c2fo10192k; 10.1007\/s12010-012-0024-y; 10.1016\/j.talanta.2012.12.041; 10.1016\/j.jprot.2013.06.023; 10.1016\/j.foodchem.2013.05.140; 10.1080\/10408398.2012.664829", "pubmedid": "624327 16448176 17117396 17654623 18211015 19449889 19994857 20941517 22249830 23271625 23598136 23806758 23871047 24915368", "mw": "238.24", "pi": "5.52", "charge_ph7": "-0.24", "gravy": "-0.85", "instability": "-37.45", "hydrophobic": "0.0", "boman": "-0.4", "helix": "0.0", "turn_pct": "0.5", "sheet": "0.5" }, { "id": "aceip0326", "seq": "GYALPHA", "length": "7", "detail": "Carp | Cereals | Pork | Chicken", "source": "Fish | Cereal | Porcine | Chicken", "ic50": "27.3 μM", "reference": "Angiotensin I-converting enzyme inhibitors in autolysates of squid liver and mantle muscle.", "doi": "10.1271\/bbb.60.1353", "pubmedid": "8987556", "mw": "727.81", "pi": "6.74", "charge_ph7": "-0.15", "gravy": "0.1286", "instability": "57.79", "hydrophobic": "0.5714", "boman": "-1.1929", "helix": "0.4286", "turn_pct": "0.2857", "sheet": "0.2857" }, { "id": "aceip0327", "seq": "GYG", "length": "3", "detail": "Fish (Cuttlefish) | Cereals", "source": "Fish | Cereal", "ic50": null, "reference": "Quantitative structure-activity relationship study of bitter di- and tri-peptides including relationship with angiotensin I-converting enzyme inhibitory activity.; QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1002\/psc.800; 10.1007\/s00894-010-0862-x; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "17117396 20941517 23871047", "mw": "295.29", "pi": "5.52", "charge_ph7": "-0.24", "gravy": "-0.7", "instability": "-49.93", "hydrophobic": "0.0", "boman": "-0.58", "helix": "0.0", "turn_pct": "0.6667", "sheet": "0.3333" }, { "id": "aceip0328", "seq": "GYK", "length": "3", "detail": "Tuna", "source": "Fish", "ic50": "160 μM", "reference": "Model of the exofacial substrate-binding site and helical folding of the human Glut1 glucose transporter based on scanning mutagenesis.", "doi": "10.1021\/bi900521n", "pubmedid": "19449892", "mw": "366.41", "pi": "8.59", "charge_ph7": "0.76", "gravy": "-1.8667", "instability": "-21.63", "hydrophobic": "0.0", "boman": "0.26", "helix": "0.3333", "turn_pct": "0.3333", "sheet": "0.3333" }, { "id": "aceip0329", "seq": "GYY", "length": "3", "detail": "Milk (bovine) | Cereals | Pork | Chicken", "source": "Milk | Cereal | Porcine | Chicken", "ic50": null, "reference": "Quantitative structure-activity relationship study of bitter di- and tri-peptides including relationship with angiotensin I-converting enzyme inhibitory activity.; QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1002\/psc.800; 10.1007\/s00894-010-0862-x; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "17117396 20941517 23871047", "mw": "401.41", "pi": "5.52", "charge_ph7": "-0.24", "gravy": "-1.0", "instability": "19.5", "hydrophobic": "0.0", "boman": "-0.22", "helix": "0.0", "turn_pct": "0.3333", "sheet": "0.6667" }, { "id": "aceip0330", "seq": "HERDPTHIKWGD", "length": "12", "detail": "ND", "source": "ND", "ic50": "8 μM", "reference": "Review on the angiotensin-I-converting enzyme (ACE) inhibitor peptides from marine proteins.", "doi": "10.1007\/s12010-012-0024-y", "pubmedid": "23271625", "mw": "1490.58", "pi": "6.02", "charge_ph7": "-1.06", "gravy": "-2.0333", "instability": "30.07", "hydrophobic": "0.25", "boman": "0.2792", "helix": "0.1667", "turn_pct": "0.3333", "sheet": "0.25" }, { "id": "aceip0331", "seq": "HG", "length": "2", "detail": "Fungi (Tricholoma giganteum) | Pholiota adiposa", "source": "Fungi", "ic50": "<20 mM", "reference": "Binding of peptide substrates and inhibitors of angiotensin-converting enzyme. Importance of the COOH-terminal dipeptide sequence.; Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.; Peptides with angiotensin I converting enzyme (ACE) inhibitory activity generated from porcine skeletal muscle proteins by the action of meat-borne Lactobacillus.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1021\/jf051263l; 10.1007\/s00894-010-0862-x; 10.1016\/j.jprot.2013.06.023; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "6243277 16448176 20941517 23806758 23871047", "mw": "212.21", "pi": "6.74", "charge_ph7": "-0.15", "gravy": "-1.8", "instability": "-46.85", "hydrophobic": "0.0", "boman": "0.025", "helix": "0.0", "turn_pct": "0.5", "sheet": "0.0" }, { "id": "aceip0332", "seq": "HGLF", "length": "4", "detail": "Milk | Chicken | Fungi (Hypsizygus marmoreus) | Fungi (Tricholoma giganteum)", "source": "Milk | Chicken | Fungi", "ic50": "0 μM", "reference": "Synthetic peptides corresponding to alpha-lactalbumin and beta-lactoglobulin sequences with angiotensin-I-converting enzyme inhibitory activity.", "doi": "10.1515\/bchm3.1996.377.4.259", "pubmedid": "8737991", "mw": "472.54", "pi": "6.74", "charge_ph7": "-0.15", "gravy": "0.75", "instability": "-18.42", "hydrophobic": "0.5", "boman": "-1.9625", "helix": "0.25", "turn_pct": "0.25", "sheet": "0.5" }, { "id": "aceip0333", "seq": "HHL", "length": "3", "detail": "Milk (bovine) | Garlic | Fish | Carp | Fish (Sea bream scale) | Fish (Sea bream) | Cereals | Pork", "source": "Milk | Plants | Fish | Cereal | Porcine", "ic50": "<20 mM", "reference": "His-His-Leu, an angiotensin I converting enzyme inhibitory peptide derived from Korean soybean paste, exerts antihypertensive activity in vivo.; Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; A molecular keypad lock based on the thiacalix[4]arene of 1,3-alternate conformation.; Vegetable foods: a cheap source of proteins and peptides with antihypertensive, antioxidant, and other less occurrence bioactivities.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1021\/jf001135r; 10.1021\/jf051263l; 10.1021\/ol900845g; 10.1016\/j.talanta.2012.12.041; 10.1080\/10408398.2012.664829", "pubmedid": "11410001 16448176 19449894 23598136 24915368", "mw": "405.45", "pi": "6.92", "charge_ph7": "-0.07", "gravy": "-0.8667", "instability": "6.67", "hydrophobic": "0.3333", "boman": "-0.98", "helix": "0.3333", "turn_pct": "0.0", "sheet": "0.3333" }, { "id": "aceip0334", "seq": "HHT", "length": "3", "detail": "ND", "source": "ND", "ic50": "<20 mM", "reference": "Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.", "doi": "10.1021\/jf051263l", "pubmedid": "16448176", "mw": "393.4", "pi": "6.92", "charge_ph7": "-0.07", "gravy": "-2.3667", "instability": "-18.47", "hydrophobic": "0.0", "boman": "0.7467", "helix": "0.0", "turn_pct": "0.0", "sheet": "0.3333" }, { "id": "aceip0335", "seq": "HIK", "length": "3", "detail": "ND", "source": "ND", "ic50": ">100 μM", "reference": "Potent synthetic analogues of angiotensin-converting enzyme inhibitor derived from Tuna muscle.; Inhibition strength of short peptides derived from an ACE inhibitory peptide.", "doi": "10.1021\/jf202902r", "pubmedid": "1368734 21923188", "mw": "396.48", "pi": "8.76", "charge_ph7": "0.85", "gravy": "-0.8667", "instability": "124.83", "hydrophobic": "0.3333", "boman": "-0.7833", "helix": "0.3333", "turn_pct": "0.0", "sheet": "0.3333" }, { "id": "aceip0336", "seq": "HIKW", "length": "4", "detail": "Synthesized", "source": "Synthesized", "ic50": ">100 μM", "reference": "Potent synthetic analogues of angiotensin-converting enzyme inhibitor derived from Tuna muscle.", "doi": "", "pubmedid": "1368734", "mw": "582.69", "pi": "8.76", "charge_ph7": "0.85", "gravy": "-0.875", "instability": "96.12", "hydrophobic": "0.5", "boman": "-1.17", "helix": "0.25", "turn_pct": "0.0", "sheet": "0.5" }, { "id": "aceip0337", "seq": "HIKWGD", "length": "6", "detail": "Chicken", "source": "Chicken", "ic50": "50 μM", "reference": "Potent synthetic analogues of angiotensin-converting enzyme inhibitor derived from Tuna muscle.", "doi": "", "pubmedid": "1368734", "mw": "754.83", "pi": "6.75", "charge_ph7": "-0.15", "gravy": "-1.2333", "instability": "50.13", "hydrophobic": "0.3333", "boman": "-0.6567", "helix": "0.1667", "turn_pct": "0.3333", "sheet": "0.3333" }, { "id": "aceip0338", "seq": "HIR", "length": "3", "detail": "Sweet-potato", "source": "Potato", "ic50": "<20 mM", "reference": "Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Bioactive peptides in amaranth (Amaranthus hypochondriacus) seed.; Quality and acceptability of a set-type yogurt made from camel milk.", "doi": "10.1021\/jf051263l; 10.1021\/jf072911z; 10.3168\/jds.2008-1408", "pubmedid": "16448176 18211015 19233778", "mw": "424.5", "pi": "9.76", "charge_ph7": "0.85", "gravy": "-1.0667", "instability": "153.13", "hydrophobic": "0.3333", "boman": "-0.4033", "helix": "0.0", "turn_pct": "0.0", "sheet": "0.3333" }, { "id": "aceip0339", "seq": "HIRL", "length": "4", "detail": "Milk (bovine) | Cereals (Wheat) | Pork | Chicken", "source": "Milk | Cereal | Porcine | Chicken", "ic50": null, "reference": "Quality and acceptability of a set-type yogurt made from camel milk.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.3168\/jds.2008-1408; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "19233778 23871047", "mw": "537.66", "pi": "9.76", "charge_ph7": "0.85", "gravy": "0.15", "instability": "117.35", "hydrophobic": "0.5", "boman": "-1.5325", "helix": "0.25", "turn_pct": "0.0", "sheet": "0.5" }, { "id": "aceip0340", "seq": "HK", "length": "2", "detail": "ND", "source": "ND", "ic50": "0 0", "reference": "Application of at-line two-dimensional liquid chromatography-mass spectrometry for identification of small hydrophilic angiotensin I-inhibiting peptides in milk hydrolysates.", "doi": "10.1007\/s00216-008-1990-3", "pubmedid": "18392815", "mw": "283.33", "pi": "8.76", "charge_ph7": "0.85", "gravy": "-3.55", "instability": "123.4", "hydrophobic": "0.0", "boman": "1.285", "helix": "0.5", "turn_pct": "0.0", "sheet": "0.0" }, { "id": "aceip0341", "seq": "HKEMPFPKYPVEPF", "length": "14", "detail": "ND", "source": "ND", "ic50": null, "reference": "Identification of angiotensin-I-converting enzyme inhibitory peptides derived from sodium caseinate hydrolysates produced by Lactobacillus helveticus NCC 2765.", "doi": "10.1021\/jf049510t", "pubmedid": "15537298", "mw": "1746.04", "pi": "6.76", "charge_ph7": "-0.15", "gravy": "-1.0", "instability": "135.19", "hydrophobic": "0.5714", "boman": "-0.3414", "helix": "0.3571", "turn_pct": "0.2857", "sheet": "0.2857" }, { "id": "aceip0342", "seq": "HL", "length": "2", "detail": "ND", "source": "ND", "ic50": "3200 μM", "reference": "Three-dimensional holograph vector of atomic interaction field (3D-HoVAIF): a novel rotation-translation invariant 3D structure descriptor and its applications to peptides.; QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.; Peptides with angiotensin I converting enzyme (ACE) inhibitory activity generated from porcine skeletal muscle proteins by the action of meat-borne Lactobacillus.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1002\/psc.892; 10.1007\/s00894-010-0862-x; 10.1016\/j.jprot.2013.06.023; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "17654623 20941517 23806758 23871047", "mw": "268.31", "pi": "6.74", "charge_ph7": "-0.15", "gravy": "0.3", "instability": "5.0", "hydrophobic": "0.5", "boman": "-1.965", "helix": "0.5", "turn_pct": "0.0", "sheet": "0.5" }, { "id": "aceip0343", "seq": "HLL", "length": "3", "detail": "ND", "source": "ND", "ic50": "<20 mM", "reference": "Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.", "doi": "10.1021\/jf051263l", "pubmedid": "16448176", "mw": "381.47", "pi": "6.74", "charge_ph7": "-0.15", "gravy": "1.4667", "instability": "6.67", "hydrophobic": "0.6667", "boman": "-2.95", "helix": "0.6667", "turn_pct": "0.0", "sheet": "0.6667" }, { "id": "aceip0344", "seq": "HLPLP", "length": "5", "detail": "Milk", "source": "Milk", "ic50": "21.6 mM", "reference": "Inhibition of angiotensin-converting enzyme by synthetic peptide fragments of various beta-caseins.; Identification of angiotensin-I-converting enzyme inhibitory peptides derived from sodium caseinate hydrolysates produced by Lactobacillus helveticus NCC 2765.; Changes in arterial blood pressure after single oral administration of milk-casein-derived peptides in spontaneously hypertensive rats.; The potential role of milk-derived peptides in cardiovascular disease.; Antihypertensive peptides from food proteins: a review.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1021\/jf049510t; 10.1002\/mnfr.200900448; 10.1039\/c1fo10017c; 10.1039\/c2fo10192k; 10.1016\/j.foodchem.2012.09.092", "pubmedid": "1368548 15537298 20397194 21779574 22249830 23194537", "mw": "575.7", "pi": "6.74", "charge_ph7": "-0.15", "gravy": "0.24", "instability": "85.04", "hydrophobic": "0.8", "boman": "-1.77", "helix": "0.4", "turn_pct": "0.4", "sheet": "0.4" }, { "id": "aceip0345", "seq": "HLPLPLL", "length": "7", "detail": "ND", "source": "ND", "ic50": "34.2 ± 2.22 μM", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "23194537", "mw": "802.02", "pi": "6.74", "charge_ph7": "-0.15", "gravy": "1.2571", "instability": "63.6", "hydrophobic": "0.8571", "boman": "-2.67", "helix": "0.5714", "turn_pct": "0.2857", "sheet": "0.5714" }, { "id": "aceip0346", "seq": "HP", "length": "2", "detail": "Synthesized", "source": "Synthesized", "ic50": "0 0", "reference": "Application of at-line two-dimensional liquid chromatography-mass spectrometry for identification of small hydrophilic angiotensin I-inhibiting peptides in milk hydrolysates.; Peptides with angiotensin I converting enzyme (ACE) inhibitory activity generated from porcine skeletal muscle proteins by the action of meat-borne Lactobacillus.", "doi": "10.1007\/s00216-008-1990-3; 10.1016\/j.jprot.2013.06.023", "pubmedid": "18392815 23806758", "mw": "252.27", "pi": "6.74", "charge_ph7": "-0.15", "gravy": "-2.4", "instability": "-9.4", "hydrophobic": "0.5", "boman": "0.495", "helix": "0.0", "turn_pct": "0.5", "sheet": "0.0" }, { "id": "aceip0347", "seq": "HPFA", "length": "4", "detail": "Milk (bovine) | Cereals | Sake", "source": "Milk | Cereal", "ic50": null, "reference": "What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1016\/j.foodchem.2013.05.140", "pubmedid": "23871047", "mw": "470.52", "pi": "6.74", "charge_ph7": "-0.15", "gravy": "-0.05", "instability": "48.45", "hydrophobic": "0.75", "boman": "-0.95", "helix": "0.25", "turn_pct": "0.25", "sheet": "0.25" }, { "id": "aceip0348", "seq": "HPFAQ", "length": "5", "detail": "Cereals | Pork | Chicken", "source": "Cereal | Porcine | Chicken", "ic50": "465 μM", "reference": "Angiotensin-converting enzyme inhibitory activity of peptides derived from caprine kefir.", "doi": "10.3168\/jds.S0022-0302(05)73032-0", "pubmedid": "16162521", "mw": "598.65", "pi": "6.74", "charge_ph7": "-0.15", "gravy": "-0.74", "instability": "40.76", "hydrophobic": "0.6", "boman": "-0.488", "helix": "0.2", "turn_pct": "0.2", "sheet": "0.2" }, { "id": "aceip0349", "seq": "HPFAQTQ", "length": "7", "detail": "Bonito", "source": "Fish", "ic50": null, "reference": "Enterococcus faecalis strains from food, environmental, and clinical origin produce ACE-inhibitory peptides and other bioactive peptides during growth in bovine skim milk.", "doi": "10.1016\/j.ijfoodmicro.2013.06.019", "pubmedid": "23845432", "mw": "827.88", "pi": "6.74", "charge_ph7": "-0.15", "gravy": "-1.1286", "instability": "21.2", "hydrophobic": "0.4286", "boman": "-0.1171", "helix": "0.1429", "turn_pct": "0.1429", "sheet": "0.2857" }, { "id": "aceip0350", "seq": "HPFAQTQSLVYP", "length": "12", "detail": "ND", "source": "ND", "ic50": "26 μM", "reference": "Inhibition of angiotensin-converting enzyme by synthetic peptide fragments of various beta-caseins.; Evaluation of the allergenicity of goat milk, cow milk, and their lactosera in a guinea pig model.", "doi": "10.3168\/jds.2008-1125", "pubmedid": "1368548 19233776", "mw": "1387.54", "pi": "6.74", "charge_ph7": "-0.15", "gravy": "-0.3", "instability": "57.15", "hydrophobic": "0.5", "boman": "-0.7333", "helix": "0.1667", "turn_pct": "0.25", "sheet": "0.4167" }, { "id": "aceip0351", "seq": "HPHPHLSF", "length": "8", "detail": "Yeast", "source": "Fungi", "ic50": "28.9 μM", "reference": "Antihypertensive peptides: production, bioavailability and incorporation into foods.; Antihypertensive peptides from food proteins: a review.", "doi": "10.1016\/j.cis.2010.11.001; 10.1039\/c2fo10192k", "pubmedid": "21185549 22249830", "mw": "971.07", "pi": "7.02", "charge_ph7": "0.02", "gravy": "-0.875", "instability": "1.55", "hydrophobic": "0.5", "boman": "-0.5112", "helix": "0.125", "turn_pct": "0.375", "sheet": "0.25" }, { "id": "aceip0352", "seq": "HPIKH", "length": "5", "detail": "ND", "source": "ND", "ic50": "1258.93 μM", "reference": "Angiotensin I-converting-enzyme-inhibitory and antibacterial peptides from Lactobacillus helveticus PR4 proteinase-hydrolyzed caseins of milk from six species.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1128\/AEM.69.9.5297-5305.2003; 10.1016\/j.foodchem.2012.09.092", "pubmedid": "12957917 23194537", "mw": "630.74", "pi": "8.76", "charge_ph7": "0.93", "gravy": "-1.48", "instability": "-14.74", "hydrophobic": "0.4", "boman": "-0.272", "helix": "0.2", "turn_pct": "0.2", "sheet": "0.2" }, { "id": "aceip0353", "seq": "HQAAGW", "length": "6", "detail": "Fish (Cuttlefish)", "source": "Fish", "ic50": "60 μM", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "23194537", "mw": "668.7", "pi": "6.74", "charge_ph7": "-0.15", "gravy": "-0.7333", "instability": "28.9", "hydrophobic": "0.5", "boman": "-0.7567", "helix": "0.3333", "turn_pct": "0.1667", "sheet": "0.1667" }, { "id": "aceip0354", "seq": "HQG", "length": "3", "detail": "Milk (bovine) | Carp | Anchovy (sauce) | Cereals (Wheat) | Pork | Chicken", "source": "Milk | Fish | Cereal | Porcine | Chicken", "ic50": "<20 mM", "reference": "Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.", "doi": "10.1021\/jf051263l", "pubmedid": "16448176", "mw": "340.34", "pi": "6.74", "charge_ph7": "-0.15", "gravy": "-2.3667", "instability": "6.67", "hydrophobic": "0.0", "boman": "0.47", "helix": "0.0", "turn_pct": "0.3333", "sheet": "0.0" }, { "id": "aceip0355", "seq": "HQIYP", "length": "5", "detail": "ND", "source": "ND", "ic50": "71.5 μM", "reference": "Inhibition of angiotensin-converting enzyme by synthetic peptide fragments of various beta-caseins.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "1368548 23194537", "mw": "656.73", "pi": "6.74", "charge_ph7": "-0.15", "gravy": "-1.02", "instability": "32.68", "hydrophobic": "0.4", "boman": "-0.486", "helix": "0.0", "turn_pct": "0.2", "sheet": "0.4" }, { "id": "aceip0356", "seq": "HQK", "length": "3", "detail": "Chicken", "source": "Chicken", "ic50": null, "reference": "Angiotensin I-converting-enzyme-inhibitory and antibacterial peptides from Lactobacillus helveticus PR4 proteinase-hydrolyzed caseins of milk from six species.", "doi": "10.1128\/AEM.69.9.5297-5305.2003", "pubmedid": "12957917", "mw": "411.46", "pi": "8.76", "charge_ph7": "0.85", "gravy": "-3.5333", "instability": "6.67", "hydrophobic": "0.0", "boman": "1.31", "helix": "0.3333", "turn_pct": "0.0", "sheet": "0.0" }, { "id": "aceip0357", "seq": "HWTTQR", "length": "6", "detail": "Milk (bovine) | Carp | Cereals | pea | Pork | Chicken", "source": "Milk | Fish | Cereal | Legume | Porcine | Chicken", "ic50": "1.44 mg\/ml", "reference": "Review on the angiotensin-I-converting enzyme (ACE) inhibitor peptides from marine proteins.", "doi": "10.1007\/s12010-012-0024-y", "pubmedid": "23271625", "mw": "827.89", "pi": "9.76", "charge_ph7": "0.85", "gravy": "-2.25", "instability": "-34.08", "hydrophobic": "0.1667", "boman": "0.5433", "helix": "0.0", "turn_pct": "0.0", "sheet": "0.5" }, { "id": "aceip0358", "seq": "HY", "length": "2", "detail": "ND", "source": "ND", "ic50": "<20 mM", "reference": "Structure and activity of angiotensin I converting enzyme inhibitory peptides from sake and sake lees.; Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Bioactive peptides in amaranth (Amaranthus hypochondriacus) seed.; Antihypertensive peptides from food proteins: a review.; Vegetable foods: a cheap source of proteins and peptides with antihypertensive, antioxidant, and other less occurrence bioactivities.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1271\/bbb.58.1767; 10.1021\/jf051263l; 10.1021\/jf072911z; 10.1039\/c2fo10192k; 10.1016\/j.talanta.2012.12.041; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "7765503 16448176 18211015 22249830 23598136 23871047", "mw": "318.33", "pi": "6.74", "charge_ph7": "-0.15", "gravy": "-2.25", "instability": "224.7", "hydrophobic": "0.0", "boman": "0.565", "helix": "0.0", "turn_pct": "0.0", "sheet": "0.5" }, { "id": "aceip0359", "seq": "IA", "length": "2", "detail": "Milk", "source": "Milk", "ic50": "<20 mM", "reference": "Antihypertensive peptides derived from milk proteins.; Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Three-dimensional holograph vector of atomic interaction field (3D-HoVAIF): a novel rotation-translation invariant 3D structure descriptor and its applications to peptides.; Vegetable foods: a cheap source of proteins and peptides with antihypertensive, antioxidant, and other less occurrence bioactivities.; Peptides with angiotensin I converting enzyme (ACE) inhibitory activity generated from porcine skeletal muscle proteins by the action of meat-borne Lactobacillus.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1002\/(SICI)1521-3803(19990601)43:3<159::AID-FOOD159>3.0.CO;2-R; 10.1021\/jf051263l; 10.1002\/psc.892; 10.1016\/j.talanta.2012.12.041; 10.1016\/j.jprot.2013.06.023; 10.1080\/10408398.2012.664829", "pubmedid": "10399348 16448176 17654623 23598136 23806758 24915368", "mw": "202.25", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "3.15", "instability": "5.0", "hydrophobic": "1.0", "boman": "-3.365", "helix": "0.5", "turn_pct": "0.0", "sheet": "0.5" }, { "id": "aceip0360", "seq": "IAE", "length": "3", "detail": "Milk", "source": "Milk", "ic50": "34.7 μM", "reference": "Angiotensin converting enzyme inhibitory peptides derived from food proteins: biochemistry, bioactivity and production.; Review on the angiotensin-I-converting enzyme (ACE) inhibitor peptides from marine proteins.; Vegetable foods: a cheap source of proteins and peptides with antihypertensive, antioxidant, and other less occurrence bioactivities.", "doi": "10.2174\/138161207780363068; 10.1007\/s12010-012-0024-y; 10.1016\/j.talanta.2012.12.041", "pubmedid": "17430180 23271625 23598136", "mw": "331.36", "pi": "4.6", "charge_ph7": "-1.23", "gravy": "0.9333", "instability": "6.67", "hydrophobic": "0.6667", "boman": "-1.6967", "helix": "0.6667", "turn_pct": "0.0", "sheet": "0.3333" }, { "id": "aceip0361", "seq": "IAIP", "length": "4", "detail": "Yeast", "source": "Fungi", "ic50": "470 μM", "reference": "Inhibition of angiotensin-converting enzyme by synthetic peptide fragments of human kappa-casein.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1016\/j.foodchem.2013.05.140", "pubmedid": "1368540 23871047", "mw": "412.52", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "2.3", "instability": "0.3", "hydrophobic": "1.0", "boman": "-2.9125", "helix": "0.25", "turn_pct": "0.25", "sheet": "0.5" }, { "id": "aceip0362", "seq": "IAIPP", "length": "5", "detail": "Hemoglobulin | Pork", "source": "Synthesized | Porcine", "ic50": "600 μM", "reference": "Inhibition of angiotensin-converting enzyme by synthetic peptide fragments of human kappa-casein.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "1368540 23194537", "mw": "509.64", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "1.52", "instability": "40.76", "hydrophobic": "1.0", "boman": "-2.33", "helix": "0.2", "turn_pct": "0.4", "sheet": "0.4" }, { "id": "aceip0363", "seq": "IAK", "length": "3", "detail": "ND", "source": "ND", "ic50": "10.0-848.0 μM", "reference": "Identification of novel angiotensin-converting enzyme-inhibitory peptides from ovine milk proteins by CE-MS and chromatographic techniques.; Changes in arterial blood pressure after single oral administration of milk-casein-derived peptides in spontaneously hypertensive rats.; Antihypertensive peptides: production, bioavailability and incorporation into foods.; Antihypertensive peptides from food proteins: a review.; Peptides with angiotensin I converting enzyme (ACE) inhibitory activity generated from porcine skeletal muscle proteins by the action of meat-borne Lactobacillus.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1002\/elps.200700324; 10.1002\/mnfr.200900448; 10.1016\/j.cis.2010.11.001; 10.1039\/c2fo10192k; 10.1016\/j.jprot.2013.06.023; 10.1080\/10408398.2012.664829", "pubmedid": "17948260 20397194 21185549 22249830 23806758 24915368", "mw": "330.42", "pi": "8.75", "charge_ph7": "0.76", "gravy": "0.8", "instability": "6.67", "hydrophobic": "0.6667", "boman": "-1.7167", "helix": "0.6667", "turn_pct": "0.0", "sheet": "0.3333" }, { "id": "aceip0364", "seq": "IAP", "length": "3", "detail": "Milk (whey) | Milk (cheese whey) | Amaranth | Synthesized | Cereals | Chicken connectin", "source": "Milk | Plants | Synthesized | Cereal | Chicken", "ic50": "<20 mM", "reference": "Isolation and characterization of angiotensin I-converting enzyme inhibitory peptides from wheat gliadin hydrolysate.; Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Vegetable foods: a cheap source of proteins and peptides with antihypertensive, antioxidant, and other less occurrence bioactivities.; Comparison of analytical methods to assay inhibitors of angiotensin I-converting enzyme.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1002\/food.200390081; 10.1021\/jf051263l; 10.1016\/j.talanta.2012.12.041; 10.1016\/j.foodchem.2013.06.048; 10.1080\/10408398.2012.664829", "pubmedid": "14609094 16448176 23598136 23993489 24915368", "mw": "299.37", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "1.5667", "instability": "70.87", "hydrophobic": "1.0", "boman": "-2.2433", "helix": "0.3333", "turn_pct": "0.3333", "sheet": "0.3333" }, { "id": "aceip0365", "seq": "IAPG", "length": "4", "detail": "ND", "source": "ND", "ic50": "11.4 μM", "reference": "Angiotensin converting enzyme inhibitory peptides derived from food proteins: biochemistry, bioactivity and production.; Review on the angiotensin-I-converting enzyme (ACE) inhibitor peptides from marine proteins.; Vegetable foods: a cheap source of proteins and peptides with antihypertensive, antioxidant, and other less occurrence bioactivities.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.2174\/138161207780363068; 10.1007\/s12010-012-0024-y; 10.1016\/j.talanta.2012.12.041; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "17430180 23271625 23598136 23871047", "mw": "356.42", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "1.075", "instability": "55.65", "hydrophobic": "0.75", "boman": "-1.9175", "helix": "0.25", "turn_pct": "0.5", "sheet": "0.25" }, { "id": "aceip0366", "seq": "IAQ", "length": "3", "detail": "Cereals", "source": "Cereal", "ic50": "<20 mM", "reference": "Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.", "doi": "10.1021\/jf051263l", "pubmedid": "16448176", "mw": "330.38", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "0.9333", "instability": "6.67", "hydrophobic": "0.6667", "boman": "-1.79", "helix": "0.3333", "turn_pct": "0.0", "sheet": "0.3333" }, { "id": "aceip0367", "seq": "IASGEPTSTPT", "length": "11", "detail": "Milk (bovine) | Carp | Cereals | Pork", "source": "Milk | Fish | Cereal | Porcine", "ic50": null, "reference": "Casein fermentate of Lactobacillus animalis DPC6134 contains a range of novel propeptide angiotensin-converting enzyme inhibitors.", "doi": "10.1128\/AEM.00096-07", "pubmedid": "17483275", "mw": "1060.11", "pi": "4.05", "charge_ph7": "-1.24", "gravy": "-0.4091", "instability": "19.75", "hydrophobic": "0.3636", "boman": "-0.3245", "helix": "0.1818", "turn_pct": "0.4545", "sheet": "0.3636" }, { "id": "aceip0368", "seq": "IASGEPTSTPTEE", "length": "13", "detail": "Milk (bovine) | Milk (whey)", "source": "Milk", "ic50": null, "reference": "Casein fermentate of Lactobacillus animalis DPC6134 contains a range of novel propeptide angiotensin-converting enzyme inhibitors.", "doi": "10.1128\/AEM.00096-07", "pubmedid": "17483275", "mw": "1318.34", "pi": "4.05", "charge_ph7": "-3.23", "gravy": "-0.8846", "instability": "58.14", "hydrophobic": "0.3077", "boman": "-0.0223", "helix": "0.3077", "turn_pct": "0.3846", "sheet": "0.3077" }, { "id": "aceip0369", "seq": "IASGEPTSTPTTEA", "length": "14", "detail": "Cereals", "source": "Cereal", "ic50": null, "reference": "Casein fermentate of Lactobacillus animalis DPC6134 contains a range of novel propeptide angiotensin-converting enzyme inhibitors.", "doi": "10.1128\/AEM.00096-07", "pubmedid": "17483275", "mw": "1361.41", "pi": "4.05", "charge_ph7": "-2.23", "gravy": "-0.4929", "instability": "31.41", "hydrophobic": "0.3571", "boman": "-0.2486", "helix": "0.2857", "turn_pct": "0.3571", "sheet": "0.3571" }, { "id": "aceip0370", "seq": "IAV", "length": "3", "detail": "ND", "source": "ND", "ic50": "153.4 μM", "reference": "Analysis of novel angiotensin I-converting enzyme inhibitory peptides from enzymatic hydrolysates of cuttlefish (Sepia officinalis) muscle proteins.; Review on the angiotensin-I-converting enzyme (ACE) inhibitor peptides from marine proteins.", "doi": "10.1021\/jf904300q; 10.1007\/s12010-012-0024-y", "pubmedid": "20180574 23271625", "mw": "301.38", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "3.5", "instability": "6.67", "hydrophobic": "1.0", "boman": "-3.59", "helix": "0.3333", "turn_pct": "0.0", "sheet": "0.6667" }, { "id": "aceip0371", "seq": "IAY", "length": "3", "detail": "ND", "source": "ND", "ic50": "<20 mM", "reference": "Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.", "doi": "10.1021\/jf051263l", "pubmedid": "16448176", "mw": "365.42", "pi": "5.52", "charge_ph7": "-0.24", "gravy": "1.6667", "instability": "6.67", "hydrophobic": "0.6667", "boman": "-2.1967", "helix": "0.3333", "turn_pct": "0.0", "sheet": "0.6667" }, { "id": "aceip0372", "seq": "IAYKP", "length": "5", "detail": "Synthesized | Fish (Alaska pollack)", "source": "Synthesized | Fish", "ic50": "2.93 μM", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "23194537", "mw": "590.71", "pi": "8.59", "charge_ph7": "0.76", "gravy": "-0.1", "instability": "-7.08", "hydrophobic": "0.6", "boman": "-1.002", "helix": "0.4", "turn_pct": "0.2", "sheet": "0.4" }, { "id": "aceip0373", "seq": "IAYKPAG", "length": "7", "detail": "Chicken", "source": "Chicken", "ic50": "4.17 μM", "reference": "Isolation and antihypertensive effect of angiotensin I-converting enzyme (ACE) inhibitory peptides from spinach Rubisco.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1021\/jf026186y; 10.1016\/j.foodchem.2012.09.092", "pubmedid": "12903942 23194537", "mw": "718.84", "pi": "8.59", "charge_ph7": "0.76", "gravy": "0.1286", "instability": "25.31", "hydrophobic": "0.5714", "boman": "-1.1086", "helix": "0.4286", "turn_pct": "0.2857", "sheet": "0.2857" }, { "id": "aceip0374", "seq": "IE", "length": "2", "detail": "Synthesized | Bovine", "source": "Synthesized | Bovine", "ic50": "0 0", "reference": "Three-dimensional holograph vector of atomic interaction field (3D-HoVAIF): a novel rotation-translation invariant 3D structure descriptor and its applications to peptides.; Application of at-line two-dimensional liquid chromatography-mass spectrometry for identification of small hydrophilic angiotensin I-inhibiting peptides in milk hydrolysates.; Peptides with angiotensin I converting enzyme (ACE) inhibitory activity generated from porcine skeletal muscle proteins by the action of meat-borne Lactobacillus.", "doi": "10.1002\/psc.892; 10.1007\/s00216-008-1990-3; 10.1016\/j.jprot.2013.06.023", "pubmedid": "17654623 18392815 23806758", "mw": "260.29", "pi": "4.6", "charge_ph7": "-1.23", "gravy": "0.5", "instability": "224.7", "hydrophobic": "0.5", "boman": "-1.64", "helix": "0.5", "turn_pct": "0.0", "sheet": "0.5" }, { "id": "aceip0375", "seq": "IELPLG", "length": "6", "detail": "Royal jelly", "source": "Insect", "ic50": "72.44 μM", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "23194537", "mw": "640.77", "pi": "4.05", "charge_ph7": "-1.24", "gravy": "1.1", "instability": "113.67", "hydrophobic": "0.6667", "boman": "-2.3433", "helix": "0.5", "turn_pct": "0.3333", "sheet": "0.5" }, { "id": "aceip0376", "seq": "IEP", "length": "3", "detail": "Milk (bovine) | Cereals (Wheat) | Pork", "source": "Milk | Cereal | Porcine", "ic50": "<10 μM", "reference": "Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.", "doi": "10.1021\/jf051263l", "pubmedid": "16448176", "mw": "357.4", "pi": "4.05", "charge_ph7": "-1.24", "gravy": "-0.2", "instability": "217.33", "hydrophobic": "0.6667", "boman": "-1.0933", "helix": "0.3333", "turn_pct": "0.3333", "sheet": "0.3333" }, { "id": "aceip0377", "seq": "IEW", "length": "3", "detail": "Cereals", "source": "Cereal", "ic50": "104 μM", "reference": "Arachin derived peptides as selective angiotensin I-converting enzyme (ACE) inhibitors: structure-activity relationship.", "doi": "10.1016\/j.peptides.2010.02.022", "pubmedid": "20214946", "mw": "446.5", "pi": "4.05", "charge_ph7": "-1.24", "gravy": "0.0333", "instability": "103.03", "hydrophobic": "0.6667", "boman": "-1.87", "helix": "0.3333", "turn_pct": "0.0", "sheet": "0.6667" }, { "id": "aceip0378", "seq": "IEY", "length": "3", "detail": "Milk (bovine) | Bonito | Fish (Alaska pollack) | Anchovy (sauce) | Fish (Sardine fermented sauce) | Cereals | pea | Pork", "source": "Milk | Fish | Cereal | Legume | Porcine", "ic50": "<10 μM", "reference": "Arachin derived peptides as selective angiotensin I-converting enzyme (ACE) inhibitors: structure-activity relationship.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1016\/j.peptides.2010.02.022; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "20214946 23871047", "mw": "423.46", "pi": "4.05", "charge_ph7": "-1.24", "gravy": "-0.1", "instability": "153.13", "hydrophobic": "0.3333", "boman": "-1.0467", "helix": "0.3333", "turn_pct": "0.0", "sheet": "0.6667" }, { "id": "aceip0379", "seq": "IF", "length": "2", "detail": "Milk | Gelatin", "source": "Milk | Animal", "ic50": "<20 mM", "reference": "Binding of peptide substrates and inhibitors of angiotensin-converting enzyme. Importance of the COOH-terminal dipeptide sequence.; Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Quantitative structure-activity relationship study of bitter di- and tri-peptides including relationship with angiotensin I-converting enzyme inhibitory activity.; Three-dimensional holograph vector of atomic interaction field (3D-HoVAIF): a novel rotation-translation invariant 3D structure descriptor and its applications to peptides.; QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.; Vegetable foods: a cheap source of proteins and peptides with antihypertensive, antioxidant, and other less occurrence bioactivities.; Peptides with angiotensin I converting enzyme (ACE) inhibitory activity generated from porcine skeletal muscle proteins by the action of meat-borne Lactobacillus.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1021\/jf051263l; 10.1002\/psc.800; 10.1002\/psc.892; 10.1007\/s00894-010-0862-x; 10.1016\/j.talanta.2012.12.041; 10.1016\/j.jprot.2013.06.023; 10.1016\/j.foodchem.2013.05.140; 10.1080\/10408398.2012.664829", "pubmedid": "6243277 16448176 17117396 17654623 20941517 23598136 23806758 23871047 24915368", "mw": "278.35", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "3.65", "instability": "5.0", "hydrophobic": "1.0", "boman": "-3.95", "helix": "0.0", "turn_pct": "0.0", "sheet": "1.0" }, { "id": "aceip0380", "seq": "IFL", "length": "3", "detail": "Milk (bovine)", "source": "Milk", "ic50": "<20 mM", "reference": "Angiotensin I-converting enzyme inhibitory peptides isolated from tofuyo fermented soybean food.; Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Vegetable foods: a cheap source of proteins and peptides with antihypertensive, antioxidant, and other less occurrence bioactivities.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.; Glycinyl-histidinyl-serine (GHS), a novel rapeseed protein-derived peptide has blood pressure-lowering effect in spontaneously hypertensive rats.", "doi": "10.1271\/bbb.67.1278; 10.1021\/jf051263l; 10.1016\/j.talanta.2012.12.041; 10.1016\/j.foodchem.2013.05.140; 10.1021\/jf400865m", "pubmedid": "12843654 16448176 23598136 23871047 23919612", "mw": "391.5", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "3.7", "instability": "6.67", "hydrophobic": "1.0", "boman": "-4.2733", "helix": "0.3333", "turn_pct": "0.0", "sheet": "1.0" }, { "id": "aceip0381", "seq": "IFVPAF", "length": "6", "detail": "Gelatin", "source": "Animal", "ic50": "3.4 μM", "reference": "Analysis of novel angiotensin-I-converting enzyme inhibitory peptides from protease-hydrolyzed marine shrimp Acetes chinensis.; Review on the angiotensin-I-converting enzyme (ACE) inhibitor peptides from marine proteins.; Rational design of angiotensin-I-converting enzyme inhibitory peptides by integrating in silico modeling and an in vitro assay.", "doi": "10.1002\/psc.789; 10.1007\/s12010-012-0024-y; 10.1002\/cmdc.201300132", "pubmedid": "16981241 23271625 23740817", "mw": "692.84", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "2.4167", "instability": "72.53", "hydrophobic": "1.0", "boman": "-2.7883", "helix": "0.1667", "turn_pct": "0.1667", "sheet": "0.6667" }, { "id": "aceip0382", "seq": "IG", "length": "2", "detail": "Pangasius catfish", "source": "Fish", "ic50": "<20 mM", "reference": "Binding of peptide substrates and inhibitors of angiotensin-converting enzyme. Importance of the COOH-terminal dipeptide sequence.; Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Three-dimensional holograph vector of atomic interaction field (3D-HoVAIF): a novel rotation-translation invariant 3D structure descriptor and its applications to peptides.; QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.; Peptides with angiotensin I converting enzyme (ACE) inhibitory activity generated from porcine skeletal muscle proteins by the action of meat-borne Lactobacillus.", "doi": "10.1021\/jf051263l; 10.1002\/psc.892; 10.1007\/s00894-010-0862-x; 10.1016\/j.jprot.2013.06.023", "pubmedid": "6243277 16448176 17654623 20941517 23806758", "mw": "188.22", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "2.05", "instability": "5.0", "hydrophobic": "0.5", "boman": "-2.93", "helix": "0.0", "turn_pct": "0.5", "sheet": "0.5" }, { "id": "aceip0383", "seq": "IGGSI", "length": "5", "detail": "Sweet-potato", "source": "Potato", "ic50": "46.56>1000 μM", "reference": "Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1080\/10408398.2012.664829", "pubmedid": "24915368", "mw": "445.51", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "1.48", "instability": "32.68", "hydrophobic": "0.4", "boman": "-2.176", "helix": "0.0", "turn_pct": "0.6", "sheet": "0.4" }, { "id": "aceip0384", "seq": "IGNTLI", "length": "6", "detail": "Casein", "source": "Milk", "ic50": null, "reference": "Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1080\/10408398.2012.664829", "pubmedid": "24915368", "mw": "629.75", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "1.3667", "instability": "-19.97", "hydrophobic": "0.5", "boman": "-2.3033", "helix": "0.1667", "turn_pct": "0.3333", "sheet": "0.6667" }, { "id": "aceip0385", "seq": "IGSENSEKTTMP", "length": "12", "detail": "ND", "source": "ND", "ic50": "773 μM", "reference": "Casein fermentate of Lactobacillus animalis DPC6134 contains a range of novel propeptide angiotensin-converting enzyme inhibitors.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1128\/AEM.00096-07; 10.1016\/j.foodchem.2012.09.092", "pubmedid": "17483275 23194537", "mw": "1293.4", "pi": "4.53", "charge_ph7": "-1.24", "gravy": "-1.0833", "instability": "77.88", "hydrophobic": "0.25", "boman": "0.0392", "helix": "0.3333", "turn_pct": "0.4167", "sheet": "0.25" }, { "id": "aceip0386", "seq": "IHAQQKEP", "length": "8", "detail": "Milk (bovine)", "source": "Milk", "ic50": null, "reference": "Enterococcus faecalis strains from food, environmental, and clinical origin produce ACE-inhibitory peptides and other bioactive peptides during growth in bovine skim milk.", "doi": "10.1016\/j.ijfoodmicro.2013.06.019", "pubmedid": "23845432", "mw": "950.05", "pi": "6.75", "charge_ph7": "-0.15", "gravy": "-1.6125", "instability": "72.33", "hydrophobic": "0.375", "boman": "0.025", "helix": "0.375", "turn_pct": "0.125", "sheet": "0.125" }, { "id": "aceip0387", "seq": "IHPF", "length": "4", "detail": "Milk (bovine)", "source": "Milk", "ic50": "11.6 μM", "reference": "Determination of endogenous peptides with in vitro ACE inhibitory activity in normotensive human plasma by the fluorometric HPLC method.", "doi": "10.1271\/bbb.61.1052", "pubmedid": "9214772", "mw": "512.6", "pi": "6.74", "charge_ph7": "-0.15", "gravy": "0.625", "instability": "79.3", "hydrophobic": "0.75", "boman": "-1.7275", "helix": "0.0", "turn_pct": "0.25", "sheet": "0.5" }, { "id": "aceip0388", "seq": "IHPFAQTQSLVYP", "length": "13", "detail": "Fish | Fish (Alaska pollack) | hydrolysate | Bovine", "source": "Fish | Bovine", "ic50": "19 μM", "reference": "Inhibition of angiotensin-converting enzyme by synthetic peptide fragments of various beta-caseins.; Evaluation of the allergenicity of goat milk, cow milk, and their lactosera in a guinea pig model.", "doi": "10.3168\/jds.2008-1125", "pubmedid": "1368548 19233776", "mw": "1500.7", "pi": "6.74", "charge_ph7": "-0.15", "gravy": "0.0692", "instability": "63.02", "hydrophobic": "0.5385", "boman": "-1.0554", "helix": "0.1538", "turn_pct": "0.2308", "sheet": "0.4615" }, { "id": "aceip0389", "seq": "II", "length": "2", "detail": "Squid", "source": "Animal", "ic50": null, "reference": "Three-dimensional holograph vector of atomic interaction field (3D-HoVAIF): a novel rotation-translation invariant 3D structure descriptor and its applications to peptides.", "doi": "10.1002\/psc.892", "pubmedid": "17654623", "mw": "244.33", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "4.5", "instability": "5.0", "hydrophobic": "1.0", "boman": "-4.92", "helix": "0.0", "turn_pct": "0.0", "sheet": "1.0" }, { "id": "aceip0390", "seq": "IIAMK", "length": "5", "detail": "Fish | Fish (Alaska pollack)", "source": "Fish", "ic50": "498 μM", "reference": "A variant peptide of buffalo colostrum β-lactoglobulin inhibits angiotensin I-converting enzyme activity.", "doi": "10.1016\/j.ejmech.2012.03.057", "pubmedid": "22541393", "mw": "574.78", "pi": "8.75", "charge_ph7": "0.76", "gravy": "1.76", "instability": "8.0", "hydrophobic": "0.8", "boman": "-2.484", "helix": "0.6", "turn_pct": "0.0", "sheet": "0.4" }, { "id": "aceip0391", "seq": "IKP", "length": "3", "detail": "Cereals (Buckwheat)", "source": "Cereal", "ic50": "<20 mM", "reference": "Peptide inhibitors for angiotensin I-converting enzyme from thermolysin digest of dried bonito.; Angiotensin I-converting enzyme inhibitory peptides derived from bonito bowels autolysate.; Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Bioactive peptides in amaranth (Amaranthus hypochondriacus) seed.; ACE inhibitory tetrapeptides from Amaranthus hypochondriacus 11S globulin.; Inhibition strength of short peptides derived from an ACE inhibitory peptide.; Antihypertensive peptides from food proteins: a review.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.; Comparison of analytical methods to assay inhibitors of angiotensin I-converting enzyme.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1271\/bbb.56.1541; 10.1271\/bbb.57.695; 10.1021\/jf051263l; 10.1021\/jf072911z; 10.1016\/j.phytochem.2009.04.006; 10.1021\/jf202902r; 10.1039\/c2fo10192k; 10.1016\/j.foodchem.2013.05.140; 10.1016\/j.foodchem.2013.06.048; 10.1080\/10408398.2012.664829", "pubmedid": "1369054 7763772 16448176 18211015 19443002 21923188 22249830 23871047 23993489 24915368", "mw": "356.46", "pi": "8.75", "charge_ph7": "0.76", "gravy": "-0.3333", "instability": "-46.77", "hydrophobic": "0.6667", "boman": "-1.1133", "helix": "0.3333", "turn_pct": "0.3333", "sheet": "0.3333" }, { "id": "aceip0392", "seq": "IKPLDY", "length": "6", "detail": "Bovine", "source": "Bovine", "ic50": "42.66 μM", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "23194537", "mw": "747.88", "pi": "5.83", "charge_ph7": "-0.24", "gravy": "-0.3333", "instability": "-18.38", "hydrophobic": "0.5", "boman": "-1.0733", "helix": "0.3333", "turn_pct": "0.3333", "sheet": "0.5" }, { "id": "aceip0393", "seq": "IKPLNY", "length": "6", "detail": "Bovine", "source": "Bovine", "ic50": "43 μM", "reference": "Peptide inhibitors for angiotensin I-converting enzyme from thermolysin digest of dried bonito.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.; Review on the angiotensin-I-converting enzyme (ACE) inhibitor peptides from marine proteins.", "doi": "10.1271\/bbb.56.1541; 10.1016\/j.foodchem.2012.09.092; 10.1007\/s12010-012-0024-y", "pubmedid": "1369054 23194537 23271625", "mw": "746.89", "pi": "8.59", "charge_ph7": "0.76", "gravy": "-0.3333", "instability": "-18.38", "hydrophobic": "0.5", "boman": "-1.0833", "helix": "0.3333", "turn_pct": "0.3333", "sheet": "0.5" }, { "id": "aceip0394", "seq": "IKPVQ", "length": "5", "detail": "Bovine", "source": "Bovine", "ic50": "33.5 μM", "reference": "Rational design of angiotensin-I-converting enzyme inhibitory peptides by integrating in silico modeling and an in vitro assay.", "doi": "10.1002\/cmdc.201300132", "pubmedid": "23740817", "mw": "583.72", "pi": "8.75", "charge_ph7": "0.76", "gravy": "-0.06", "instability": "14.46", "hydrophobic": "0.6", "boman": "-1.204", "helix": "0.2", "turn_pct": "0.2", "sheet": "0.4" }, { "id": "aceip0395", "seq": "IKW", "length": "3", "detail": "Fish | Catfish | Fish (Catfish)", "source": "Fish", "ic50": "<20 mM", "reference": "ACE inhibitory peptides derived from enzymatic hydrolysates of animal muscle protein: a review.; Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Angiotensin I-converting enzyme-inhibitory peptides obtained from chicken collagen hydrolysate.; Inhibition strength of short peptides derived from an ACE inhibitory peptide.; Antihypertensive peptides from food proteins: a review.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1021\/jf0508908; 10.1021\/jf051263l; 10.1021\/jf072669w; 10.1021\/jf202902r; 10.1039\/c2fo10192k; 10.1080\/10408398.2012.664829", "pubmedid": "16218651 16448176 18808143 21923188 22249830 24915368", "mw": "445.56", "pi": "8.75", "charge_ph7": "0.76", "gravy": "-0.1", "instability": "-21.63", "hydrophobic": "0.6667", "boman": "-1.89", "helix": "0.3333", "turn_pct": "0.0", "sheet": "0.6667" }, { "id": "aceip0396", "seq": "IKWGD", "length": "5", "detail": "Pork", "source": "Porcine", "ic50": ">100 μM", "reference": "Potent synthetic analogues of angiotensin-converting enzyme inhibitor derived from Tuna muscle.", "doi": "", "pubmedid": "1368734", "mw": "617.69", "pi": "6.09", "charge_ph7": "-0.24", "gravy": "-0.84", "instability": "-29.72", "hydrophobic": "0.4", "boman": "-0.986", "helix": "0.2", "turn_pct": "0.4", "sheet": "0.4" }, { "id": "aceip0397", "seq": "IKY", "length": "3", "detail": "Fungi (P.Cystidiosus)", "source": "Fungi", "ic50": "<20 mM", "reference": "Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Arachin derived peptides as selective angiotensin I-converting enzyme (ACE) inhibitors: structure-activity relationship.", "doi": "10.1021\/jf051263l; 10.1016\/j.peptides.2010.02.022", "pubmedid": "16448176 20214946", "mw": "422.52", "pi": "8.59", "charge_ph7": "0.76", "gravy": "-0.2333", "instability": "-21.63", "hydrophobic": "0.3333", "boman": "-1.0667", "helix": "0.3333", "turn_pct": "0.0", "sheet": "0.6667" }, { "id": "aceip0398", "seq": "IL", "length": "2", "detail": "Milk (bovine) | Cereals | Bovine", "source": "Milk | Cereal | Bovine", "ic50": "<20 mM", "reference": "Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Quantitative structure-activity relationship study of bitter di- and tri-peptides including relationship with angiotensin I-converting enzyme inhibitory activity.; Three-dimensional holograph vector of atomic interaction field (3D-HoVAIF): a novel rotation-translation invariant 3D structure descriptor and its applications to peptides.", "doi": "10.1021\/jf051263l; 10.1002\/psc.800; 10.1002\/psc.892", "pubmedid": "16448176 17117396 17654623", "mw": "244.33", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "4.15", "instability": "101.3", "hydrophobic": "1.0", "boman": "-4.92", "helix": "0.5", "turn_pct": "0.0", "sheet": "1.0" }, { "id": "aceip0399", "seq": "ILP", "length": "3", "detail": "Bovine", "source": "Bovine", "ic50": "<20 mM", "reference": "Inhibition of angiotensin-converting enzyme by synthetic peptide fragments of various beta-caseins.; Bioactive peptides in amaranth (Amaranthus hypochondriacus) seed.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1021\/jf072911z; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "1368548 18211015 23871047", "mw": "341.45", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "2.2333", "instability": "135.07", "hydrophobic": "1.0", "boman": "-3.28", "helix": "0.3333", "turn_pct": "0.3333", "sheet": "0.6667" }, { "id": "aceip0400", "seq": "IMY", "length": "3", "detail": "Casein", "source": "Milk", "ic50": "<20 mM", "reference": "Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1021\/jf051263l; 10.1080\/10408398.2012.664829", "pubmedid": "16448176 24915368", "mw": "425.54", "pi": "5.52", "charge_ph7": "-0.24", "gravy": "1.7", "instability": "85.6", "hydrophobic": "0.6667", "boman": "-2.3767", "helix": "0.3333", "turn_pct": "0.0", "sheet": "0.6667" }, { "id": "aceip0401", "seq": "IN", "length": "2", "detail": "Cheese (Manchego cheese)", "source": "Milk", "ic50": null, "reference": "Three-dimensional holograph vector of atomic interaction field (3D-HoVAIF): a novel rotation-translation invariant 3D structure descriptor and its applications to peptides.", "doi": "10.1002\/psc.892", "pubmedid": "17654623", "mw": "245.28", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "0.5", "instability": "5.0", "hydrophobic": "0.5", "boman": "-1.65", "helix": "0.0", "turn_pct": "0.5", "sheet": "0.5" }, { "id": "aceip0402", "seq": "INDPF", "length": "5", "detail": "ND", "source": "ND", "ic50": "46.56>1000 μM", "reference": "Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1080\/10408398.2012.664829", "pubmedid": "24915368", "mw": "604.65", "pi": "4.05", "charge_ph7": "-1.24", "gravy": "-0.26", "instability": "46.52", "hydrophobic": "0.6", "boman": "-0.92", "helix": "0.0", "turn_pct": "0.6", "sheet": "0.4" }, { "id": "aceip0403", "seq": "INSQ", "length": "4", "detail": "Casein", "source": "Milk", "ic50": "4-628 μM", "reference": "Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1080\/10408398.2012.664829", "pubmedid": "24915368", "mw": "460.48", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "-0.825", "instability": "55.65", "hydrophobic": "0.25", "boman": "-0.275", "helix": "0.0", "turn_pct": "0.5", "sheet": "0.25" }, { "id": "aceip0404", "seq": "IP", "length": "2", "detail": "Milk (bovine) | Cereals (Wheat) | Legumin | Pork | Chicken", "source": "Milk | Cereal | Legume | Porcine | Chicken", "ic50": "<20 mM", "reference": "Binding of peptide substrates and inhibitors of angiotensin-converting enzyme. Importance of the COOH-terminal dipeptide sequence.; Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Three-dimensional holograph vector of atomic interaction field (3D-HoVAIF): a novel rotation-translation invariant 3D structure descriptor and its applications to peptides.; QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.; Peptides with angiotensin I converting enzyme (ACE) inhibitory activity generated from porcine skeletal muscle proteins by the action of meat-borne Lactobacillus.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1021\/jf051263l; 10.1002\/psc.892; 10.1007\/s00894-010-0862-x; 10.1016\/j.jprot.2013.06.023; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "6243277 16448176 17654623 20941517 23806758 23871047", "mw": "228.29", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "1.45", "instability": "-9.4", "hydrophobic": "1.0", "boman": "-2.46", "helix": "0.0", "turn_pct": "0.5", "sheet": "0.5" }, { "id": "aceip0405", "seq": "IPA", "length": "3", "detail": "Flaxseed", "source": "Plants", "ic50": "<20 mM", "reference": "Structural analysis of new antihypertensive peptides derived from cheese whey protein by proteinase K digestion.; Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Antihypertensive peptides: production, bioavailability and incorporation into foods.; Antihypertensive peptides from food proteins: a review.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.3168\/jds.S0022-0302(98)75878-3; 10.1021\/jf051263l; 10.1016\/j.cis.2010.11.001; 10.1039\/c2fo10192k; 10.1016\/j.foodchem.2013.05.140; 10.1080\/10408398.2012.664829", "pubmedid": "9891260 16448176 21185549 22249830 23871047 24915368", "mw": "299.37", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "1.5667", "instability": "61.27", "hydrophobic": "1.0", "boman": "-2.2433", "helix": "0.3333", "turn_pct": "0.3333", "sheet": "0.3333" }, { "id": "aceip0406", "seq": "IPAI", "length": "4", "detail": "ND", "source": "ND", "ic50": null, "reference": "What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1016\/j.foodchem.2013.05.140", "pubmedid": "23871047", "mw": "412.52", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "2.3", "instability": "48.45", "hydrophobic": "1.0", "boman": "-2.9125", "helix": "0.25", "turn_pct": "0.25", "sheet": "0.5" }, { "id": "aceip0407", "seq": "IPAIN", "length": "5", "detail": "Sweet-potato", "source": "Potato", "ic50": "432.6 μM", "reference": "Angiotensin-converting enzyme inhibitory activity of peptides derived from caprine kefir.", "doi": "10.3168\/jds.S0022-0302(05)73032-0", "pubmedid": "16162521", "mw": "526.63", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "1.14", "instability": "40.76", "hydrophobic": "0.8", "boman": "-2.006", "helix": "0.2", "turn_pct": "0.4", "sheet": "0.4" }, { "id": "aceip0408", "seq": "IPNPIGSE", "length": "8", "detail": "Milk (bovine) | Cereals | Pork | Chicken", "source": "Milk | Cereal | Porcine | Chicken", "ic50": null, "reference": "Enterococcus faecalis strains from food, environmental, and clinical origin produce ACE-inhibitory peptides and other bioactive peptides during growth in bovine skim milk.", "doi": "10.1016\/j.ijfoodmicro.2013.06.019", "pubmedid": "23845432", "mw": "825.91", "pi": "4.6", "charge_ph7": "-1.23", "gravy": "-0.3", "instability": "25.62", "hydrophobic": "0.5", "boman": "-0.835", "helix": "0.125", "turn_pct": "0.625", "sheet": "0.25" }, { "id": "aceip0409", "seq": "IPP", "length": "3", "detail": "Milk", "source": "Milk", "ic50": "<20 mM", "reference": "Purification and characterization of angiotensin I-converting enzyme inhibitors from sour milk.; Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Evaluation of the allergenicity of goat milk, cow milk, and their lactosera in a guinea pig model.; Rheological, sensorial, and chemopreventive properties of milk fermented with exopolysaccharide-producing lactic cultures.; Antihypertensive peptides: production, bioavailability and incorporation into foods.; LC-MS\/MS quantification of bioactive angiotensin I-converting enzyme inhibitory peptides in rye malt sourdoughs.; Antihypertensive peptides from food proteins: a review.; VPPIPP and IPPVPP: two hexapeptides innovated to exert antihypertensive activity.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.; Comparison of analytical methods to assay inhibitors of angiotensin I-converting enzyme.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.3168\/jds.S0022-0302(95)76689-9; 10.1021\/jf051263l; 10.3168\/jds.2008-1125; 10.3168\/jds.2008-1256; 10.1016\/j.cis.2010.11.001; 10.1021\/jf2033329; 10.1039\/c2fo10192k; 10.1371\/journal.pone.0062384; 10.1016\/j.foodchem.2013.05.140; 10.1016\/j.foodchem.2013.06.048; 10.1080\/10408398.2012.664829", "pubmedid": "7790570 16448176 19233776 19233777 21185549 21985248 22249830 23638059 23871047 23993489 24915368", "mw": "325.4", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "0.4333", "instability": "61.27", "hydrophobic": "1.0", "boman": "-1.64", "helix": "0.0", "turn_pct": "0.6667", "sheet": "0.3333" }, { "id": "aceip0410", "seq": "IPPLTQ", "length": "6", "detail": "Milk (bovine) | Amaranth | Sardine | Pork | Chicken connectin", "source": "Milk | Plants | Fish | Porcine | Chicken", "ic50": null, "reference": "Enterococcus faecalis strains from food, environmental, and clinical origin produce ACE-inhibitory peptides and other bioactive peptides during growth in bovine skim milk.", "doi": "10.1016\/j.ijfoodmicro.2013.06.019", "pubmedid": "23845432", "mw": "667.79", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "0.15", "instability": "23.07", "hydrophobic": "0.6667", "boman": "-1.37", "helix": "0.1667", "turn_pct": "0.3333", "sheet": "0.5" }, { "id": "aceip0411", "seq": "IPPVPP", "length": "6", "detail": "Milk (human)", "source": "Milk", "ic50": "13.17 %", "reference": "VPPIPP and IPPVPP: two hexapeptides innovated to exert antihypertensive activity.", "doi": "10.1371\/journal.pone.0062384", "pubmedid": "23638059", "mw": "618.76", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "0.3833", "instability": "131.93", "hydrophobic": "1.0", "boman": "-1.4933", "helix": "0.0", "turn_pct": "0.6667", "sheet": "0.3333" }, { "id": "aceip0412", "seq": "IPQ", "length": "3", "detail": "Milk", "source": "Milk", "ic50": null, "reference": "Angiotensin I-converting-enzyme-inhibitory and antibacterial peptides from Lactobacillus helveticus PR4 proteinase-hydrolyzed caseins of milk from six species.", "doi": "10.1128\/AEM.69.9.5297-5305.2003", "pubmedid": "12957917", "mw": "356.42", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "-0.2", "instability": "61.27", "hydrophobic": "0.6667", "boman": "-1.1867", "helix": "0.0", "turn_pct": "0.3333", "sheet": "0.3333" }, { "id": "aceip0413", "seq": "IPQEVLP", "length": "7", "detail": "Milk (bovine) | Cereals (Wheat) | pea | Pork | Chicken", "source": "Milk | Cereal | Legume | Porcine | Chicken", "ic50": "690 μM", "reference": "Inhibition of angiotensin-converting enzyme by synthetic peptide fragments of various beta-caseins.", "doi": "", "pubmedid": "1368548", "mw": "794.94", "pi": "4.05", "charge_ph7": "-1.24", "gravy": "0.3286", "instability": "87.0", "hydrophobic": "0.7143", "boman": "-1.5543", "helix": "0.2857", "turn_pct": "0.2857", "sheet": "0.4286" }, { "id": "aceip0414", "seq": "IPY", "length": "3", "detail": "ND", "source": "ND", "ic50": "206 μM", "reference": "Angiotensin converting enzyme inhibitory peptides derived from food proteins: biochemistry, bioactivity and production.", "doi": "10.2174\/138161207780363068", "pubmedid": "17430180", "mw": "391.46", "pi": "5.52", "charge_ph7": "-0.24", "gravy": "0.5333", "instability": "-2.93", "hydrophobic": "0.6667", "boman": "-1.5933", "helix": "0.0", "turn_pct": "0.3333", "sheet": "0.6667" }, { "id": "aceip0415", "seq": "IQ", "length": "2", "detail": "Milk (bovine) | Cereals (Wheat) | Pork | Chicken", "source": "Milk | Cereal | Porcine | Chicken", "ic50": null, "reference": "Three-dimensional holograph vector of atomic interaction field (3D-HoVAIF): a novel rotation-translation invariant 3D structure descriptor and its applications to peptides.", "doi": "10.1002\/psc.892", "pubmedid": "17654623", "mw": "259.3", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "0.5", "instability": "5.0", "hydrophobic": "0.5", "boman": "-1.78", "helix": "0.0", "turn_pct": "0.0", "sheet": "0.5" }, { "id": "aceip0416", "seq": "IQKEDVPSER", "length": "10", "detail": "Sweet-potato", "source": "Potato", "ic50": null, "reference": "Casein fermentate of Lactobacillus animalis DPC6134 contains a range of novel propeptide angiotensin-converting enzyme inhibitors.", "doi": "10.1128\/AEM.00096-07", "pubmedid": "17483275", "mw": "1200.3", "pi": "4.68", "charge_ph7": "-1.23", "gravy": "-1.61", "instability": "86.04", "hydrophobic": "0.3", "boman": "0.25", "helix": "0.3", "turn_pct": "0.3", "sheet": "0.2" }, { "id": "aceip0417", "seq": "IQP", "length": "3", "detail": "Shrimp", "source": "Shrimp", "ic50": "3.8 μM", "reference": "Angiotensin I converting enzyme inhibitory peptides produced by autolysis reactions from wheat bran.; Antihypertensive peptides from food proteins: a review.; Vegetable foods: a cheap source of proteins and peptides with antihypertensive, antioxidant, and other less occurrence bioactivities.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1021\/jf900857w; 10.1039\/c2fo10192k; 10.1016\/j.talanta.2012.12.041; 10.1016\/j.foodchem.2013.05.140; 10.1080\/10408398.2012.664829", "pubmedid": "19572648 22249830 23598136 23871047 24915368", "mw": "356.42", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "-0.2", "instability": "70.87", "hydrophobic": "0.6667", "boman": "-1.1867", "helix": "0.0", "turn_pct": "0.3333", "sheet": "0.3333" }, { "id": "aceip0418", "seq": "IR", "length": "2", "detail": "Casein | Milk (whey) | Milk (Fermented Milk) | Milk (Digested milk products)", "source": "Milk", "ic50": "<20 mM", "reference": "Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Bioactive peptides in amaranth (Amaranthus hypochondriacus) seed.; Quality and acceptability of a set-type yogurt made from camel milk.; Model of the exofacial substrate-binding site and helical folding of the human Glut1 glucose transporter based on scanning mutagenesis.; Peptides with angiotensin I converting enzyme (ACE) inhibitory activity generated from porcine skeletal muscle proteins by the action of meat-borne Lactobacillus.", "doi": "10.1021\/jf051263l; 10.1021\/jf072911z; 10.3168\/jds.2008-1408; 10.1021\/bi900521n; 10.1016\/j.jprot.2013.06.023", "pubmedid": "16448176 18211015 19233778 19449892 23806758", "mw": "287.36", "pi": "9.75", "charge_ph7": "0.76", "gravy": "0.0", "instability": "5.0", "hydrophobic": "0.5", "boman": "-1.1", "helix": "0.0", "turn_pct": "0.0", "sheet": "0.5" }, { "id": "aceip0419", "seq": "IRA", "length": "3", "detail": "Milk (bovine) | Fish (Sardine fermented sauce) | Cereals | Pork | Chicken", "source": "Milk | Fish | Cereal | Porcine | Chicken", "ic50": "<20 mM", "reference": "Structures and activity of angiotensin-converting enzyme inhibitors in an alpha-zein hydrolysate.; Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Bioactive peptides in amaranth (Amaranthus hypochondriacus) seed.; Cellular membrane disruption by amyloid fibrils involved intermolecular disulfide cross-linking.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1021\/jf051263l; 10.1021\/jf072911z; 10.1021\/bi900219c; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "1368684 16448176 18211015 19449893 23871047", "mw": "358.44", "pi": "9.75", "charge_ph7": "0.76", "gravy": "0.6", "instability": "6.67", "hydrophobic": "0.6667", "boman": "-1.3367", "helix": "0.3333", "turn_pct": "0.0", "sheet": "0.3333" }, { "id": "aceip0420", "seq": "IRAQQ", "length": "5", "detail": "ND", "source": "ND", "ic50": "4.2 μM", "reference": "Structures and activity of angiotensin-converting enzyme inhibitors in an alpha-zein hydrolysate.; Cellular membrane disruption by amyloid fibrils involved intermolecular disulfide cross-linking.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1021\/bi900219c; 10.1016\/j.foodchem.2012.09.092", "pubmedid": "1368684 19449893 23194537", "mw": "614.69", "pi": "9.75", "charge_ph7": "0.76", "gravy": "-1.04", "instability": "46.52", "hydrophobic": "0.4", "boman": "-0.258", "helix": "0.2", "turn_pct": "0.0", "sheet": "0.2" }, { "id": "aceip0421", "seq": "IRP", "length": "3", "detail": "Silkworm", "source": "Insect", "ic50": "<10 μM", "reference": "Angiotensin I-converting enzyme inhibitory peptides derived from bonito bowels autolysate.; Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1271\/bbb.57.695; 10.1021\/jf051263l; 10.1016\/j.foodchem.2013.05.140; 10.1080\/10408398.2012.664829", "pubmedid": "7763772 16448176 23871047 24915368", "mw": "384.47", "pi": "9.75", "charge_ph7": "0.76", "gravy": "-0.5333", "instability": "70.87", "hydrophobic": "0.6667", "boman": "-0.7333", "helix": "0.0", "turn_pct": "0.3333", "sheet": "0.3333" }, { "id": "aceip0422", "seq": "IRPVQ", "length": "5", "detail": "ND", "source": "ND", "ic50": "1.4 μM", "reference": "Isolation and characterization of angiotensin I-converting enzyme inhibitory peptides derived from bonito bowels.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1271\/bbb.57.1743; 10.1016\/j.foodchem.2012.09.092", "pubmedid": "7764272 23194537", "mw": "611.73", "pi": "9.75", "charge_ph7": "0.76", "gravy": "-0.18", "instability": "85.04", "hydrophobic": "0.6", "boman": "-0.976", "helix": "0.0", "turn_pct": "0.2", "sheet": "0.4" }, { "id": "aceip0423", "seq": "IRYLPRG", "length": "7", "detail": "Fish (Cuttlefish)", "source": "Fish", "ic50": "4.2 μM", "reference": "Vegetable foods: a cheap source of proteins and peptides with antihypertensive, antioxidant, and other less occurrence bioactivities.", "doi": "10.1016\/j.talanta.2012.12.041", "pubmedid": "23598136", "mw": "874.04", "pi": "10.84", "charge_ph7": "1.76", "gravy": "-0.5714", "instability": "2.41", "hydrophobic": "0.4286", "boman": "-0.7429", "helix": "0.1429", "turn_pct": "0.2857", "sheet": "0.4286" }, { "id": "aceip0424", "seq": "ISHIYVWK", "length": "8", "detail": "Chicken", "source": "Chicken", "ic50": "3.77 μM", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "23194537", "mw": "1045.23", "pi": "8.6", "charge_ph7": "0.85", "gravy": "0.3875", "instability": "63.67", "hydrophobic": "0.5", "boman": "-1.5825", "helix": "0.125", "turn_pct": "0.125", "sheet": "0.625" }, { "id": "aceip0425", "seq": "ITF", "length": "3", "detail": "Milk-Cheese (Goat milk protein and cheeses)", "source": "Milk", "ic50": "<20 mM", "reference": "Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1021\/jf051263l; 10.1080\/10408398.2012.664829", "pubmedid": "16448176 24915368", "mw": "379.45", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "2.2", "instability": "47.8", "hydrophobic": "0.6667", "boman": "-2.5467", "helix": "0.0", "turn_pct": "0.0", "sheet": "1.0" }, { "id": "aceip0426", "seq": "ITRINKK", "length": "7", "detail": "Milk (caprine kefir)", "source": "Milk", "ic50": null, "reference": "Enterococcus faecalis strains from food, environmental, and clinical origin produce ACE-inhibitory peptides and other bioactive peptides during growth in bovine skim milk.", "doi": "10.1016\/j.ijfoodmicro.2013.06.019", "pubmedid": "23845432", "mw": "872.07", "pi": "11.17", "charge_ph7": "2.76", "gravy": "-1.0714", "instability": "42.4", "hydrophobic": "0.2857", "boman": "-0.2971", "helix": "0.2857", "turn_pct": "0.1429", "sheet": "0.4286" }, { "id": "aceip0427", "seq": "ITRY", "length": "4", "detail": "Milk (caprine kefir)", "source": "Milk", "ic50": "236.9 μM", "reference": "Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1080\/10408398.2012.664829", "pubmedid": "24915368", "mw": "551.64", "pi": "8.75", "charge_ph7": "0.76", "gravy": "-0.5", "instability": "-11.35", "hydrophobic": "0.25", "boman": "-0.45", "helix": "0.0", "turn_pct": "0.0", "sheet": "0.75" }, { "id": "aceip0428", "seq": "ITT", "length": "3", "detail": "Fungi (Agaricus bisporus)", "source": "Fungi", "ic50": "<20 mM", "reference": "Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Peptide inhibitors for angiotensin I-converting enzyme from enzymatic hydrolysates of porcine skeletal muscle proteins.", "doi": "10.1021\/jf051263l; 10.1016\/s0309-1740(00)00108-x", "pubmedid": "16448176 22061507", "mw": "333.38", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "1.0333", "instability": "6.67", "hydrophobic": "0.3333", "boman": "-1.4667", "helix": "0.0", "turn_pct": "0.0", "sheet": "1.0" }, { "id": "aceip0429", "seq": "ITTNP", "length": "5", "detail": "Milk (caprine)", "source": "Milk", "ic50": "549 μM", "reference": "Angiotensin-I converting enzyme inhibitory peptide derived from porcine skeletal muscle myosin and its antihypertensive activity in spontaneously hypertensive rats.; Angiotensin I-converting enzyme-inhibitory peptides obtained from chicken collagen hydrolysate.; Peptide inhibitors for angiotensin I-converting enzyme from enzymatic hydrolysates of porcine skeletal muscle proteins.; Antihypertensive peptides from food proteins: a review.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1111\/j.1750-3841.2007.00571.x; 10.1021\/jf072669w; 10.1016\/s0309-1740(00)00108-x; 10.1039\/c2fo10192k; 10.1016\/j.foodchem.2012.09.092; 10.1080\/10408398.2012.664829", "pubmedid": "18034756 18808143 22061507 22249830 23194537 24915368", "mw": "544.6", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "-0.4", "instability": "-27.82", "hydrophobic": "0.4", "boman": "-0.556", "helix": "0.0", "turn_pct": "0.4", "sheet": "0.6" }, { "id": "aceip0430", "seq": "ITTNPY", "length": "6", "detail": "ND", "source": "ND", "ic50": null, "reference": "Angiotensin I-converting enzyme inhibitory peptides generated from in vitro gastrointestinal digestion of pork meat.", "doi": "10.1021\/jf904204n", "pubmedid": "20151679", "mw": "707.77", "pi": "5.52", "charge_ph7": "-0.24", "gravy": "-0.55", "instability": "-21.52", "hydrophobic": "0.3333", "boman": "-0.44", "helix": "0.0", "turn_pct": "0.3333", "sheet": "0.6667" }, { "id": "aceip0431", "seq": "IV", "length": "2", "detail": "Milk (Fermented Milk)", "source": "Milk", "ic50": null, "reference": "Quantitative structure-activity relationship study of bitter di- and tri-peptides including relationship with angiotensin I-converting enzyme inhibitory activity.; Three-dimensional holograph vector of atomic interaction field (3D-HoVAIF): a novel rotation-translation invariant 3D structure descriptor and its applications to peptides.", "doi": "10.1002\/psc.800; 10.1002\/psc.892", "pubmedid": "17117396 17654623", "mw": "230.3", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "4.35", "instability": "-37.45", "hydrophobic": "1.0", "boman": "-4.48", "helix": "0.0", "turn_pct": "0.0", "sheet": "1.0" }, { "id": "aceip0432", "seq": "IVF", "length": "3", "detail": "ND", "source": "ND", "ic50": "33.11 μM", "reference": "Antihypertensive peptides from food proteins: a review.", "doi": "10.1039\/c2fo10192k", "pubmedid": "22249830", "mw": "377.48", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "3.8333", "instability": "-21.63", "hydrophobic": "1.0", "boman": "-3.98", "helix": "0.0", "turn_pct": "0.0", "sheet": "1.0" }, { "id": "aceip0433", "seq": "IVGRPHQG", "length": "8", "detail": "ND", "source": "ND", "ic50": null, "reference": "Temporal gene expression and probiotic attributes of Lactobacillus acidophilus during growth in milk.", "doi": "10.3168\/jds.2008-1457", "pubmedid": "19233780", "mw": "862.98", "pi": "9.76", "charge_ph7": "0.85", "gravy": "-0.6125", "instability": "11.6", "hydrophobic": "0.375", "boman": "-0.7212", "helix": "0.0", "turn_pct": "0.375", "sheet": "0.25" }, { "id": "aceip0434", "seq": "IVGRPR", "length": "6", "detail": "Bonito", "source": "Fish", "ic50": "302 μM", "reference": "Antihypertensive peptides from food proteins: a review.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1039\/c2fo10192k; 10.1016\/j.foodchem.2012.09.092", "pubmedid": "22249830 23194537", "mw": "696.84", "pi": "12.0", "charge_ph7": "1.76", "gravy": "-0.3833", "instability": "-0.43", "hydrophobic": "0.5", "boman": "-0.7433", "helix": "0.0", "turn_pct": "0.3333", "sheet": "0.3333" }, { "id": "aceip0435", "seq": "IVGRPRH", "length": "7", "detail": "Milk (bovine) | Synthesized | Cereals (Soybean+Wheat) | Soybean (Fermented) | Soybean Sauce", "source": "Milk | Synthesized | Cereal | Legume", "ic50": "300 μM", "reference": "Review on the angiotensin-I-converting enzyme (ACE) inhibitor peptides from marine proteins.", "doi": "10.1007\/s12010-012-0024-y", "pubmedid": "23271625", "mw": "833.98", "pi": "12.0", "charge_ph7": "1.85", "gravy": "-0.7857", "instability": "28.57", "hydrophobic": "0.4286", "boman": "-0.4957", "helix": "0.0", "turn_pct": "0.2857", "sheet": "0.2857" }, { "id": "aceip0436", "seq": "IVGRPRHQG", "length": "9", "detail": "Sardine", "source": "Fish", "ic50": "2.4 μM", "reference": "Peptide inhibitors for angiotensin I-converting enzyme from thermolysin digest of dried bonito.; QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.; Antihypertensive peptides from food proteins: a review.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.; Review on the angiotensin-I-converting enzyme (ACE) inhibitor peptides from marine proteins.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1271\/bbb.56.1541; 10.1007\/s00894-010-0862-x; 10.1039\/c2fo10192k; 10.1016\/j.foodchem.2012.09.092; 10.1007\/s12010-012-0024-y; 10.1080\/10408398.2012.664829", "pubmedid": "1369054 20941517 22249830 23194537 23271625 24915368", "mw": "1019.16", "pi": "12.0", "charge_ph7": "1.85", "gravy": "-1.0444", "instability": "24.44", "hydrophobic": "0.3333", "boman": "-0.3389", "helix": "0.0", "turn_pct": "0.3333", "sheet": "0.2222" }, { "id": "aceip0437", "seq": "IVIF", "length": "4", "detail": "Milk (bovine) | Amaranth | Garlic | Silkworm | Fish | Fish (Sea bream scale) | Fish (Sea bream) | Cereals (Soybean+Wheat) | Soybean | Soybean (Fermented) | Soybean Sauce | Pork | Chicken connectin | Spider", "source": "Milk | Plants | Insect | Fish | Cereal | Legume | Porcine | Chicken | Arthropod", "ic50": null, "reference": "What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1016\/j.foodchem.2013.05.140", "pubmedid": "23871047", "mw": "490.64", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "4.0", "instability": "-13.73", "hydrophobic": "1.0", "boman": "-4.215", "helix": "0.0", "turn_pct": "0.0", "sheet": "1.0" }, { "id": "aceip0438", "seq": "IVPNSVEQKH", "length": "10", "detail": "Squid", "source": "Animal", "ic50": null, "reference": "Casein fermentate of Lactobacillus animalis DPC6134 contains a range of novel propeptide angiotensin-converting enzyme inhibitors.", "doi": "10.1128\/AEM.00096-07", "pubmedid": "17483275", "mw": "1150.28", "pi": "6.75", "charge_ph7": "-0.15", "gravy": "-0.71", "instability": "39.03", "hydrophobic": "0.4", "boman": "-0.497", "helix": "0.2", "turn_pct": "0.3", "sheet": "0.3" }, { "id": "aceip0439", "seq": "IVQ", "length": "3", "detail": "ND", "source": "ND", "ic50": "<20 mM", "reference": "Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.", "doi": "10.1021\/jf051263l", "pubmedid": "16448176", "mw": "358.43", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "1.7333", "instability": "-21.63", "hydrophobic": "0.6667", "boman": "-2.5333", "helix": "0.0", "turn_pct": "0.0", "sheet": "0.6667" }, { "id": "aceip0440", "seq": "IVVE", "length": "4", "detail": "Milk (bovine) | pea", "source": "Milk | Legume", "ic50": "315.3 μM", "reference": "Review on the angiotensin-I-converting enzyme (ACE) inhibitor peptides from marine proteins.; Vegetable foods: a cheap source of proteins and peptides with antihypertensive, antioxidant, and other less occurrence bioactivities.", "doi": "10.1007\/s12010-012-0024-y; 10.1016\/j.talanta.2012.12.041", "pubmedid": "23271625 23598136", "mw": "458.55", "pi": "4.6", "charge_ph7": "-1.23", "gravy": "2.35", "instability": "-13.73", "hydrophobic": "0.75", "boman": "-2.84", "helix": "0.25", "turn_pct": "0.0", "sheet": "0.75" }, { "id": "aceip0441", "seq": "IVY", "length": "3", "detail": "ND", "source": "ND", "ic50": "<20 mM", "reference": "Determination of antihypertensive small peptides, Val-Tyr and Ile-Val-Tyr, by fluorometric high-performance liquid chromatography combined with a double heart-cut column-switching technique.; Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Antihypertensive effect of angiotensin I-converting enzyme inhibitory peptides from a sesame protein hydrolysate in spontaneously hypertensive rats.; Inhibition strength of short peptides derived from an ACE inhibitory peptide.; Vegetable foods: a cheap source of proteins and peptides with antihypertensive, antioxidant, and other less occurrence bioactivities.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.; Comparison of analytical methods to assay inhibitors of angiotensin I-converting enzyme.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.2116\/analsci.21.997; 10.1021\/jf051263l; 10.1271\/bbb.70.1118; 10.1021\/jf202902r; 10.1016\/j.talanta.2012.12.041; 10.1016\/j.foodchem.2013.05.140; 10.1016\/j.foodchem.2013.06.048; 10.1080\/10408398.2012.664829", "pubmedid": "16122175 16448176 16717411 21923188 23598136 23871047 23993489 24915368", "mw": "393.48", "pi": "5.52", "charge_ph7": "-0.24", "gravy": "2.4667", "instability": "-46.77", "hydrophobic": "0.6667", "boman": "-2.94", "helix": "0.0", "turn_pct": "0.0", "sheet": "1.0" }, { "id": "aceip0442", "seq": "IW", "length": "2", "detail": "ND", "source": "Egg", "ic50": "<10 μM", "reference": "Angiotensin I-converting enzyme inhibitory peptides derived from wakame (Undaria pinnatifida) and their antihypertensive effect in spontaneously hypertensive rats.; Antihypertensive effects of Undaria pinnatifida (wakame) peptide on blood pressure in spontaneously hypertensive rats.; Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Three-dimensional holograph vector of atomic interaction field (3D-HoVAIF): a novel rotation-translation invariant 3D structure descriptor and its applications to peptides.; QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.; Inhibition strength of short peptides derived from an ACE inhibitory peptide.; Antihypertensive peptides from food proteins: a review.; Review on the angiotensin-I-converting enzyme (ACE) inhibitor peptides from marine proteins.; Vegetable foods: a cheap source of proteins and peptides with antihypertensive, antioxidant, and other less occurrence bioactivities.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1021\/jf020482t; 10.1016\/j.jnutbio.2003.11.004; 10.1021\/jf051263l; 10.1002\/psc.892; 10.1007\/s00894-010-0862-x; 10.1021\/jf202902r; 10.1039\/c2fo10192k; 10.1007\/s12010-012-0024-y; 10.1016\/j.talanta.2012.12.041; 10.1016\/j.foodchem.2013.05.140; 10.1080\/10408398.2012.664829", "pubmedid": "12358510 15135150 16448176 17654623 20941517 21923188 22249830 23271625 23598136 23871047 24915368", "mw": "317.38", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "1.8", "instability": "5.0", "hydrophobic": "1.0", "boman": "-3.625", "helix": "0.0", "turn_pct": "0.0", "sheet": "1.0" }, { "id": "aceip0443", "seq": "IWH", "length": "3", "detail": "Egg (Ovalbumin)", "source": "Egg", "ic50": "<20 mM", "reference": "Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Antihypertensive peptides from food proteins: a review.; Review on the angiotensin-I-converting enzyme (ACE) inhibitor peptides from marine proteins.", "doi": "10.1021\/jf051263l; 10.1039\/c2fo10192k; 10.1007\/s12010-012-0024-y", "pubmedid": "16448176 22249830 23271625", "mw": "454.52", "pi": "6.74", "charge_ph7": "-0.15", "gravy": "0.1333", "instability": "85.6", "hydrophobic": "0.6667", "boman": "-2.0867", "helix": "0.0", "turn_pct": "0.0", "sheet": "0.6667" }, { "id": "aceip0444", "seq": "IWHHT", "length": "5", "detail": "Sweet-potato", "source": "Potato", "ic50": "<10 μM", "reference": "Peptide inhibitors for angiotensin I-converting enzyme from thermolysin digest of dried bonito.; Antihypertensive peptides from food proteins: a review.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.; Review on the angiotensin-I-converting enzyme (ACE) inhibitor peptides from marine proteins.", "doi": "10.1271\/bbb.56.1541; 10.1039\/c2fo10192k; 10.1016\/j.foodchem.2012.09.092; 10.1007\/s12010-012-0024-y", "pubmedid": "1369054 22249830 23194537 23271625", "mw": "692.77", "pi": "6.92", "charge_ph7": "-0.07", "gravy": "-0.7", "instability": "40.28", "hydrophobic": "0.4", "boman": "-1.002", "helix": "0.0", "turn_pct": "0.0", "sheet": "0.6" }, { "id": "aceip0445", "seq": "IY", "length": "2", "detail": "Bonito", "source": "Fish", "ic50": "<20 mM", "reference": "Peptide inhibitors for angiotensin I-converting enzyme from thermolysin digest of dried bonito.; Angiotensin I-converting enzyme inhibitory peptides in an alkaline protease hydrolyzate derived from sardine muscle.; Angiotensin I-converting enzyme inhibitory peptides derived from wakame (Undaria pinnatifida) and their antihypertensive effect in spontaneously hypertensive rats.; New antihypertensive peptides isolated from rapeseed.; Antihypertensive effects of Undaria pinnatifida (wakame) peptide on blood pressure in spontaneously hypertensive rats.; Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Three-dimensional holograph vector of atomic interaction field (3D-HoVAIF): a novel rotation-translation invariant 3D structure descriptor and its applications to peptides.; Bioactive peptides in amaranth (Amaranthus hypochondriacus) seed.; Model of the exofacial substrate-binding site and helical folding of the human Glut1 glucose transporter based on scanning mutagenesis.; Angiotensin I converting enzyme inhibitory peptides produced by autolysis reactions from wheat bran.; Antihypertensive peptides from food proteins: a review.; Review on the angiotensin-I-converting enzyme (ACE) inhibitor peptides from marine proteins.; Vegetable foods: a cheap source of proteins and peptides with antihypertensive, antioxidant, and other less occurrence bioactivities.; Peptides with angiotensin I converting enzyme (ACE) inhibitory activity generated from porcine skeletal muscle proteins by the action of meat-borne Lactobacillus.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.; Glycinyl-histidinyl-serine (GHS), a novel rapeseed protein-derived peptide has blood pressure-lowering effect in spontaneously hypertensive rats.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1271\/bbb.56.1541; 10.1271\/bbb.58.2244; 10.1021\/jf020482t; 10.1016\/s0196-9781(03)00174-8; 10.1016\/j.jnutbio.2003.11.004; 10.1021\/jf051263l; 10.1002\/psc.892; 10.1021\/jf072911z; 10.1021\/bi900521n; 10.1021\/jf900857w; 10.1039\/c2fo10192k; 10.1007\/s12010-012-0024-y; 10.1016\/j.talanta.2012.12.041; 10.1016\/j.jprot.2013.06.023; 10.1016\/j.foodchem.2013.05.140; 10.1021\/jf400865m; 10.1080\/10408398.2012.664829", "pubmedid": "1369054 7765718 12358510 12948830 15135150 16448176 17654623 18211015 19449892 19572648 22249830 23271625 23598136 23806758 23871047 23919612 24915368", "mw": "294.35", "pi": "5.52", "charge_ph7": "-0.24", "gravy": "1.6", "instability": "5.0", "hydrophobic": "0.5", "boman": "-2.39", "helix": "0.0", "turn_pct": "0.0", "sheet": "1.0" }, { "id": "aceip0446", "seq": "IYLL", "length": "4", "detail": "Milk (bovine) | Cereals | Pork | Chicken", "source": "Milk | Cereal | Porcine | Chicken", "ic50": "42 μM", "reference": "Vegetable foods: a cheap source of proteins and peptides with antihypertensive, antioxidant, and other less occurrence bioactivities.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1016\/j.talanta.2012.12.041; 10.1080\/10408398.2012.664829", "pubmedid": "23598136 24915368", "mw": "520.66", "pi": "5.52", "charge_ph7": "-0.24", "gravy": "2.7", "instability": "7.5", "hydrophobic": "0.75", "boman": "-3.655", "helix": "0.5", "turn_pct": "0.0", "sheet": "1.0" }, { "id": "aceip0447", "seq": "IYP", "length": "3", "detail": "Milk (caprine)", "source": "Milk", "ic50": "61 μM", "reference": "The potential role of milk-derived peptides in cardiovascular disease.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1039\/c1fo10017c; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "21779574 23871047", "mw": "391.46", "pi": "5.52", "charge_ph7": "-0.24", "gravy": "0.5333", "instability": "47.8", "hydrophobic": "0.6667", "boman": "-1.5933", "helix": "0.0", "turn_pct": "0.3333", "sheet": "0.6667" }, { "id": "aceip0448", "seq": "IYPR", "length": "4", "detail": "WIPO | Soybean | Soybean (Fermented)", "source": "Legume", "ic50": "10 μM", "reference": "Structure and activity of angiotensin I converting enzyme inhibitory peptides from sake and sake lees.", "doi": "10.1271\/bbb.58.1767", "pubmedid": "7765503", "mw": "547.65", "pi": "8.75", "charge_ph7": "0.76", "gravy": "-0.725", "instability": "19.5", "hydrophobic": "0.5", "boman": "-0.515", "helix": "0.0", "turn_pct": "0.25", "sheet": "0.5" }, { "id": "aceip0449", "seq": "IYPRY", "length": "5", "detail": "Synthesized", "source": "Synthesized", "ic50": "4.1 μM", "reference": "Structure and activity of angiotensin I converting enzyme inhibitory peptides from sake and sake lees.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.; Vegetable foods: a cheap source of proteins and peptides with antihypertensive, antioxidant, and other less occurrence bioactivities.", "doi": "10.1271\/bbb.58.1767; 10.1016\/j.foodchem.2012.09.092; 10.1016\/j.talanta.2012.12.041", "pubmedid": "7765503 23194537 23598136", "mw": "710.82", "pi": "8.59", "charge_ph7": "0.76", "gravy": "-0.84", "instability": "2.52", "hydrophobic": "0.4", "boman": "-0.384", "helix": "0.0", "turn_pct": "0.2", "sheet": "0.6" }, { "id": "aceip0450", "seq": "JEWPPGHHIPP", "length": "11", "detail": "Synthesized | Tuna", "source": "Synthesized | Fish", "ic50": null, "reference": "Identification of novel bradykinin-potentiating peptides and C-type natriuretic peptide from Lachesis muta venom.", "doi": "10.1016\/j.toxicon.2005.03.006", "pubmedid": "15876444", "mw": null, "pi": null, "charge_ph7": null, "gravy": null, "instability": null, "hydrophobic": null, "boman": null, "helix": null, "turn_pct": null, "sheet": null }, { "id": "aceip0451", "seq": "JGGWPRPGPEIPP", "length": "13", "detail": "Tuna", "source": "Fish", "ic50": null, "reference": "Angiotensin-converting enzyme inhibitors from the venom of Bothrops jararaca. Isolation, elucidation of structure, and synthesis.", "doi": "10.1021\/bi00798a004", "pubmedid": "4334402", "mw": null, "pi": null, "charge_ph7": null, "gravy": null, "instability": null, "hydrophobic": null, "boman": null, "helix": null, "turn_pct": null, "sheet": null }, { "id": "aceip0452", "seq": "JGLPPGPPIPP", "length": "11", "detail": "Tuna", "source": "Fish", "ic50": null, "reference": "Bradykinin-potentiating peptides from the venom of Agkistrodon halys blomhoffi. Isolation of five bradykinin potentiators and the amino acid sequences of two of them, potentiators B and C.", "doi": "10.1021\/bi00782a007", "pubmedid": "4323853", "mw": null, "pi": null, "charge_ph7": null, "gravy": null, "instability": null, "hydrophobic": null, "boman": null, "helix": null, "turn_pct": null, "sheet": null }, { "id": "aceip0453", "seq": "JGLPPGPVIPP", "length": "11", "detail": "Milk | Amaranth | Synthesized", "source": "Milk | Plants | Synthesized", "ic50": null, "reference": "Inhibition of angiotensin-coverting enzyme by analogs of peptides from Bothrops jararaca venom.", "doi": "10.1007\/BF01930447", "pubmedid": "4354751", "mw": null, "pi": null, "charge_ph7": null, "gravy": null, "instability": null, "hydrophobic": null, "boman": null, "helix": null, "turn_pct": null, "sheet": null }, { "id": "aceip0454", "seq": "JGRPPGPPIP", "length": "10", "detail": "Milk", "source": "Milk", "ic50": null, "reference": "Structure of potentiator A, one of the five bradykinin potentiating peptides from the venom of Agkistrodon halys blomhoffii.", "doi": "10.1007\/BF01926673", "pubmedid": "4730295", "mw": null, "pi": null, "charge_ph7": null, "gravy": null, "instability": null, "hydrophobic": null, "boman": null, "helix": null, "turn_pct": null, "sheet": null }, { "id": "aceip0455", "seq": "JKKWPPGHHIPP", "length": "12", "detail": "Milk (bovine) | Cereals | Chicken", "source": "Milk | Cereal | Chicken", "ic50": null, "reference": "Identification of novel bradykinin-potentiating peptides and C-type natriuretic peptide from Lachesis muta venom.", "doi": "10.1016\/j.toxicon.2005.03.006", "pubmedid": "15876444", "mw": null, "pi": null, "charge_ph7": null, "gravy": null, "instability": null, "hydrophobic": null, "boman": null, "helix": null, "turn_pct": null, "sheet": null }, { "id": "aceip0456", "seq": "JKPWPPGHHIPP", "length": "12", "detail": "Milk (Casein)", "source": "Milk", "ic50": null, "reference": "Identification of novel bradykinin-potentiating peptides and C-type natriuretic peptide from Lachesis muta venom.", "doi": "10.1016\/j.toxicon.2005.03.006", "pubmedid": "15876444", "mw": null, "pi": null, "charge_ph7": null, "gravy": null, "instability": null, "hydrophobic": null, "boman": null, "helix": null, "turn_pct": null, "sheet": null }, { "id": "aceip0457", "seq": "JKW", "length": "3", "detail": "Milk (bovine) | Cereals | Pork", "source": "Milk | Cereal | Porcine", "ic50": null, "reference": "Primary structure and biological activity of bradykinin potentiating peptides from Bothrops insularis snake venom.", "doi": "10.1007\/BF01025312", "pubmedid": "2386615", "mw": null, "pi": null, "charge_ph7": null, "gravy": null, "instability": null, "hydrophobic": null, "boman": null, "helix": null, "turn_pct": null, "sheet": null }, { "id": "aceip0458", "seq": "JKWALPKVPP", "length": "10", "detail": "WIPO", "source": "ND", "ic50": null, "reference": "High throughput screening of bradykinin-potentiating peptides in Bothrops moojeni snake venom using precursor ion mass spectrometry.", "doi": "10.1016\/j.toxicon.2008.02.019", "pubmedid": "18471845", "mw": null, "pi": null, "charge_ph7": null, "gravy": null, "instability": null, "hydrophobic": null, "boman": null, "helix": null, "turn_pct": null, "sheet": null }, { "id": "aceip0459", "seq": "JKWAP", "length": "5", "detail": "Milk (bovine) | Milk (human) | Milk (Casein) | Egg (Ovalbumin)", "source": "Milk | Egg", "ic50": null, "reference": "Isolation of bradykinin-potentiating peptides from Bothrops jararaca venom.", "doi": "10.1021\/bi00815a005", "pubmedid": "4317874", "mw": null, "pi": null, "charge_ph7": null, "gravy": null, "instability": null, "hydrophobic": null, "boman": null, "helix": null, "turn_pct": null, "sheet": null }, { "id": "aceip0460", "seq": "JKWDPPPISPP", "length": "11", "detail": "Milk (Goat milk protein)", "source": "Milk", "ic50": null, "reference": "Identification of novel bradykinin-potentiating peptides and C-type natriuretic peptide from Lachesis muta venom.", "doi": "10.1016\/j.toxicon.2005.03.006", "pubmedid": "15876444", "mw": null, "pi": null, "charge_ph7": null, "gravy": null, "instability": null, "hydrophobic": null, "boman": null, "helix": null, "turn_pct": null, "sheet": null }, { "id": "aceip0461", "seq": "JKWDPPPPSPP", "length": "11", "detail": "Casein", "source": "Milk", "ic50": null, "reference": "Inhibition of angiotensin-coverting enzyme by analogs of peptides from Bothrops jararaca venom.", "doi": "10.1007\/BF01930447", "pubmedid": "4354751", "mw": null, "pi": null, "charge_ph7": null, "gravy": null, "instability": null, "hydrophobic": null, "boman": null, "helix": null, "turn_pct": null, "sheet": null }, { "id": "aceip0462", "seq": "JKWDPPPVSPP", "length": "11", "detail": "Cereals (Maize)", "source": "Cereal", "ic50": null, "reference": "Structure of bradykinin-potentiating peptide containing tryptophan from the venom of Agkistrodon halys blomhoffii.", "doi": "10.1007\/BF01897966", "pubmedid": "5530287", "mw": null, "pi": null, "charge_ph7": null, "gravy": null, "instability": null, "hydrophobic": null, "boman": null, "helix": null, "turn_pct": null, "sheet": null }, { "id": "aceip0463", "seq": "JKWHRNPEIP", "length": "10", "detail": "Milk (bovine) | Cereals | Pork", "source": "Milk | Cereal | Porcine", "ic50": null, "reference": "High throughput screening of bradykinin-potentiating peptides in Bothrops moojeni snake venom using precursor ion mass spectrometry.", "doi": "10.1016\/j.toxicon.2008.02.019", "pubmedid": "18471845", "mw": null, "pi": null, "charge_ph7": null, "gravy": null, "instability": null, "hydrophobic": null, "boman": null, "helix": null, "turn_pct": null, "sheet": null }, { "id": "aceip0464", "seq": "JKWP", "length": "4", "detail": "ND", "source": "ND", "ic50": null, "reference": "High throughput screening of bradykinin-potentiating peptides in Bothrops moojeni snake venom using precursor ion mass spectrometry.", "doi": "10.1016\/j.toxicon.2008.02.019", "pubmedid": "18471845", "mw": null, "pi": null, "charge_ph7": null, "gravy": null, "instability": null, "hydrophobic": null, "boman": null, "helix": null, "turn_pct": null, "sheet": null }, { "id": "aceip0465", "seq": "JKWPGPK", "length": "7", "detail": "Milk (caprine kefir)", "source": "Milk", "ic50": null, "reference": "High throughput screening of bradykinin-potentiating peptides in Bothrops moojeni snake venom using precursor ion mass spectrometry.", "doi": "10.1016\/j.toxicon.2008.02.019", "pubmedid": "18471845", "mw": null, "pi": null, "charge_ph7": null, "gravy": null, "instability": null, "hydrophobic": null, "boman": null, "helix": null, "turn_pct": null, "sheet": null }, { "id": "aceip0466", "seq": "JKWPGPKVP", "length": "9", "detail": "Milk (bovine)", "source": "Milk", "ic50": null, "reference": "High throughput screening of bradykinin-potentiating peptides in Bothrops moojeni snake venom using precursor ion mass spectrometry.", "doi": "10.1016\/j.toxicon.2008.02.019", "pubmedid": "18471845", "mw": null, "pi": null, "charge_ph7": null, "gravy": null, "instability": null, "hydrophobic": null, "boman": null, "helix": null, "turn_pct": null, "sheet": null }, { "id": "aceip0467", "seq": "JKWPHEHPP", "length": "9", "detail": "Milk (bovine, buffalo and ovine)", "source": "Milk", "ic50": null, "reference": "High throughput screening of bradykinin-potentiating peptides in Bothrops moojeni snake venom using precursor ion mass spectrometry.", "doi": "10.1016\/j.toxicon.2008.02.019", "pubmedid": "18471845", "mw": null, "pi": null, "charge_ph7": null, "gravy": null, "instability": null, "hydrophobic": null, "boman": null, "helix": null, "turn_pct": null, "sheet": null }, { "id": "aceip0468", "seq": "JKWPKGPLPP", "length": "10", "detail": "Milk | Enzymatic-hydrolysis", "source": "Milk | Synthesized", "ic50": null, "reference": "High throughput screening of bradykinin-potentiating peptides in Bothrops moojeni snake venom using precursor ion mass spectrometry.", "doi": "10.1016\/j.toxicon.2008.02.019", "pubmedid": "18471845", "mw": null, "pi": null, "charge_ph7": null, "gravy": null, "instability": null, "hydrophobic": null, "boman": null, "helix": null, "turn_pct": null, "sheet": null }, { "id": "aceip0469", "seq": "JKWPPGKVPP", "length": "10", "detail": "Milk (Casein)", "source": "Milk", "ic50": null, "reference": "High throughput screening of bradykinin-potentiating peptides in Bothrops moojeni snake venom using precursor ion mass spectrometry.", "doi": "10.1016\/j.toxicon.2008.02.019", "pubmedid": "18471845", "mw": null, "pi": null, "charge_ph7": null, "gravy": null, "instability": null, "hydrophobic": null, "boman": null, "helix": null, "turn_pct": null, "sheet": null }, { "id": "aceip0470", "seq": "JKWPRP", "length": "6", "detail": "Sardine", "source": "Fish", "ic50": null, "reference": "High throughput screening of bradykinin-potentiating peptides in Bothrops moojeni snake venom using precursor ion mass spectrometry.", "doi": "10.1016\/j.toxicon.2008.02.019", "pubmedid": "18471845", "mw": null, "pi": null, "charge_ph7": null, "gravy": null, "instability": null, "hydrophobic": null, "boman": null, "helix": null, "turn_pct": null, "sheet": null }, { "id": "aceip0471", "seq": "JKWPRPGPEIPP", "length": "12", "detail": "Synthesized", "source": "Synthesized", "ic50": null, "reference": "High throughput screening of bradykinin-potentiating peptides in Bothrops moojeni snake venom using precursor ion mass spectrometry.", "doi": "10.1016\/j.toxicon.2008.02.019", "pubmedid": "18471845", "mw": null, "pi": null, "charge_ph7": null, "gravy": null, "instability": null, "hydrophobic": null, "boman": null, "helix": null, "turn_pct": null, "sheet": null }, { "id": "aceip0472", "seq": "JNWKSP", "length": "6", "detail": "Milk (human)", "source": "Milk", "ic50": null, "reference": "A novel peptide from the ACEI\/BPP-CNP precursor in the venom of Crotalus durissus collilineatus.", "doi": "10.1016\/j.cbpc.2006.04.006", "pubmedid": "16979945", "mw": null, "pi": null, "charge_ph7": null, "gravy": null, "instability": null, "hydrophobic": null, "boman": null, "helix": null, "turn_pct": null, "sheet": null }, { "id": "aceip0473", "seq": "JNWPRPGPEIP", "length": "11", "detail": "Milk (Casein)", "source": "Milk", "ic50": null, "reference": "High throughput screening of bradykinin-potentiating peptides in Bothrops moojeni snake venom using precursor ion mass spectrometry.", "doi": "10.1016\/j.toxicon.2008.02.019", "pubmedid": "18471845", "mw": null, "pi": null, "charge_ph7": null, "gravy": null, "instability": null, "hydrophobic": null, "boman": null, "helix": null, "turn_pct": null, "sheet": null }, { "id": "aceip0474", "seq": "JNWPRPQIPP", "length": "10", "detail": "ND", "source": "ND", "ic50": null, "reference": "Angiotensin-converting enzyme inhibitors from the venom of Bothrops jararaca. Isolation, elucidation of structure, and synthesis.", "doi": "10.1021\/bi00798a004", "pubmedid": "4334402", "mw": null, "pi": null, "charge_ph7": null, "gravy": null, "instability": null, "hydrophobic": null, "boman": null, "helix": null, "turn_pct": null, "sheet": null }, { "id": "aceip0475", "seq": "JRWPHLEIPP", "length": "10", "detail": "ND", "source": "ND", "ic50": null, "reference": "A novel peptide from the ACEI\/BPP-CNP precursor in the venom of Crotalus durissus collilineatus.", "doi": "10.1016\/j.cbpc.2006.04.006", "pubmedid": "16979945", "mw": null, "pi": null, "charge_ph7": null, "gravy": null, "instability": null, "hydrophobic": null, "boman": null, "helix": null, "turn_pct": null, "sheet": null }, { "id": "aceip0476", "seq": "JSWP", "length": "4", "detail": "Fish | Fish (Seaweed pipefish)", "source": "Fish", "ic50": null, "reference": "High throughput screening of bradykinin-potentiating peptides in Bothrops moojeni snake venom using precursor ion mass spectrometry.", "doi": "10.1016\/j.toxicon.2008.02.019", "pubmedid": "18471845", "mw": null, "pi": null, "charge_ph7": null, "gravy": null, "instability": null, "hydrophobic": null, "boman": null, "helix": null, "turn_pct": null, "sheet": null }, { "id": "aceip0477", "seq": "JSWPGPNIPP", "length": "10", "detail": "Milk (bovine) | Amaranth | Cereals | Sake | Chicken connectin", "source": "Milk | Plants | Cereal | Chicken", "ic50": null, "reference": "Angiotensin-converting enzyme inhibitors from the venom of Bothrops jararaca. Isolation, elucidation of structure, and synthesis.", "doi": "10.1021\/bi00798a004", "pubmedid": "4334402", "mw": null, "pi": null, "charge_ph7": null, "gravy": null, "instability": null, "hydrophobic": null, "boman": null, "helix": null, "turn_pct": null, "sheet": null }, { "id": "aceip0478", "seq": "JTNW", "length": "4", "detail": "Milk (bovine) | Milk (Casein) | Soybean | Pork | Chicken", "source": "Milk | Legume | Porcine | Chicken", "ic50": null, "reference": "High throughput screening of bradykinin-potentiating peptides in Bothrops moojeni snake venom using precursor ion mass spectrometry.", "doi": "10.1016\/j.toxicon.2008.02.019", "pubmedid": "18471845", "mw": null, "pi": null, "charge_ph7": null, "gravy": null, "instability": null, "hydrophobic": null, "boman": null, "helix": null, "turn_pct": null, "sheet": null }, { "id": "aceip0479", "seq": "JWPRPQIPP", "length": "9", "detail": "Algae (Spirulina platensis)", "source": "Bacteria", "ic50": null, "reference": "Angiotensin-converting enzyme inhibitors from the venom of Bothrops jararaca. Isolation, elucidation of structure, and synthesis.", "doi": "10.1021\/bi00798a004", "pubmedid": "4334402", "mw": null, "pi": null, "charge_ph7": null, "gravy": null, "instability": null, "hydrophobic": null, "boman": null, "helix": null, "turn_pct": null, "sheet": null }, { "id": "aceip0480", "seq": "JWPRPTPQIPP", "length": "11", "detail": "Milk (human)", "source": "Milk", "ic50": null, "reference": "Angiotensin-converting enzyme inhibitors from the venom of Bothrops jararaca. Isolation, elucidation of structure, and synthesis.", "doi": "10.1021\/bi00798a004", "pubmedid": "4334402", "mw": null, "pi": null, "charge_ph7": null, "gravy": null, "instability": null, "hydrophobic": null, "boman": null, "helix": null, "turn_pct": null, "sheet": null }, { "id": "aceip0481", "seq": "KA", "length": "2", "detail": "Milk (human)", "source": "Milk", "ic50": "31.5 μM", "reference": "Three-dimensional holograph vector of atomic interaction field (3D-HoVAIF): a novel rotation-translation invariant 3D structure descriptor and its applications to peptides.; Peptides with angiotensin I converting enzyme (ACE) inhibitory activity generated from porcine skeletal muscle proteins by the action of meat-borne Lactobacillus.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1002\/psc.892; 10.1016\/j.jprot.2013.06.023; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "17654623 23806758 23871047", "mw": "217.27", "pi": "8.75", "charge_ph7": "0.76", "gravy": "-1.05", "instability": "5.0", "hydrophobic": "0.5", "boman": "-0.115", "helix": "1.0", "turn_pct": "0.0", "sheet": "0.0" }, { "id": "aceip0482", "seq": "KAFR", "length": "4", "detail": "Milk (bovine) | Milk (Casein) | Milk-Cheese (Sheep milk and cheeses proteins) | Milk (Ovine milk proteins) | Enzymatic-hydrolysis | Pork | Egg (Ovalbumin)", "source": "Milk | Synthesized | Porcine | Egg", "ic50": null, "reference": "Purification, activity and sequence of angiotensin I converting enzyme inhibitory peptide from alcalase hydrolysate of peanut flour.", "doi": "10.1021\/jf901787e", "pubmedid": "19886677", "mw": "520.62", "pi": "11.0", "charge_ph7": "1.76", "gravy": "-0.95", "instability": "7.5", "hydrophobic": "0.5", "boman": "-0.1225", "helix": "0.5", "turn_pct": "0.0", "sheet": "0.25" }, { "id": "aceip0483", "seq": "KAPVA", "length": "5", "detail": "Cereals (Wheat)", "source": "Cereal", "ic50": "46.56 μM", "reference": "Angiotensin I-converting enzyme inhibitory peptides generated from in vitro gastrointestinal digestion of pork meat.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1021\/jf904204n; 10.1016\/j.foodchem.2012.09.092; 10.1080\/10408398.2012.664829", "pubmedid": "20151679 23194537 24915368", "mw": "484.59", "pi": "8.75", "charge_ph7": "0.76", "gravy": "0.46", "instability": "85.04", "hydrophobic": "0.8", "boman": "-1.216", "helix": "0.6", "turn_pct": "0.2", "sheet": "0.2" }, { "id": "aceip0484", "seq": "KAVPYPQ", "length": "7", "detail": "Algae (Spirulina platensis)", "source": "Bacteria", "ic50": null, "reference": "Identification of angiotensin-I-converting enzyme inhibitory peptides derived from sodium caseinate hydrolysates produced by Lactobacillus helveticus NCC 2765.", "doi": "10.1021\/jf049510t", "pubmedid": "15537298", "mw": "801.93", "pi": "8.59", "charge_ph7": "0.76", "gravy": "-0.8429", "instability": "81.23", "hydrophobic": "0.5714", "boman": "-0.3957", "helix": "0.2857", "turn_pct": "0.2857", "sheet": "0.2857" }, { "id": "aceip0485", "seq": "KDERF", "length": "5", "detail": "ND", "source": "ND", "ic50": "10.0-848.0 μM", "reference": "Identification of novel angiotensin-converting enzyme-inhibitory peptides from ovine milk proteins by CE-MS and chromatographic techniques.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1002\/elps.200700324; 10.1080\/10408398.2012.664829", "pubmedid": "17948260 24915368", "mw": "693.75", "pi": "6.07", "charge_ph7": "-0.24", "gravy": "-2.52", "instability": "8.0", "hydrophobic": "0.2", "boman": "0.928", "helix": "0.4", "turn_pct": "0.2", "sheet": "0.2" }, { "id": "aceip0486", "seq": "KDI", "length": "3", "detail": "Milk (bovine)", "source": "Milk", "ic50": null, "reference": "Hot topic: Changes in angiotensin-converting enzyme inhibition and concentrations of the tripeptides Val-Pro-Pro and Ile-Pro-Pro during ripening of different Swiss cheese varieties.", "doi": "10.3168\/jds.2008-1531", "pubmedid": "19233775", "mw": "374.43", "pi": "5.84", "charge_ph7": "-0.24", "gravy": "-0.9667", "instability": "6.67", "hydrophobic": "0.3333", "boman": "-0.5533", "helix": "0.3333", "turn_pct": "0.3333", "sheet": "0.3333" }, { "id": "aceip0487", "seq": "KDYRL", "length": "5", "detail": "Milk (bovine)", "source": "Milk", "ic50": "26.5 μM", "reference": "Novel angiotensin I-converting enzyme inhibitory peptides isolated from Alcalase hydrolysate of mung bean protein.; Vegetable foods: a cheap source of proteins and peptides with antihypertensive, antioxidant, and other less occurrence bioactivities.", "doi": "10.1002\/psc.758; 10.1016\/j.talanta.2012.12.041", "pubmedid": "16680798 23598136", "mw": "693.79", "pi": "8.59", "charge_ph7": "0.76", "gravy": "-1.88", "instability": "-25.82", "hydrophobic": "0.2", "boman": "0.24", "helix": "0.4", "turn_pct": "0.2", "sheet": "0.4" }, { "id": "aceip0488", "seq": "KE", "length": "2", "detail": "Milk (bovine)", "source": "Milk", "ic50": "0 0", "reference": "Application of at-line two-dimensional liquid chromatography-mass spectrometry for identification of small hydrophilic angiotensin I-inhibiting peptides in milk hydrolysates.; Peptides with angiotensin I converting enzyme (ACE) inhibitory activity generated from porcine skeletal muscle proteins by the action of meat-borne Lactobacillus.", "doi": "10.1007\/s00216-008-1990-3; 10.1016\/j.jprot.2013.06.023", "pubmedid": "18392815 23806758", "mw": "275.3", "pi": "6.22", "charge_ph7": "-0.23", "gravy": "-3.7", "instability": "5.0", "hydrophobic": "0.0", "boman": "1.61", "helix": "1.0", "turn_pct": "0.0", "sheet": "0.0" }, { "id": "aceip0489", "seq": "KEIW", "length": "4", "detail": "Fish (Cuttlefish)", "source": "Fish", "ic50": null, "reference": "[Purification and identification of a novel ACE inhibitory peptide derived from the mud snail Bellamya purificata by RP-HPLC\/MALDI-TOF MS].", "doi": "", "pubmedid": "17432577", "mw": "574.67", "pi": "6.0", "charge_ph7": "-0.24", "gravy": "-0.95", "instability": "55.65", "hydrophobic": "0.5", "boman": "-1.0075", "helix": "0.5", "turn_pct": "0.0", "sheet": "0.5" }, { "id": "aceip0490", "seq": "KEKV", "length": "4", "detail": "ND", "source": "ND", "ic50": null, "reference": "Hot topic: Changes in angiotensin-converting enzyme inhibition and concentrations of the tripeptides Val-Pro-Pro and Ile-Pro-Pro during ripening of different Swiss cheese varieties.", "doi": "10.3168\/jds.2008-1531", "pubmedid": "19233775", "mw": "502.6", "pi": "8.59", "charge_ph7": "0.76", "gravy": "-1.775", "instability": "-13.73", "hydrophobic": "0.25", "boman": "0.19", "helix": "0.75", "turn_pct": "0.0", "sheet": "0.25" }, { "id": "aceip0491", "seq": "KF", "length": "2", "detail": "ND", "source": "ND", "ic50": "<20 mM", "reference": "Antihypertensive effects of Undaria pinnatifida (wakame) peptide on blood pressure in spontaneously hypertensive rats.; Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Quantitative structure-activity relationship study of bitter di- and tri-peptides including relationship with angiotensin I-converting enzyme inhibitory activity.; Inhibition strength of short peptides derived from an ACE inhibitory peptide.; Peptides with angiotensin I converting enzyme (ACE) inhibitory activity generated from porcine skeletal muscle proteins by the action of meat-borne Lactobacillus.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1016\/j.jnutbio.2003.11.004; 10.1021\/jf051263l; 10.1002\/psc.800; 10.1021\/jf202902r; 10.1016\/j.jprot.2013.06.023; 10.1016\/j.foodchem.2013.05.140; 10.1080\/10408398.2012.664829", "pubmedid": "15135150 16448176 17117396 21923188 23806758 23871047 24915368", "mw": "293.36", "pi": "8.75", "charge_ph7": "0.76", "gravy": "-0.55", "instability": "5.0", "hydrophobic": "0.5", "boman": "-0.7", "helix": "0.5", "turn_pct": "0.0", "sheet": "0.5" }, { "id": "aceip0492", "seq": "KFAR", "length": "4", "detail": "Spinach", "source": "Plants", "ic50": "16.9 mg\/ml", "reference": "Purification, activity and sequence of angiotensin I converting enzyme inhibitory peptide from alcalase hydrolysate of peanut flour.", "doi": "10.1021\/jf901787e", "pubmedid": "19886677", "mw": "520.63", "pi": "11.0", "charge_ph7": "1.76", "gravy": "-0.95", "instability": "7.5", "hydrophobic": "0.5", "boman": "-0.1225", "helix": "0.5", "turn_pct": "0.0", "sheet": "0.25" }, { "id": "aceip0493", "seq": "KFAWPQ", "length": "6", "detail": "Milk", "source": "Milk", "ic50": "177.1 μM", "reference": "Angiotensin-converting enzyme inhibitory activity of peptides derived from caprine kefir.", "doi": "10.3168\/jds.S0022-0302(05)73032-0", "pubmedid": "16162521", "mw": "775.89", "pi": "8.75", "charge_ph7": "0.76", "gravy": "-0.8833", "instability": "40.43", "hydrophobic": "0.6667", "boman": "-0.6967", "helix": "0.3333", "turn_pct": "0.1667", "sheet": "0.3333" }, { "id": "aceip0494", "seq": "KFYG", "length": "4", "detail": "Legume (Pea proteins)", "source": "Legume", "ic50": "90.5 μM", "reference": "Identification of an antihypertensive peptide from peptic digest of wakame (Undaria pinnatifida).; Review on the angiotensin-I-converting enzyme (ACE) inhibitor peptides from marine proteins.; Vegetable foods: a cheap source of proteins and peptides with antihypertensive, antioxidant, and other less occurrence bioactivities.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1016\/s0955-2863(00)00110-8; 10.1007\/s12010-012-0024-y; 10.1016\/j.talanta.2012.12.041; 10.1016\/j.foodchem.2013.05.140; 10.1080\/10408398.2012.664829", "pubmedid": "11091100 23271625 23598136 23871047 24915368", "mw": "513.59", "pi": "8.59", "charge_ph7": "0.76", "gravy": "-0.7", "instability": "67.78", "hydrophobic": "0.25", "boman": "-0.55", "helix": "0.25", "turn_pct": "0.25", "sheet": "0.5" }, { "id": "aceip0495", "seq": "KG", "length": "2", "detail": "Milk (bovine) | Carp | Cereals | Pork | Chicken", "source": "Milk | Fish | Cereal | Porcine | Chicken", "ic50": "<20 mM", "reference": "Binding of peptide substrates and inhibitors of angiotensin-converting enzyme. Importance of the COOH-terminal dipeptide sequence.; Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Three-dimensional holograph vector of atomic interaction field (3D-HoVAIF): a novel rotation-translation invariant 3D structure descriptor and its applications to peptides.; QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.; Peptides with angiotensin I converting enzyme (ACE) inhibitory activity generated from porcine skeletal muscle proteins by the action of meat-borne Lactobacillus.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1021\/jf051263l; 10.1002\/psc.892; 10.1007\/s00894-010-0862-x; 10.1016\/j.jprot.2013.06.023; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "6243277 16448176 17654623 20941517 23806758 23871047", "mw": "203.24", "pi": "8.75", "charge_ph7": "0.76", "gravy": "-2.15", "instability": "-37.45", "hydrophobic": "0.0", "boman": "0.32", "helix": "0.5", "turn_pct": "0.5", "sheet": "0.0" }, { "id": "aceip0496", "seq": "KGYGGVSL", "length": "8", "detail": "Chicken", "source": "Chicken", "ic50": "300.9 μM", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "23194537", "mw": "779.88", "pi": "8.59", "charge_ph7": "0.76", "gravy": "0.1", "instability": "-7.66", "hydrophobic": "0.25", "boman": "-1.1525", "helix": "0.25", "turn_pct": "0.5", "sheet": "0.375" }, { "id": "aceip0497", "seq": "KGYGGVSLPEW", "length": "11", "detail": "Meat", "source": "Meat", "ic50": "0.7 μM", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "23194537", "mw": "1192.32", "pi": "6.0", "charge_ph7": "-0.24", "gravy": "-0.4727", "instability": "16.8", "hydrophobic": "0.3636", "boman": "-0.9009", "helix": "0.2727", "turn_pct": "0.4545", "sheet": "0.3636" }, { "id": "aceip0498", "seq": "KHIQKEDVPSER", "length": "12", "detail": "Catfish", "source": "Fish", "ic50": null, "reference": "Casein fermentate of Lactobacillus animalis DPC6134 contains a range of novel propeptide angiotensin-converting enzyme inhibitors.", "doi": "10.1128\/AEM.00096-07", "pubmedid": "17483275", "mw": "1465.61", "pi": "6.76", "charge_ph7": "-0.15", "gravy": "-1.9333", "instability": "109.98", "hydrophobic": "0.25", "boman": "0.4225", "helix": "0.3333", "turn_pct": "0.25", "sheet": "0.1667" }, { "id": "aceip0499", "seq": "KIHPFAQAQ", "length": "9", "detail": "Fish (Catfish)", "source": "Fish", "ic50": "132.6 μM", "reference": "Angiotensin-converting enzyme inhibitory activity of peptides derived from caprine kefir.", "doi": "10.3168\/jds.S0022-0302(05)73032-0", "pubmedid": "16162521", "mw": "1039.19", "pi": "8.76", "charge_ph7": "0.85", "gravy": "-0.5333", "instability": "31.37", "hydrophobic": "0.5556", "boman": "-0.6922", "helix": "0.3333", "turn_pct": "0.1111", "sheet": "0.2222" }, { "id": "aceip0500", "seq": "KIHPFAQTQSLVYP", "length": "14", "detail": "ND", "source": "ND", "ic50": "39 μM", "reference": "Inhibition of angiotensin-converting enzyme by synthetic peptide fragments of various beta-caseins.; Evaluation of the allergenicity of goat milk, cow milk, and their lactosera in a guinea pig model.", "doi": "10.3168\/jds.2008-1125", "pubmedid": "1368548 19233776", "mw": "1628.87", "pi": "8.6", "charge_ph7": "0.85", "gravy": "-0.2143", "instability": "53.16", "hydrophobic": "0.5", "boman": "-0.8671", "helix": "0.2143", "turn_pct": "0.2143", "sheet": "0.4286" }, { "id": "aceip0501", "seq": "KIYPSFQPQPLIYP", "length": "14", "detail": "Milk | Cereals", "source": "Milk | Cereal", "ic50": "8.6 μM", "reference": "Inhibition of angiotensin-converting enzyme by synthetic peptide fragments of various beta-caseins.", "doi": "", "pubmedid": "1368548", "mw": "1690.98", "pi": "8.5", "charge_ph7": "0.76", "gravy": "-0.3643", "instability": "75.88", "hydrophobic": "0.5714", "boman": "-0.88", "helix": "0.1429", "turn_pct": "0.3571", "sheet": "0.4286" }, { "id": "aceip0502", "seq": "KKYMVPQL", "length": "8", "detail": "Oat", "source": "Cereal", "ic50": "77.1 μM", "reference": "Antihypertensive peptides: production, bioavailability and incorporation into foods.", "doi": "10.1016\/j.cis.2010.11.001", "pubmedid": "21185549", "mw": "1006.26", "pi": "9.7", "charge_ph7": "1.76", "gravy": "-0.5375", "instability": "111.83", "hydrophobic": "0.5", "boman": "-0.8312", "helix": "0.5", "turn_pct": "0.125", "sheet": "0.375" }, { "id": "aceip0503", "seq": "KKYNVPQL", "length": "8", "detail": "Arachin", "source": "Legume", "ic50": "77.1 mM", "reference": "Changes in arterial blood pressure after single oral administration of milk-casein-derived peptides in spontaneously hypertensive rats.", "doi": "10.1002\/mnfr.200900448", "pubmedid": "20397194", "mw": "989.17", "pi": "9.7", "charge_ph7": "1.76", "gravy": "-1.2125", "instability": "56.9", "hydrophobic": "0.375", "boman": "-0.335", "helix": "0.375", "turn_pct": "0.25", "sheet": "0.375" }, { "id": "aceip0504", "seq": "KL", "length": "2", "detail": "Milk", "source": "Milk", "ic50": "50.2 μM", "reference": "Peptides with angiotensin I converting enzyme (ACE) inhibitory activity generated from porcine skeletal muscle proteins by the action of meat-borne Lactobacillus.", "doi": "10.1016\/j.jprot.2013.06.023", "pubmedid": "23806758", "mw": "259.35", "pi": "8.75", "charge_ph7": "0.76", "gravy": "-0.05", "instability": "-37.45", "hydrophobic": "0.5", "boman": "-1.67", "helix": "1.0", "turn_pct": "0.0", "sheet": "0.5" }, { "id": "aceip0505", "seq": "KLKFV", "length": "5", "detail": "Oat | Legume (Peanut)", "source": "Cereal | Legume", "ic50": "30.2 μM", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "23194537", "mw": "633.82", "pi": "10.0", "charge_ph7": "1.76", "gravy": "0.6", "instability": "-25.96", "hydrophobic": "0.6", "boman": "-1.756", "helix": "0.6", "turn_pct": "0.0", "sheet": "0.6" }, { "id": "aceip0506", "seq": "KLP", "length": "3", "detail": "Milk (bovine) | Royal jelly | Tuna | Cereals | Cereals (Wheat) | Soybean Sauce | Pork | Chicken", "source": "Milk | Insect | Fish | Cereal | Legume | Porcine | Chicken", "ic50": "500 μM", "reference": "Angiotensin I-converting enzyme inhibitory peptides generated from in vitro gastrointestinal digestion of pork meat.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1021\/jf904204n; 10.1016\/j.foodchem.2013.05.140; 10.1080\/10408398.2012.664829", "pubmedid": "20151679 23871047 24915368", "mw": "356.46", "pi": "8.75", "charge_ph7": "0.76", "gravy": "-0.5667", "instability": "42.57", "hydrophobic": "0.6667", "boman": "-1.1133", "helix": "0.6667", "turn_pct": "0.3333", "sheet": "0.3333" }, { "id": "aceip0507", "seq": "KLPAGTLF", "length": "8", "detail": "Tuna | Cereals", "source": "Fish | Cereal", "ic50": "13.4 μM", "reference": "Novel angiotensin I-converting enzyme inhibitory peptides isolated from Alcalase hydrolysate of mung bean protein.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1002\/psc.758; 10.1080\/10408398.2012.664829", "pubmedid": "16680798 24915368", "mw": "846.02", "pi": "8.75", "charge_ph7": "0.76", "gravy": "0.7", "instability": "35.67", "hydrophobic": "0.625", "boman": "-1.7163", "helix": "0.5", "turn_pct": "0.25", "sheet": "0.5" }, { "id": "aceip0508", "seq": "KP", "length": "2", "detail": "Soybean | Soybean (Fermented) | Soybean (Tofoyu)", "source": "Legume", "ic50": "<20 mM", "reference": "Angiotensin I-converting enzyme inhibitory activity and insulin secretion stimulative activity of fermented fish sauce.; Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Quantitative structure-activity relationship study of bitter di- and tri-peptides including relationship with angiotensin I-converting enzyme inhibitory activity.; Review on the angiotensin-I-converting enzyme (ACE) inhibitor peptides from marine proteins.; Peptides with angiotensin I converting enzyme (ACE) inhibitory activity generated from porcine skeletal muscle proteins by the action of meat-borne Lactobacillus.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1016\/S1389-1723(03)70138-8; 10.1021\/jf051263l; 10.1002\/psc.800; 10.1007\/s12010-012-0024-y; 10.1016\/j.jprot.2013.06.023; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "16233562 16448176 17117396 23271625 23806758 23871047", "mw": "243.3", "pi": "8.75", "charge_ph7": "0.76", "gravy": "-2.75", "instability": "-32.7", "hydrophobic": "0.5", "boman": "0.79", "helix": "0.5", "turn_pct": "0.5", "sheet": "0.0" }, { "id": "aceip0509", "seq": "KPF", "length": "3", "detail": "Shrimp", "source": "Shrimp", "ic50": null, "reference": "Quantitative structure-activity relationship study of bitter di- and tri-peptides including relationship with angiotensin I-converting enzyme inhibitory activity.; QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1002\/psc.800; 10.1007\/s00894-010-0862-x; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "17117396 20941517 23871047", "mw": "390.48", "pi": "8.75", "charge_ph7": "0.76", "gravy": "-0.9", "instability": "45.73", "hydrophobic": "0.6667", "boman": "-0.4667", "helix": "0.3333", "turn_pct": "0.3333", "sheet": "0.3333" }, { "id": "aceip0510", "seq": "KPK", "length": "3", "detail": "Carp | Cereals (Wheat) | Pork", "source": "Fish | Cereal | Porcine", "ic50": null, "reference": "Quantitative structure-activity relationship study of bitter di- and tri-peptides including relationship with angiotensin I-converting enzyme inhibitory activity.; QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1002\/psc.800; 10.1007\/s00894-010-0862-x; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "17117396 20941517 23871047", "mw": "371.48", "pi": "10.0", "charge_ph7": "1.76", "gravy": "-3.1333", "instability": "-18.47", "hydrophobic": "0.3333", "boman": "1.0533", "helix": "0.6667", "turn_pct": "0.3333", "sheet": "0.0" }, { "id": "aceip0511", "seq": "KPPETV", "length": "6", "detail": "Nomura Jellyfish", "source": "Animal", "ic50": "24.1 μM", "reference": "Analysis of novel angiotensin-I-converting enzyme inhibitory peptides from protease-hydrolyzed marine shrimp Acetes chinensis.; Review on the angiotensin-I-converting enzyme (ACE) inhibitor peptides from marine proteins.", "doi": "10.1002\/psc.789; 10.1007\/s12010-012-0024-y", "pubmedid": "16981241 23271625", "mw": "669.77", "pi": "6.0", "charge_ph7": "-0.24", "gravy": "-1.1833", "instability": "56.83", "hydrophobic": "0.5", "boman": "-0.0933", "helix": "0.3333", "turn_pct": "0.3333", "sheet": "0.3333" }, { "id": "aceip0512", "seq": "KR", "length": "2", "detail": "ND", "source": "ND", "ic50": "380 μM", "reference": "Peptides with angiotensin I converting enzyme (ACE) inhibitory activity generated from porcine skeletal muscle proteins by the action of meat-borne Lactobacillus.", "doi": "10.1016\/j.jprot.2013.06.023", "pubmedid": "23806758", "mw": "302.37", "pi": "11.0", "charge_ph7": "1.76", "gravy": "-4.2", "instability": "168.0", "hydrophobic": "0.0", "boman": "2.15", "helix": "0.5", "turn_pct": "0.0", "sheet": "0.0" }, { "id": "aceip0513", "seq": "KRQKYDI", "length": "7", "detail": "Milk", "source": "Milk", "ic50": "26.2 26.2", "reference": "Porcine skeletal muscle troponin is a good source of peptides with Angiotensin-I converting enzyme inhibitory activity and antihypertensive effects in spontaneously hypertensive rats.; Antihypertensive peptides from food proteins: a review.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1021\/jf071408j; 10.1039\/c2fo10192k; 10.1080\/10408398.2012.664829", "pubmedid": "18163567 22249830 24915368", "mw": "950.09", "pi": "9.7", "charge_ph7": "1.76", "gravy": "-2.3", "instability": "116.49", "hydrophobic": "0.1429", "boman": "0.5914", "helix": "0.2857", "turn_pct": "0.1429", "sheet": "0.2857" }, { "id": "aceip0514", "seq": "KRVIQY", "length": "6", "detail": "Chicken", "source": "Chicken", "ic50": "6.1 μM", "reference": "Antihypertensive peptides from food proteins: a review.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1039\/c2fo10192k; 10.1080\/10408398.2012.664829", "pubmedid": "22249830 24915368", "mw": "805.96", "pi": "9.99", "charge_ph7": "1.76", "gravy": "-0.75", "instability": "50.1", "hydrophobic": "0.3333", "boman": "-0.5267", "helix": "0.1667", "turn_pct": "0.0", "sheet": "0.5" }, { "id": "aceip0515", "seq": "KTAP", "length": "4", "detail": "Milk (bovine)", "source": "Milk", "ic50": "37 μM", "reference": "Inhibition of angiotensin-converting enzyme by synthetic peptide fragments of human kappa-casein.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1016\/j.foodchem.2013.05.140", "pubmedid": "1368540 23871047", "mw": "415.48", "pi": "8.75", "charge_ph7": "0.76", "gravy": "-1.1", "instability": "55.65", "hydrophobic": "0.5", "boman": "0.0075", "helix": "0.5", "turn_pct": "0.25", "sheet": "0.25" }, { "id": "aceip0516", "seq": "KVAGPK", "length": "6", "detail": "Meat", "source": "Meat", "ic50": "305 μM", "reference": "Novel angiotensin I-converting enzyme inhibitory peptides derived from edible mushroom Agaricus bisporus (J.E. Lange) Imbach identified by LC-MS\/MS.", "doi": "10.1016\/j.foodchem.2013.10.053", "pubmedid": "24262574", "mw": "598.74", "pi": "10.0", "charge_ph7": "1.76", "gravy": "-0.6333", "instability": "-5.82", "hydrophobic": "0.5", "boman": "-0.605", "helix": "0.5", "turn_pct": "0.3333", "sheet": "0.1667" }, { "id": "aceip0517", "seq": "KVLAGM", "length": "6", "detail": "Fish", "source": "Fish", "ic50": "30 μM", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "23194537", "mw": "617.8", "pi": "8.75", "charge_ph7": "0.76", "gravy": "1.2333", "instability": "-5.82", "hydrophobic": "0.6667", "boman": "-2.08", "helix": "0.6667", "turn_pct": "0.1667", "sheet": "0.3333" }, { "id": "aceip0518", "seq": "KVLPVP", "length": "6", "detail": "Milk (bovine)", "source": "Milk", "ic50": "4.6 μM", "reference": "Identification of an antihypertensive peptide from casein hydrolysate produced by a proteinase from Lactobacillus helveticus CP790.; Evaluation of the allergenicity of goat milk, cow milk, and their lactosera in a guinea pig model.; Ala-Val-Phe and Val-Phe: ACE inhibitory peptides derived from insect protein with antihypertensive activity in spontaneously hypertensive rats.; Antihypertensive peptides: production, bioavailability and incorporation into foods.; Antihypertensive peptides from food proteins: a review.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.3168\/jds.S0022-0302(96)76487-1; 10.3168\/jds.2008-1125; 10.1016\/j.peptides.2009.05.029; 10.1016\/j.cis.2010.11.001; 10.1039\/c2fo10192k; 10.1016\/j.foodchem.2012.09.092", "pubmedid": "8880454 19233776 19524628 21185549 22249830 23194537", "mw": "651.84", "pi": "8.75", "charge_ph7": "0.76", "gravy": "0.85", "instability": "90.48", "hydrophobic": "0.8333", "boman": "-1.9033", "helix": "0.3333", "turn_pct": "0.3333", "sheet": "0.5" }, { "id": "aceip0519", "seq": "KVLPVPQ", "length": "7", "detail": "Meat", "source": "Meat", "ic50": "522.67 μM", "reference": "Identification of an antihypertensive peptide from casein hydrolysate produced by a proteinase from Lactobacillus helveticus CP790.; Identification of angiotensin-I-converting enzyme inhibitory peptides derived from sodium caseinate hydrolysates produced by Lactobacillus helveticus NCC 2765.; Evaluation of the allergenicity of goat milk, cow milk, and their lactosera in a guinea pig model.; Ala-Val-Phe and Val-Phe: ACE inhibitory peptides derived from insect protein with antihypertensive activity in spontaneously hypertensive rats.; Antihypertensive peptides: production, bioavailability and incorporation into foods.; Bioactive peptides derived from milk proteins and their health beneficial potentials: an update.; Antihypertensive peptides from food proteins: a review.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.; VPPIPP and IPPVPP: two hexapeptides innovated to exert antihypertensive activity.", "doi": "10.3168\/jds.S0022-0302(96)76487-1; 10.1021\/jf049510t; 10.3168\/jds.2008-1125; 10.1016\/j.peptides.2009.05.029; 10.1016\/j.cis.2010.11.001; 10.1039\/c0fo00016g; 10.1039\/c2fo10192k; 10.1016\/j.foodchem.2012.09.092; 10.1371\/journal.pone.0062384", "pubmedid": "8880454 15537298 19233776 19524628 21185549 21773582 22249830 23194537 23638059", "mw": "779.97", "pi": "8.75", "charge_ph7": "0.76", "gravy": "0.2286", "instability": "106.5", "hydrophobic": "0.7143", "boman": "-1.4371", "helix": "0.2857", "turn_pct": "0.2857", "sheet": "0.4286" }, { "id": "aceip0520", "seq": "KVREGT", "length": "6", "detail": "Milk", "source": "Milk", "ic50": "9.1 μM", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "23194537", "mw": "688.77", "pi": "8.75", "charge_ph7": "0.76", "gravy": "-1.4667", "instability": "-19.97", "hydrophobic": "0.1667", "boman": "0.2033", "helix": "0.3333", "turn_pct": "0.1667", "sheet": "0.3333" }, { "id": "aceip0521", "seq": "KVREGTTY", "length": "8", "detail": "Milk", "source": "Milk", "ic50": "102.8 μM", "reference": "Glutamine pretreatment reduces IL-8 production in human intestinal epithelial cells by limiting IkappaBalpha ubiquitination.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1093\/jn\/136.6.1461; 10.1016\/j.foodchem.2012.09.092; 10.1080\/10408398.2012.664829", "pubmedid": "16702304 23194537 24915368", "mw": "953.05", "pi": "8.59", "charge_ph7": "0.76", "gravy": "-1.35", "instability": "-12.48", "hydrophobic": "0.125", "boman": "0.2025", "helix": "0.25", "turn_pct": "0.125", "sheet": "0.5" }, { "id": "aceip0522", "seq": "KW", "length": "2", "detail": "Human", "source": "Human", "ic50": "<20 mM", "reference": "Angiotensin I-converting enzyme inhibitory peptides in an alkaline protease hydrolyzate derived from sardine muscle.; Antihypertensive effects of Undaria pinnatifida (wakame) peptide on blood pressure in spontaneously hypertensive rats.; Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Inhibition strength of short peptides derived from an ACE inhibitory peptide.; Peptides with angiotensin I converting enzyme (ACE) inhibitory activity generated from porcine skeletal muscle proteins by the action of meat-borne Lactobacillus.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1271\/bbb.58.2244; 10.1016\/j.jnutbio.2003.11.004; 10.1021\/jf051263l; 10.1021\/jf202902r; 10.1016\/j.jprot.2013.06.023; 10.1080\/10408398.2012.664829", "pubmedid": "7765718 15135150 16448176 21923188 23806758 24915368", "mw": "332.4", "pi": "8.75", "charge_ph7": "0.76", "gravy": "-2.4", "instability": "5.0", "hydrophobic": "0.5", "boman": "-0.375", "helix": "0.5", "turn_pct": "0.0", "sheet": "0.5" }, { "id": "aceip0523", "seq": "KWL", "length": "3", "detail": "Milk (bovine)", "source": "Milk", "ic50": "43.6 μM", "reference": "Inhibition strength of short peptides derived from an ACE inhibitory peptide.", "doi": "10.1021\/jf202902r", "pubmedid": "21923188", "mw": "445.56", "pi": "8.75", "charge_ph7": "0.76", "gravy": "-0.3333", "instability": "47.8", "hydrophobic": "0.6667", "boman": "-1.89", "helix": "0.6667", "turn_pct": "0.0", "sheet": "0.6667" }, { "id": "aceip0524", "seq": "KWLP", "length": "4", "detail": "Meat", "source": "Meat", "ic50": "5 μM", "reference": "Inhibition strength of short peptides derived from an ACE inhibitory peptide.", "doi": "10.1021\/jf202902r", "pubmedid": "21923188", "mw": "542.67", "pi": "8.75", "charge_ph7": "0.76", "gravy": "-0.65", "instability": "86.5", "hydrophobic": "0.75", "boman": "-1.4175", "helix": "0.5", "turn_pct": "0.25", "sheet": "0.5" }, { "id": "aceip0525", "seq": "KY", "length": "2", "detail": "ND", "source": "ND", "ic50": "<20 mM", "reference": "Antihypertensive effects of Undaria pinnatifida (wakame) peptide on blood pressure in spontaneously hypertensive rats.; Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Antihypertensive peptides from food proteins: a review.; Review on the angiotensin-I-converting enzyme (ACE) inhibitor peptides from marine proteins.; Vegetable foods: a cheap source of proteins and peptides with antihypertensive, antioxidant, and other less occurrence bioactivities.; Peptides with angiotensin I converting enzyme (ACE) inhibitory activity generated from porcine skeletal muscle proteins by the action of meat-borne Lactobacillus.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1016\/j.jnutbio.2003.11.004; 10.1021\/jf051263l; 10.1039\/c2fo10192k; 10.1007\/s12010-012-0024-y; 10.1016\/j.talanta.2012.12.041; 10.1016\/j.jprot.2013.06.023; 10.1016\/j.foodchem.2013.05.140; 10.1080\/10408398.2012.664829", "pubmedid": "15135150 16448176 22249830 23271625 23598136 23806758 23871047 24915368", "mw": "309.36", "pi": "8.59", "charge_ph7": "0.76", "gravy": "-2.6", "instability": "5.0", "hydrophobic": "0.0", "boman": "0.86", "helix": "0.5", "turn_pct": "0.0", "sheet": "0.5" }, { "id": "aceip0526", "seq": "KYPVEPFTESQSLTL", "length": "15", "detail": "Milk (caprine)", "source": "Milk", "ic50": "93 mM\/L", "reference": "Antihypertensive effect of the peptides derived from casein by an extracellular proteinase from Lactobacillus helveticus CP790.", "doi": "10.3168\/jds.S0022-0302(94)77026-0", "pubmedid": "8201050", "mw": "1738.93", "pi": "4.53", "charge_ph7": "-1.24", "gravy": "-0.4867", "instability": "123.89", "hydrophobic": "0.4", "boman": "-0.5533", "helix": "0.3333", "turn_pct": "0.2667", "sheet": "0.4667" }, { "id": "aceip0527", "seq": "KYPVEPFTESQSLTLTDVENLHL", "length": "23", "detail": "Milk | Casein | Sweet-potato", "source": "Milk | Potato", "ic50": null, "reference": "Identification of angiotensin-I-converting enzyme inhibitory peptides derived from sodium caseinate hydrolysates produced by Lactobacillus helveticus NCC 2765.", "doi": "10.1021\/jf049510t", "pubmedid": "15537298", "mw": "2660.92", "pi": "4.4", "charge_ph7": "-3.15", "gravy": "-0.4304", "instability": "84.28", "hydrophobic": "0.3913", "boman": "-0.6952", "helix": "0.3478", "turn_pct": "0.2609", "sheet": "0.4783" }, { "id": "aceip0528", "seq": "KYPVQPFTESQSLTL", "length": "15", "detail": "Meat", "source": "Meat", "ic50": "44 μM", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "23194537", "mw": "1737.95", "pi": "6.0", "charge_ph7": "-0.24", "gravy": "-0.4867", "instability": "123.89", "hydrophobic": "0.4", "boman": "-0.572", "helix": "0.2667", "turn_pct": "0.2667", "sheet": "0.4667" }, { "id": "aceip0529", "seq": "LA", "length": "2", "detail": "Fish | Meat", "source": "Fish | Meat", "ic50": "310 μM", "reference": "Three-dimensional holograph vector of atomic interaction field (3D-HoVAIF): a novel rotation-translation invariant 3D structure descriptor and its applications to peptides.; QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1002\/psc.892; 10.1007\/s00894-010-0862-x; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "17654623 20941517 23871047", "mw": "202.25", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "2.8", "instability": "5.0", "hydrophobic": "1.0", "boman": "-3.365", "helix": "1.0", "turn_pct": "0.0", "sheet": "0.5" }, { "id": "aceip0530", "seq": "LAA", "length": "3", "detail": "Milk", "source": "Milk", "ic50": "<20 mM", "reference": "Structures and activity of angiotensin-converting enzyme inhibitors in an alpha-zein hydrolysate.; Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Bioactive peptides in amaranth (Amaranthus hypochondriacus) seed.; Cellular membrane disruption by amyloid fibrils involved intermolecular disulfide cross-linking.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1021\/jf051263l; 10.1021\/jf072911z; 10.1021\/bi900219c; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "1368684 16448176 18211015 19449893 23871047", "mw": "273.33", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "2.4667", "instability": "6.67", "hydrophobic": "1.0", "boman": "-2.8467", "helix": "1.0", "turn_pct": "0.0", "sheet": "0.3333" }, { "id": "aceip0531", "seq": "LAHKAL", "length": "6", "detail": "Milk", "source": "Milk", "ic50": "621 μM", "reference": "Use of beta-cyclodextrin to decrease the level of cholesterol in milk fat.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.3168\/jds.2008-1452; 10.1016\/j.foodchem.2012.09.092", "pubmedid": "19233779 23194537", "mw": "651.8", "pi": "8.76", "charge_ph7": "0.85", "gravy": "0.6833", "instability": "33.65", "hydrophobic": "0.6667", "boman": "-1.815", "helix": "0.8333", "turn_pct": "0.0", "sheet": "0.3333" }, { "id": "aceip0532", "seq": "LALPP", "length": "5", "detail": "Legume (Pea proteins)", "source": "Legume", "ic50": "0 μM", "reference": "Inhibition of angiotensin-converting enzyme by synthetic peptide fragments of various beta-caseins.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "1368548 23194537", "mw": "509.64", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "1.24", "instability": "85.04", "hydrophobic": "1.0", "boman": "-2.33", "helix": "0.6", "turn_pct": "0.4", "sheet": "0.4" }, { "id": "aceip0533", "seq": "LAMA", "length": "4", "detail": "Milk | Meat", "source": "Milk | Meat", "ic50": "556 μM", "reference": "Bioactive peptides in amaranth (Amaranthus hypochondriacus) seed.", "doi": "10.1021\/jf072911z", "pubmedid": "18211015", "mw": "404.52", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "2.325", "instability": "38.35", "hydrophobic": "1.0", "boman": "-2.7225", "helix": "1.0", "turn_pct": "0.0", "sheet": "0.25" }, { "id": "aceip0534", "seq": "LANVST", "length": "6", "detail": "Amaranth | Synthesized | Bonito | Animal | Legume", "source": "Plants | Synthesized | Fish | Animal | Legume", "ic50": null, "reference": "Isolation and characterization of a bradykinin-potentiating peptide from a bovine peptic hemoglobin hydrolysate.", "doi": "10.1016\/0014-5793(92)80104-o", "pubmedid": "1544478", "mw": "603.67", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "0.8", "instability": "8.33", "hydrophobic": "0.5", "boman": "-1.3417", "helix": "0.3333", "turn_pct": "0.3333", "sheet": "0.5" }, { "id": "aceip0535", "seq": "LAP", "length": "3", "detail": "ND", "source": "ND", "ic50": "<20 mM", "reference": "Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Temporal gene expression and probiotic attributes of Lactobacillus acidophilus during growth in milk.; Vegetable foods: a cheap source of proteins and peptides with antihypertensive, antioxidant, and other less occurrence bioactivities.; Rational design of angiotensin-I-converting enzyme inhibitory peptides by integrating in silico modeling and an in vitro assay.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1021\/jf051263l; 10.3168\/jds.2008-1457; 10.1016\/j.talanta.2012.12.041; 10.1002\/cmdc.201300132; 10.1080\/10408398.2012.664829", "pubmedid": "16448176 19233780 23598136 23740817 24915368", "mw": "299.37", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "1.3333", "instability": "70.87", "hydrophobic": "1.0", "boman": "-2.2433", "helix": "0.6667", "turn_pct": "0.3333", "sheet": "0.3333" }, { "id": "aceip0536", "seq": "LAQ", "length": "3", "detail": "Bonito", "source": "Fish", "ic50": null, "reference": "Isolation from alpha-zein of thermolysin peptides with angiotensin I-converting enzyme inhibitory activity.; Cellular membrane disruption by amyloid fibrils involved intermolecular disulfide cross-linking.", "doi": "10.1271\/bbb.60.661; 10.1021\/bi900219c", "pubmedid": "8829536 19449893", "mw": "330.38", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "0.7", "instability": "6.67", "hydrophobic": "0.6667", "boman": "-1.79", "helix": "0.6667", "turn_pct": "0.0", "sheet": "0.3333" }, { "id": "aceip0537", "seq": "LAY", "length": "3", "detail": "ND", "source": "ND", "ic50": "<20 mM", "reference": "Structures and activity of angiotensin-converting enzyme inhibitors in an alpha-zein hydrolysate.; Isolation from alpha-zein of thermolysin peptides with angiotensin I-converting enzyme inhibitory activity.; Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Bioactive peptides in amaranth (Amaranthus hypochondriacus) seed.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1271\/bbb.60.661; 10.1021\/jf051263l; 10.1021\/jf072911z; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "1368684 8829536 16448176 18211015 23871047", "mw": "365.42", "pi": "5.52", "charge_ph7": "-0.24", "gravy": "1.4333", "instability": "6.67", "hydrophobic": "0.6667", "boman": "-2.1967", "helix": "0.6667", "turn_pct": "0.0", "sheet": "0.6667" }, { "id": "aceip0538", "seq": "LDAQSAPLR", "length": "9", "detail": "Synthesized | Food-protein | Chicken | Meat", "source": "Synthesized | Chicken | Meat", "ic50": "635 μM", "reference": "Angiotensin I-converting enzyme inhibitory properties of whey protein digests: concentration and characterization of active peptides.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1017\/s0022029999003982; 10.1016\/j.foodchem.2012.09.092", "pubmedid": "10717843 23194537", "mw": "970.08", "pi": "5.84", "charge_ph7": "-0.24", "gravy": "-0.3", "instability": "100.51", "hydrophobic": "0.5556", "boman": "-0.7622", "helix": "0.4444", "turn_pct": "0.3333", "sheet": "0.2222" }, { "id": "aceip0539", "seq": "LDIQK", "length": "5", "detail": "Tuna", "source": "Fish", "ic50": "27.6 μM", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "23194537", "mw": "615.72", "pi": "5.84", "charge_ph7": "-0.24", "gravy": "-0.52", "instability": "8.0", "hydrophobic": "0.4", "boman": "-1.044", "helix": "0.4", "turn_pct": "0.2", "sheet": "0.4" }, { "id": "aceip0540", "seq": "LDL", "length": "3", "detail": "Arachin", "source": "Legume", "ic50": null, "reference": "Quantitative structure-activity relationship study of bitter di- and tri-peptides including relationship with angiotensin I-converting enzyme inhibitory activity.; QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1002\/psc.800; 10.1007\/s00894-010-0862-x; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "17117396 20941517 23871047", "mw": "359.42", "pi": "4.05", "charge_ph7": "-1.24", "gravy": "1.3667", "instability": "6.67", "hydrophobic": "0.6667", "boman": "-2.72", "helix": "0.6667", "turn_pct": "0.3333", "sheet": "0.6667" }, { "id": "aceip0541", "seq": "LE", "length": "2", "detail": "ND", "source": "ND", "ic50": null, "reference": "Quantitative structure-activity relationship study of bitter di- and tri-peptides including relationship with angiotensin I-converting enzyme inhibitory activity.", "doi": "10.1002\/psc.800", "pubmedid": "17117396", "mw": "260.29", "pi": "4.6", "charge_ph7": "-1.23", "gravy": "0.15", "instability": "5.0", "hydrophobic": "0.5", "boman": "-1.64", "helix": "1.0", "turn_pct": "0.0", "sheet": "0.5" }, { "id": "aceip0542", "seq": "LEE", "length": "3", "detail": "Milk (bovine) | Milk (human) | Amaranth | Cereals (Wheat) | Chicken", "source": "Milk | Plants | Cereal | Chicken", "ic50": "<20 mM", "reference": "Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.", "doi": "10.1021\/jf051263l", "pubmedid": "16448176", "mw": "389.4", "pi": "4.24", "charge_ph7": "-2.23", "gravy": "-1.0667", "instability": "115.33", "hydrophobic": "0.3333", "boman": "-0.5467", "helix": "1.0", "turn_pct": "0.0", "sheet": "0.3333" }, { "id": "aceip0543", "seq": "LEF", "length": "3", "detail": "Sweet-potato", "source": "Potato", "ic50": "<10 μM", "reference": "LC-MS\/MS coupled with QSAR modeling in characterising of angiotensin I-converting enzyme inhibitory peptides from soybean proteins.", "doi": "10.1016\/j.foodchem.2013.04.064", "pubmedid": "23871011", "mw": "407.46", "pi": "4.05", "charge_ph7": "-1.24", "gravy": "1.0333", "instability": "6.67", "hydrophobic": "0.6667", "boman": "-2.0867", "helix": "0.6667", "turn_pct": "0.0", "sheet": "0.6667" }, { "id": "aceip0544", "seq": "LEIAKNGLSTTSNPKR", "length": "16", "detail": "Royal jelly", "source": "Insect", "ic50": null, "reference": "High throughput screening of bradykinin-potentiating peptides in Bothrops moojeni snake venom using precursor ion mass spectrometry.", "doi": "10.1016\/j.toxicon.2008.02.019", "pubmedid": "18471845", "mw": "1728.94", "pi": "9.99", "charge_ph7": "1.76", "gravy": "-0.8688", "instability": "30.59", "hydrophobic": "0.3125", "boman": "-0.2844", "helix": "0.375", "turn_pct": "0.375", "sheet": "0.3125" }, { "id": "aceip0545", "seq": "LEIVPK", "length": "6", "detail": "ND", "source": "ND", "ic50": ">1000 μM", "reference": "Angiotensin-converting enzyme inhibitory activity of peptides derived from caprine kefir.; Enterococcus faecalis strains from food, environmental, and clinical origin produce ACE-inhibitory peptides and other bioactive peptides during growth in bovine skim milk.", "doi": "10.3168\/jds.S0022-0302(05)73032-0; 10.1016\/j.ijfoodmicro.2013.06.019", "pubmedid": "16162521 23845432", "mw": "697.86", "pi": "6.0", "charge_ph7": "-0.24", "gravy": "0.5833", "instability": "58.38", "hydrophobic": "0.6667", "boman": "-1.7767", "helix": "0.5", "turn_pct": "0.1667", "sheet": "0.5" }, { "id": "aceip0546", "seq": "LEK", "length": "3", "detail": "ND", "source": "ND", "ic50": "<20 mM", "reference": "Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Inhibition strength of short peptides derived from an ACE inhibitory peptide.", "doi": "10.1021\/jf051263l; 10.1021\/jf202902r", "pubmedid": "16448176 21923188", "mw": "388.46", "pi": "6.0", "charge_ph7": "-0.24", "gravy": "-1.2", "instability": "6.67", "hydrophobic": "0.3333", "boman": "-0.5667", "helix": "1.0", "turn_pct": "0.0", "sheet": "0.3333" }, { "id": "aceip0547", "seq": "LEL", "length": "3", "detail": "Milk", "source": "Milk", "ic50": null, "reference": "Quantitative structure-activity relationship study of bitter di- and tri-peptides including relationship with angiotensin I-converting enzyme inhibitory activity.; QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1002\/psc.800; 10.1007\/s00894-010-0862-x; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "17117396 20941517 23871047", "mw": "373.44", "pi": "4.05", "charge_ph7": "-1.24", "gravy": "1.3667", "instability": "6.67", "hydrophobic": "0.6667", "boman": "-2.7333", "helix": "1.0", "turn_pct": "0.0", "sheet": "0.6667" }, { "id": "aceip0548", "seq": "LENLHLP", "length": "7", "detail": "Casein", "source": "Milk", "ic50": ">1000 μM", "reference": "Inhibition of angiotensin-converting enzyme by synthetic peptide fragments of various beta-caseins.", "doi": "", "pubmedid": "1368548", "mw": "834.96", "pi": "5.24", "charge_ph7": "-1.15", "gravy": "-0.0571", "instability": "36.09", "hydrophobic": "0.5714", "boman": "-1.5014", "helix": "0.5714", "turn_pct": "0.2857", "sheet": "0.4286" }, { "id": "aceip0549", "seq": "LENLHLPLP", "length": "9", "detail": "Milk | Meat", "source": "Milk | Meat", "ic50": "86 μM", "reference": "Inhibition of angiotensin-converting enzyme by synthetic peptide fragments of various beta-caseins.", "doi": "", "pubmedid": "1368548", "mw": "1045.23", "pi": "5.24", "charge_ph7": "-1.15", "gravy": "0.2", "instability": "51.69", "hydrophobic": "0.6667", "boman": "-1.7144", "helix": "0.5556", "turn_pct": "0.3333", "sheet": "0.4444" }, { "id": "aceip0550", "seq": "LEP", "length": "3", "detail": "Casein", "source": "Milk", "ic50": "<10 μM", "reference": "Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; ACE inhibitory tetrapeptides from Amaranthus hypochondriacus 11S globulin.", "doi": "10.1021\/jf051263l; 10.1016\/j.phytochem.2009.04.006", "pubmedid": "16448176 19443002", "mw": "357.4", "pi": "4.05", "charge_ph7": "-1.24", "gravy": "-0.4333", "instability": "70.87", "hydrophobic": "0.6667", "boman": "-1.0933", "helix": "0.6667", "turn_pct": "0.3333", "sheet": "0.3333" }, { "id": "aceip0551", "seq": "LEPP", "length": "4", "detail": "Cereals (Buckwheat)", "source": "Cereal", "ic50": null, "reference": "What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1016\/j.foodchem.2013.05.140", "pubmedid": "23871047", "mw": "454.52", "pi": "4.05", "charge_ph7": "-1.24", "gravy": "-0.725", "instability": "103.8", "hydrophobic": "0.75", "boman": "-0.82", "helix": "0.5", "turn_pct": "0.5", "sheet": "0.25" }, { "id": "aceip0552", "seq": "LF", "length": "2", "detail": "Milk (whey)", "source": "Milk", "ic50": "<20 mM", "reference": "Isolation from alpha-zein of thermolysin peptides with angiotensin I-converting enzyme inhibitory activity.; Angiotensin I-converting enzyme inhibitory peptides in a hydrolyzed chicken breast muscle extract.; Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Quantitative structure-activity relationship study of bitter di- and tri-peptides including relationship with angiotensin I-converting enzyme inhibitory activity.; Three-dimensional holograph vector of atomic interaction field (3D-HoVAIF): a novel rotation-translation invariant 3D structure descriptor and its applications to peptides.; Bioactive peptides in amaranth (Amaranthus hypochondriacus) seed.; Quality and acceptability of a set-type yogurt made from camel milk.; Use of beta-cyclodextrin to decrease the level of cholesterol in milk fat.; Peptides with angiotensin I converting enzyme (ACE) inhibitory activity generated from porcine skeletal muscle proteins by the action of meat-borne Lactobacillus.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1271\/bbb.60.661; 10.1021\/jf020604h; 10.1021\/jf051263l; 10.1002\/psc.800; 10.1002\/psc.892; 10.1021\/jf072911z; 10.3168\/jds.2008-1408; 10.3168\/jds.2008-1452; 10.1016\/j.jprot.2013.06.023; 10.1080\/10408398.2012.664829", "pubmedid": "8829536 12617616 16448176 17117396 17654623 18211015 19233778 19233779 23806758 24915368", "mw": "278.35", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "3.3", "instability": "5.0", "hydrophobic": "1.0", "boman": "-3.95", "helix": "0.5", "turn_pct": "0.0", "sheet": "1.0" }, { "id": "aceip0553", "seq": "LFDKPVSPL", "length": "9", "detail": "Milk (bovine) | Cereals (Wheat) | Pork | Chicken", "source": "Milk | Cereal | Porcine | Chicken", "ic50": null, "reference": "Angiotensin I-converting enzyme inhibitory peptides generated from in vitro gastrointestinal digestion of pork meat.", "doi": "10.1021\/jf904204n", "pubmedid": "20151679", "mw": "1015.2", "pi": "5.84", "charge_ph7": "-0.24", "gravy": "0.3556", "instability": "75.01", "hydrophobic": "0.6667", "boman": "-1.4178", "helix": "0.3333", "turn_pct": "0.4444", "sheet": "0.4444" }, { "id": "aceip0554", "seq": "LG", "length": "2", "detail": "Milk (whey) | Milk (caprine) | Milk (Digested milk products) | Milk (cheese whey) | Enzymatic-hydrolysis | Cereals", "source": "Milk | Synthesized | Cereal", "ic50": "<20 mM", "reference": "Binding of peptide substrates and inhibitors of angiotensin-converting enzyme. Importance of the COOH-terminal dipeptide sequence.; Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Quantitative structure-activity relationship study of bitter di- and tri-peptides including relationship with angiotensin I-converting enzyme inhibitory activity.; Three-dimensional holograph vector of atomic interaction field (3D-HoVAIF): a novel rotation-translation invariant 3D structure descriptor and its applications to peptides.; QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.; Peptides with angiotensin I converting enzyme (ACE) inhibitory activity generated from porcine skeletal muscle proteins by the action of meat-borne Lactobacillus.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1021\/jf051263l; 10.1002\/psc.800; 10.1002\/psc.892; 10.1007\/s00894-010-0862-x; 10.1016\/j.jprot.2013.06.023; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "6243277 16448176 17117396 17654623 20941517 23806758 23871047", "mw": "188.22", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "1.7", "instability": "5.0", "hydrophobic": "0.5", "boman": "-2.93", "helix": "0.5", "turn_pct": "0.5", "sheet": "0.5" }, { "id": "aceip0555", "seq": "LGFPTTKTYFPHF", "length": "13", "detail": "ND", "source": "ND", "ic50": "4.92 μM", "reference": "Novel angiotensin I-converting enzyme inhibitory peptides derived from an edible mushroom, Pleurotus cystidiosus O.K. Miller identified by LC-MS\/MS.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1186\/1472-6882-13-313; 10.1080\/10408398.2012.664829", "pubmedid": "24215325 24915368", "mw": "1555.77", "pi": "8.6", "charge_ph7": "0.85", "gravy": "-0.1462", "instability": "30.88", "hydrophobic": "0.4615", "boman": "-0.87", "helix": "0.1538", "turn_pct": "0.2308", "sheet": "0.6154" }, { "id": "aceip0556", "seq": "LGG", "length": "3", "detail": "Milk (caprine kefir)", "source": "Milk", "ic50": null, "reference": "Quantitative structure-activity relationship study of bitter di- and tri-peptides including relationship with angiotensin I-converting enzyme inhibitory activity.; QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1002\/psc.800; 10.1007\/s00894-010-0862-x; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "17117396 20941517 23871047", "mw": "245.28", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "1.0", "instability": "47.8", "hydrophobic": "0.3333", "boman": "-2.2667", "helix": "0.3333", "turn_pct": "0.6667", "sheet": "0.3333" }, { "id": "aceip0557", "seq": "LGI", "length": "3", "detail": "Egg (Ovalbumin)", "source": "Egg", "ic50": "<20 mM", "reference": "Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1021\/jf051263l; 10.1080\/10408398.2012.664829", "pubmedid": "16448176 24915368", "mw": "301.38", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "2.6333", "instability": "-21.63", "hydrophobic": "0.6667", "boman": "-3.5933", "helix": "0.3333", "turn_pct": "0.3333", "sheet": "0.6667" }, { "id": "aceip0558", "seq": "LGL", "length": "3", "detail": "Milk", "source": "Milk", "ic50": null, "reference": "Quantitative structure-activity relationship study of bitter di- and tri-peptides including relationship with angiotensin I-converting enzyme inhibitory activity.; QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1002\/psc.800; 10.1007\/s00894-010-0862-x; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "17117396 20941517 23871047", "mw": "301.38", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "2.4", "instability": "6.67", "hydrophobic": "0.6667", "boman": "-3.5933", "helix": "0.6667", "turn_pct": "0.3333", "sheet": "0.6667" }, { "id": "aceip0559", "seq": "LGP", "length": "3", "detail": "Casein", "source": "Milk", "ic50": "0.72 μM", "reference": "Structure and activity of angiotensin I converting enzyme inhibitory peptides derived from Alaskan pollack skin.; Assessing the dependence of (51)V A(z) value on the aromatic ring orientation of V(IV)O(2+) pyridine complexes.", "doi": "10.5483\/bmbrep.2002.35.2.239; 10.1021\/ic9001779", "pubmedid": "12297036 19449891", "mw": "285.34", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "0.6", "instability": "6.67", "hydrophobic": "0.6667", "boman": "-1.9533", "helix": "0.3333", "turn_pct": "0.6667", "sheet": "0.3333" }, { "id": "aceip0560", "seq": "LGPLGHQ", "length": "7", "detail": "Milk (bovine)", "source": "Milk", "ic50": "4.22 μM", "reference": "Active peptides from skate (Okamejei kenojei) skin gelatin diminish angiotensin-I converting enzyme activity and intracellular free radical-mediated oxidation.", "doi": "10.1016\/j.foodchem.2013.07.067", "pubmedid": "24054237", "mw": "720.82", "pi": "6.74", "charge_ph7": "-0.15", "gravy": "-0.2143", "instability": "8.57", "hydrophobic": "0.4286", "boman": "-1.3386", "helix": "0.2857", "turn_pct": "0.4286", "sheet": "0.2857" }, { "id": "aceip0561", "seq": "LGPVRGPFPI", "length": "10", "detail": "Milk (bovine) | Casein | Milk (Casein) | Milk (Fermented Milk) | Cheese (Swiss) | Milk (Skimmed milk) | Milk (sour milk) | Cereals (Wheat) | Cereals (Rye) | Lactobacillus helveticus", "source": "Milk | Cereal | Bacteria", "ic50": null, "reference": "Identification of angiotensin-I-converting enzyme inhibitory peptides derived from sodium caseinate hydrolysates produced by Lactobacillus helveticus NCC 2765.", "doi": "10.1021\/jf049510t", "pubmedid": "15537298", "mw": "1052.27", "pi": "9.75", "charge_ph7": "0.76", "gravy": "0.52", "instability": "58.29", "hydrophobic": "0.7", "boman": "-1.602", "helix": "0.1", "turn_pct": "0.5", "sheet": "0.4" }, { "id": "aceip0562", "seq": "LGQTPTK", "length": "7", "detail": "Soybean", "source": "Legume", "ic50": null, "reference": "Inhibitory profile of nonapeptide derived from porcine troponin C against angiotensin I-converting enzyme.", "doi": "10.1021\/jf0350865", "pubmedid": "14969529", "mw": "743.85", "pi": "8.75", "charge_ph7": "0.76", "gravy": "-1.0", "instability": "8.57", "hydrophobic": "0.2857", "boman": "-0.3429", "helix": "0.2857", "turn_pct": "0.2857", "sheet": "0.4286" }, { "id": "aceip0563", "seq": "LGTQY", "length": "5", "detail": "Milk (bovine)", "source": "Milk", "ic50": null, "reference": "Enterococcus faecalis strains from food, environmental, and clinical origin produce ACE-inhibitory peptides and other bioactive peptides during growth in bovine skim milk.", "doi": "10.1016\/j.ijfoodmicro.2013.06.019", "pubmedid": "23845432", "mw": "580.63", "pi": "5.52", "charge_ph7": "-0.24", "gravy": "-0.42", "instability": "-39.14", "hydrophobic": "0.2", "boman": "-0.82", "helix": "0.2", "turn_pct": "0.2", "sheet": "0.6" }, { "id": "aceip0564", "seq": "LGTQYTDAPSFSDIPNPIGSENSEK", "length": "25", "detail": "Milk (Fermented Milk)", "source": "Milk", "ic50": null, "reference": "Angiotensin I-converting-enzyme-inhibitory and antibacterial peptides from Lactobacillus helveticus PR4 proteinase-hydrolyzed caseins of milk from six species.", "doi": "10.1128\/AEM.69.9.5297-5305.2003", "pubmedid": "12957917", "mw": "2667.79", "pi": "4.05", "charge_ph7": "-3.23", "gravy": "-0.9", "instability": "25.29", "hydrophobic": "0.32", "boman": "-0.1836", "helix": "0.2", "turn_pct": "0.52", "sheet": "0.28" }, { "id": "aceip0565", "seq": "LHGPYP", "length": "6", "detail": "Synthesized", "source": "Synthesized", "ic50": "75.4 μM", "reference": "Rational design of angiotensin-I-converting enzyme inhibitory peptides by integrating in silico modeling and an in vitro assay.", "doi": "10.1002\/cmdc.201300132", "pubmedid": "23740817", "mw": "682.77", "pi": "6.74", "charge_ph7": "-0.15", "gravy": "-0.7167", "instability": "11.62", "hydrophobic": "0.5", "boman": "-0.7883", "helix": "0.1667", "turn_pct": "0.5", "sheet": "0.3333" }, { "id": "aceip0566", "seq": "LHLP", "length": "4", "detail": "Milk (Casein)", "source": "Milk", "ic50": "210 μM", "reference": "Inhibition of angiotensin-converting enzyme by synthetic peptide fragments of various beta-caseins.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1016\/j.foodchem.2013.05.140", "pubmedid": "1368548 23871047", "mw": "478.58", "pi": "6.74", "charge_ph7": "-0.15", "gravy": "0.7", "instability": "55.65", "hydrophobic": "0.75", "boman": "-2.2125", "helix": "0.5", "turn_pct": "0.25", "sheet": "0.5" }, { "id": "aceip0567", "seq": "LHLPAP", "length": "6", "detail": "Milk (human)", "source": "Milk", "ic50": "4.2 μM", "reference": "Stability to gastrointestinal enzymes and structure-activity relationship of beta-casein-peptides with antihypertensive properties.; Rational design of angiotensin-I-converting enzyme inhibitory peptides by integrating in silico modeling and an in vitro assay.", "doi": "10.1016\/j.peptides.2009.06.031; 10.1002\/cmdc.201300132", "pubmedid": "19591889 23740817", "mw": "646.78", "pi": "6.74", "charge_ph7": "-0.15", "gravy": "0.5", "instability": "104.63", "hydrophobic": "0.8333", "boman": "-1.7767", "helix": "0.5", "turn_pct": "0.3333", "sheet": "0.3333" }, { "id": "aceip0568", "seq": "LHLPGP", "length": "6", "detail": "Milk", "source": "Milk", "ic50": "1.9 μM", "reference": "Stability to gastrointestinal enzymes and structure-activity relationship of beta-casein-peptides with antihypertensive properties.", "doi": "10.1016\/j.peptides.2009.06.031", "pubmedid": "19591889", "mw": "632.75", "pi": "6.74", "charge_ph7": "-0.15", "gravy": "0.1333", "instability": "40.43", "hydrophobic": "0.6667", "boman": "-1.6317", "helix": "0.3333", "turn_pct": "0.5", "sheet": "0.3333" }, { "id": "aceip0569", "seq": "LHLPLL", "length": "6", "detail": "Milk | Cereals", "source": "Milk | Cereal", "ic50": "3.5 μM", "reference": "Stability to gastrointestinal enzymes and structure-activity relationship of beta-casein-peptides with antihypertensive properties.", "doi": "10.1016\/j.peptides.2009.06.031", "pubmedid": "19591889", "mw": "704.9", "pi": "6.74", "charge_ph7": "-0.15", "gravy": "1.7333", "instability": "40.43", "hydrophobic": "0.8333", "boman": "-3.115", "helix": "0.6667", "turn_pct": "0.1667", "sheet": "0.6667" }, { "id": "aceip0570", "seq": "LHLPLP", "length": "6", "detail": "ND", "source": "ND", "ic50": "2.9 μM", "reference": "Inhibition of angiotensin-converting enzyme by synthetic peptide fragments of various beta-caseins.; Stability to gastrointestinal enzymes and structure-activity relationship of beta-casein-peptides with antihypertensive properties.; Antihypertensive peptides: production, bioavailability and incorporation into foods.; The potential role of milk-derived peptides in cardiovascular disease.; Enterococcus faecalis strains from food, environmental, and clinical origin produce ACE-inhibitory peptides and other bioactive peptides during growth in bovine skim milk.", "doi": "10.1016\/j.peptides.2009.06.031; 10.1016\/j.cis.2010.11.001; 10.1039\/c1fo10017c; 10.1016\/j.ijfoodmicro.2013.06.019", "pubmedid": "1368548 19591889 21185549 21779574 23845432", "mw": "688.86", "pi": "6.74", "charge_ph7": "-0.15", "gravy": "0.8333", "instability": "72.53", "hydrophobic": "0.8333", "boman": "-2.295", "helix": "0.5", "turn_pct": "0.3333", "sheet": "0.5" }, { "id": "aceip0571", "seq": "LHLPLPL", "length": "7", "detail": "Milk", "source": "Milk", "ic50": "425 μM", "reference": "Antihypertensive effect of peptides obtained from Enterococcus faecalis-fermented milk in rats.; Antihypertensive peptides: production, bioavailability and incorporation into foods.; Antihypertensive peptides from food proteins: a review.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.; Enterococcus faecalis strains from food, environmental, and clinical origin produce ACE-inhibitory peptides and other bioactive peptides during growth in bovine skim milk.", "doi": "10.3168\/jds.S0022-0302(06)72372-4; 10.1016\/j.cis.2010.11.001; 10.1039\/c2fo10192k; 10.1016\/j.foodchem.2012.09.092; 10.1016\/j.ijfoodmicro.2013.06.019", "pubmedid": "16899668 21185549 22249830 23194537 23845432", "mw": "802.02", "pi": "6.74", "charge_ph7": "-0.15", "gravy": "1.2571", "instability": "63.6", "hydrophobic": "0.8571", "boman": "-2.67", "helix": "0.5714", "turn_pct": "0.2857", "sheet": "0.5714" }, { "id": "aceip0572", "seq": "LHLPLPLL", "length": "8", "detail": "Milk", "source": "Milk", "ic50": null, "reference": "Identification of angiotensin-I-converting enzyme inhibitory peptides derived from sodium caseinate hydrolysates produced by Lactobacillus helveticus NCC 2765.; Enterococcus faecalis strains from food, environmental, and clinical origin produce ACE-inhibitory peptides and other bioactive peptides during growth in bovine skim milk.", "doi": "10.1021\/jf049510t; 10.1016\/j.ijfoodmicro.2013.06.019", "pubmedid": "15537298 23845432", "mw": "915.17", "pi": "6.74", "charge_ph7": "-0.15", "gravy": "1.575", "instability": "56.9", "hydrophobic": "0.875", "boman": "-2.9512", "helix": "0.625", "turn_pct": "0.25", "sheet": "0.625" }, { "id": "aceip0573", "seq": "LHLPLR", "length": "6", "detail": "Milk (bovine)", "source": "Milk", "ic50": "1.8 μM", "reference": "Stability to gastrointestinal enzymes and structure-activity relationship of beta-casein-peptides with antihypertensive properties.", "doi": "10.1016\/j.peptides.2009.06.031", "pubmedid": "19591889", "mw": "747.93", "pi": "9.76", "charge_ph7": "0.85", "gravy": "0.35", "instability": "72.53", "hydrophobic": "0.6667", "boman": "-1.8417", "helix": "0.5", "turn_pct": "0.1667", "sheet": "0.5" }, { "id": "aceip0574", "seq": "LHLPYP", "length": "6", "detail": "Milk | Porphyra yezoensis | Cereals (Wheat) | Algae (Spirulina platensis)", "source": "Milk | Plants | Cereal | Bacteria", "ic50": "2.3 μM", "reference": "Stability to gastrointestinal enzymes and structure-activity relationship of beta-casein-peptides with antihypertensive properties.", "doi": "10.1016\/j.peptides.2009.06.031", "pubmedid": "19591889", "mw": "738.87", "pi": "6.74", "charge_ph7": "-0.15", "gravy": "-0.0167", "instability": "61.0", "hydrophobic": "0.6667", "boman": "-1.4517", "helix": "0.3333", "turn_pct": "0.3333", "sheet": "0.5" }, { "id": "aceip0575", "seq": "LHLWLP", "length": "6", "detail": "Milk | Egg (Ovalbumin)", "source": "Milk | Egg", "ic50": "9 μM", "reference": "Stability to gastrointestinal enzymes and structure-activity relationship of beta-casein-peptides with antihypertensive properties.", "doi": "10.1016\/j.peptides.2009.06.031", "pubmedid": "19591889", "mw": "777.95", "pi": "6.74", "charge_ph7": "-0.15", "gravy": "0.95", "instability": "100.47", "hydrophobic": "0.8333", "boman": "-2.6833", "helix": "0.5", "turn_pct": "0.1667", "sheet": "0.6667" }, { "id": "aceip0576", "seq": "LHLYLP", "length": "6", "detail": "Egg (Ovalbumin)", "source": "Egg", "ic50": "18.9 μM", "reference": "Stability to gastrointestinal enzymes and structure-activity relationship of beta-casein-peptides with antihypertensive properties.", "doi": "10.1016\/j.peptides.2009.06.031", "pubmedid": "19591889", "mw": "754.92", "pi": "6.74", "charge_ph7": "-0.15", "gravy": "0.8833", "instability": "40.43", "hydrophobic": "0.6667", "boman": "-2.2717", "helix": "0.5", "turn_pct": "0.1667", "sheet": "0.6667" }, { "id": "aceip0577", "seq": "LHP", "length": "3", "detail": "Milk | Cereals | Egg (Ovalbumin) | Meat", "source": "Milk | Cereal | Egg | Meat", "ic50": "0.77 mg\/ml", "reference": "Antihypertensive peptides from food proteins: a review.; Vegetable foods: a cheap source of proteins and peptides with antihypertensive, antioxidant, and other less occurrence bioactivities.", "doi": "10.1039\/c2fo10192k; 10.1016\/j.talanta.2012.12.041", "pubmedid": "22249830 23598136", "mw": "365.43", "pi": "6.74", "charge_ph7": "-0.15", "gravy": "-0.3333", "instability": "-2.93", "hydrophobic": "0.6667", "boman": "-1.31", "helix": "0.3333", "turn_pct": "0.3333", "sheet": "0.3333" }, { "id": "aceip0578", "seq": "LHSMKEG", "length": "7", "detail": "Egg (Ovalbumin)", "source": "Egg", "ic50": null, "reference": "Enterococcus faecalis strains from food, environmental, and clinical origin produce ACE-inhibitory peptides and other bioactive peptides during growth in bovine skim milk.", "doi": "10.1016\/j.ijfoodmicro.2013.06.019", "pubmedid": "23845432", "mw": "800.92", "pi": "6.75", "charge_ph7": "-0.15", "gravy": "-0.8714", "instability": "8.57", "hydrophobic": "0.2857", "boman": "-0.4514", "helix": "0.5714", "turn_pct": "0.2857", "sheet": "0.1429" }, { "id": "aceip0579", "seq": "LI", "length": "2", "detail": "Milk (bovine) | Amaranth | Soybean | pea | Pork | Chicken", "source": "Milk | Plants | Legume | Porcine | Chicken", "ic50": null, "reference": "Quantitative structure-activity relationship study of bitter di- and tri-peptides including relationship with angiotensin I-converting enzyme inhibitory activity.", "doi": "10.1002\/psc.800", "pubmedid": "17117396", "mw": "244.33", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "4.15", "instability": "5.0", "hydrophobic": "1.0", "boman": "-4.92", "helix": "0.5", "turn_pct": "0.0", "sheet": "1.0" }, { "id": "aceip0580", "seq": "LIPPGVPY", "length": "8", "detail": "Milk (bovine) | Milk | Amaranth | Cereals (Maize) | Maize", "source": "Milk | Plants | Cereal", "ic50": "17.38 μM", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.; Vegetable foods: a cheap source of proteins and peptides with antihypertensive, antioxidant, and other less occurrence bioactivities.", "doi": "10.1016\/j.foodchem.2012.09.092; 10.1016\/j.talanta.2012.12.041", "pubmedid": "23194537 23598136", "mw": "855.03", "pi": "5.52", "charge_ph7": "-0.24", "gravy": "0.75", "instability": "53.3", "hydrophobic": "0.75", "boman": "-1.835", "helix": "0.125", "turn_pct": "0.5", "sheet": "0.5" }, { "id": "aceip0581", "seq": "LIQP", "length": "4", "detail": "Cereals (Maize) | alpha-zein", "source": "Cereal", "ic50": null, "reference": "Isolation from alpha-zein of thermolysin peptides with angiotensin I-converting enzyme inhibitory activity.", "doi": "10.1271\/bbb.60.661", "pubmedid": "8829536", "mw": "469.57", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "0.8", "instability": "55.65", "hydrophobic": "0.75", "boman": "-2.12", "helix": "0.25", "turn_pct": "0.25", "sheet": "0.5" }, { "id": "aceip0582", "seq": "LIY", "length": "3", "detail": "Milk", "source": "Milk", "ic50": "<20 mM", "reference": "Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Inhibition strength of short peptides derived from an ACE inhibitory peptide.; Rational design of angiotensin-I-converting enzyme inhibitory peptides by integrating in silico modeling and an in vitro assay.", "doi": "10.1021\/jf051263l; 10.1021\/jf202902r; 10.1002\/cmdc.201300132", "pubmedid": "16448176 21923188 23740817", "mw": "407.5", "pi": "5.52", "charge_ph7": "-0.24", "gravy": "2.3333", "instability": "6.67", "hydrophobic": "0.6667", "boman": "-3.2333", "helix": "0.3333", "turn_pct": "0.0", "sheet": "1.0" }, { "id": "aceip0583", "seq": "LIYP", "length": "4", "detail": "Soybean", "source": "Legume", "ic50": "10 μM", "reference": "Inhibition of angiotensin-converting enzyme by synthetic peptide fragments of various beta-caseins.; The potential role of milk-derived peptides in cardiovascular disease.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1039\/c1fo10017c; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "1368548 21779574 23871047", "mw": "504.62", "pi": "5.52", "charge_ph7": "-0.24", "gravy": "1.35", "instability": "38.35", "hydrophobic": "0.75", "boman": "-2.425", "helix": "0.25", "turn_pct": "0.25", "sheet": "0.75" }, { "id": "aceip0584", "seq": "LKA", "length": "3", "detail": "Milk | Meat", "source": "Milk | Meat", "ic50": "0.32-14 μM", "reference": "Temporal gene expression and probiotic attributes of Lactobacillus acidophilus during growth in milk.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.3168\/jds.2008-1457; 10.1080\/10408398.2012.664829", "pubmedid": "19233780 24915368", "mw": "330.42", "pi": "8.75", "charge_ph7": "0.76", "gravy": "0.5667", "instability": "-21.63", "hydrophobic": "0.6667", "boman": "-1.7167", "helix": "1.0", "turn_pct": "0.0", "sheet": "0.3333" }, { "id": "aceip0585", "seq": "LKKYKVPQ", "length": "8", "detail": "Milk | Bonito | Chicken | Egg (Ovalbumin)", "source": "Milk | Fish | Chicken | Egg", "ic50": null, "reference": "Enterococcus faecalis strains from food, environmental, and clinical origin produce ACE-inhibitory peptides and other bioactive peptides during growth in bovine skim milk.", "doi": "10.1016\/j.ijfoodmicro.2013.06.019", "pubmedid": "23845432", "mw": "1003.24", "pi": "10.0", "charge_ph7": "2.76", "gravy": "-1.2625", "instability": "35.68", "hydrophobic": "0.375", "boman": "-0.34", "helix": "0.5", "turn_pct": "0.125", "sheet": "0.375" }, { "id": "aceip0586", "seq": "LKL", "length": "3", "detail": "Bonito", "source": "Fish", "ic50": "<20 mM", "reference": "Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.", "doi": "10.1021\/jf051263l", "pubmedid": "16448176", "mw": "372.5", "pi": "8.75", "charge_ph7": "0.76", "gravy": "1.2333", "instability": "-49.93", "hydrophobic": "0.6667", "boman": "-2.7533", "helix": "1.0", "turn_pct": "0.0", "sheet": "0.6667" }, { "id": "aceip0587", "seq": "LKP", "length": "3", "detail": "Milk", "source": "Milk", "ic50": "<10 μM", "reference": "ACE inhibitory peptides derived from enzymatic hydrolysates of animal muscle protein: a review.; Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Angiotensin converting enzyme inhibitory peptides derived from food proteins: biochemistry, bioactivity and production.; Temporal gene expression and probiotic attributes of Lactobacillus acidophilus during growth in milk.; Model of the exofacial substrate-binding site and helical folding of the human Glut1 glucose transporter based on scanning mutagenesis.; Inhibition strength of short peptides derived from an ACE inhibitory peptide.; Antihypertensive peptides from food proteins: a review.; Review on the angiotensin-I-converting enzyme (ACE) inhibitor peptides from marine proteins.; Vegetable foods: a cheap source of proteins and peptides with antihypertensive, antioxidant, and other less occurrence bioactivities.; Glycinyl-histidinyl-serine (GHS), a novel rapeseed protein-derived peptide has blood pressure-lowering effect in spontaneously hypertensive rats.; Comparison of analytical methods to assay inhibitors of angiotensin I-converting enzyme.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1021\/jf0508908; 10.1021\/jf051263l; 10.2174\/138161207780363068; 10.3168\/jds.2008-1457; 10.1021\/bi900521n; 10.1021\/jf202902r; 10.1039\/c2fo10192k; 10.1007\/s12010-012-0024-y; 10.1016\/j.talanta.2012.12.041; 10.1021\/jf400865m; 10.1016\/j.foodchem.2013.06.048; 10.1080\/10408398.2012.664829", "pubmedid": "16218651 16448176 17430180 19233780 19449892 21923188 22249830 23271625 23598136 23919612 23993489 24915368", "mw": "356.46", "pi": "8.75", "charge_ph7": "0.76", "gravy": "-0.5667", "instability": "-46.77", "hydrophobic": "0.6667", "boman": "-1.1133", "helix": "0.6667", "turn_pct": "0.3333", "sheet": "0.3333" }, { "id": "aceip0588", "seq": "LKPDM", "length": "5", "detail": "Milk | Egg (Ovotransferrin)", "source": "Milk | Egg", "ic50": "9.69 μM", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "23194537", "mw": "602.74", "pi": "5.84", "charge_ph7": "-0.24", "gravy": "-0.66", "instability": "-39.14", "hydrophobic": "0.6", "boman": "-0.802", "helix": "0.6", "turn_pct": "0.4", "sheet": "0.2" }, { "id": "aceip0589", "seq": "LKPMN", "length": "5", "detail": "Egg (Ovalbumin)", "source": "Egg", "ic50": "2.4 μM", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "23194537", "mw": "601.76", "pi": "8.75", "charge_ph7": "0.76", "gravy": "-0.66", "instability": "-39.14", "hydrophobic": "0.6", "boman": "-0.814", "helix": "0.6", "turn_pct": "0.4", "sheet": "0.2" }, { "id": "aceip0590", "seq": "LKPNM", "length": "5", "detail": "Egg (Ovalbumin)", "source": "Egg", "ic50": "2.4 μM", "reference": "Peptide inhibitors for angiotensin I-converting enzyme from thermolysin digest of dried bonito.; LKPNM: a prodrug-type ACE-inhibitory peptide derived from fish protein.; Antihypertensive peptides from food proteins: a review.; Review on the angiotensin-I-converting enzyme (ACE) inhibitor peptides from marine proteins.; Comparison of analytical methods to assay inhibitors of angiotensin I-converting enzyme.; Novel angiotensin I-converting enzyme inhibitory peptides derived from an edible mushroom, Pleurotus cystidiosus O.K. Miller identified by LC-MS\/MS.", "doi": "10.1271\/bbb.56.1541; 10.1016\/s0162-3109(99)00118-6; 10.1039\/c2fo10192k; 10.1007\/s12010-012-0024-y; 10.1016\/j.foodchem.2013.06.048; 10.1186\/1472-6882-13-313", "pubmedid": "1369054 10604535 22249830 23271625 23993489 24215325", "mw": "601.76", "pi": "8.75", "charge_ph7": "0.76", "gravy": "-0.66", "instability": "-24.06", "hydrophobic": "0.6", "boman": "-0.814", "helix": "0.6", "turn_pct": "0.4", "sheet": "0.2" }, { "id": "aceip0591", "seq": "LKPTPEGN", "length": "8", "detail": "Egg (Ovalbumin)", "source": "Egg", "ic50": "2691.53 μM", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "23194537", "mw": "854.95", "pi": "6.0", "charge_ph7": "-0.24", "gravy": "-1.425", "instability": "-0.18", "hydrophobic": "0.375", "boman": "-0.095", "helix": "0.375", "turn_pct": "0.5", "sheet": "0.25" }, { "id": "aceip0592", "seq": "LKVGVKQY", "length": "8", "detail": "Spinach", "source": "Plants", "ic50": "11 μM", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "23194537", "mw": "934.13", "pi": "9.7", "charge_ph7": "1.76", "gravy": "-0.1", "instability": "-6.56", "hydrophobic": "0.375", "boman": "-1.16", "helix": "0.375", "turn_pct": "0.125", "sheet": "0.5" }, { "id": "aceip0593", "seq": "LKY", "length": "3", "detail": "ND", "source": "ND", "ic50": "0.33-5.80 mg\/ml", "reference": "Isolation and identification of antihypertensive peptides from antarctic krill tail meat hydrolysate.; Vegetable foods: a cheap source of proteins and peptides with antihypertensive, antioxidant, and other less occurrence bioactivities.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1111\/j.1750-3841.2009.01138.x; 10.1016\/j.talanta.2012.12.041; 10.1016\/j.foodchem.2013.05.140; 10.1080\/10408398.2012.664829", "pubmedid": "19490329 23598136 23871047 24915368", "mw": "422.52", "pi": "8.59", "charge_ph7": "0.76", "gravy": "-0.4667", "instability": "-21.63", "hydrophobic": "0.3333", "boman": "-1.0667", "helix": "0.6667", "turn_pct": "0.0", "sheet": "0.6667" }, { "id": "aceip0594", "seq": "LL", "length": "2", "detail": "Soybean", "source": "Legume", "ic50": null, "reference": "Quantitative structure-activity relationship study of bitter di- and tri-peptides including relationship with angiotensin I-converting enzyme inhibitory activity.; Three-dimensional holograph vector of atomic interaction field (3D-HoVAIF): a novel rotation-translation invariant 3D structure descriptor and its applications to peptides.", "doi": "10.1002\/psc.800; 10.1002\/psc.892", "pubmedid": "17117396 17654623", "mw": "244.33", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "3.8", "instability": "5.0", "hydrophobic": "1.0", "boman": "-4.92", "helix": "1.0", "turn_pct": "0.0", "sheet": "1.0" }, { "id": "aceip0595", "seq": "LLF", "length": "3", "detail": "Milk", "source": "Milk", "ic50": "<20 mM", "reference": "Camel (camelus dromedarius) milk PP3: evidence for an insertion in the amino-terminal sequence of the camel milk whey protein.; Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Angiotensin converting enzyme inhibitory peptides derived from food proteins: biochemistry, bioactivity and production.; Effect of simulated gastrointestinal digestion on the antihypertensive properties of synthetic beta-lactoglobulin peptide sequences.; Antihypertensive peptides: production, bioavailability and incorporation into foods.; Antihypertensive peptides from food proteins: a review.; LC-MS\/MS coupled with QSAR modeling in characterising of angiotensin I-converting enzyme inhibitory peptides from soybean proteins.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1139\/o99-067; 10.1021\/jf051263l; 10.2174\/138161207780363068; 10.1017\/S0022029907002609; 10.1016\/j.cis.2010.11.001; 10.1039\/c2fo10192k; 10.1016\/j.foodchem.2013.04.064; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "10735560 16448176 17430180 17466121 21185549 22249830 23871011 23871047", "mw": "391.5", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "3.4667", "instability": "6.67", "hydrophobic": "1.0", "boman": "-4.2733", "helix": "0.6667", "turn_pct": "0.0", "sheet": "1.0" }, { "id": "aceip0596", "seq": "LLG", "length": "3", "detail": "Cereals (Buckwheat)", "source": "Cereal", "ic50": null, "reference": "Quantitative structure-activity relationship study of bitter di- and tri-peptides including relationship with angiotensin I-converting enzyme inhibitory activity.; QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1002\/psc.800; 10.1007\/s00894-010-0862-x; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "17117396 20941517 23871047", "mw": "301.38", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "2.4", "instability": "6.67", "hydrophobic": "0.6667", "boman": "-3.5933", "helix": "0.6667", "turn_pct": "0.3333", "sheet": "0.6667" }, { "id": "aceip0597", "seq": "LLL", "length": "3", "detail": "Milk | Sweet-potato", "source": "Milk | Potato", "ic50": null, "reference": "Quantitative structure-activity relationship study of bitter di- and tri-peptides including relationship with angiotensin I-converting enzyme inhibitory activity.; QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1002\/psc.800; 10.1007\/s00894-010-0862-x; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "17117396 20941517 23871047", "mw": "357.49", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "3.8", "instability": "6.67", "hydrophobic": "1.0", "boman": "-4.92", "helix": "1.0", "turn_pct": "0.0", "sheet": "1.0" }, { "id": "aceip0598", "seq": "LLLAHLL", "length": "7", "detail": "Milk (bovine)", "source": "Milk", "ic50": "5.19 μM", "reference": "Identification of angiotensin I-converting enzyme inhibitory peptides from koumiss, a traditional fermented mare's milk.", "doi": "10.3168\/jds.2009-2672", "pubmedid": "20172208", "mw": "792.02", "pi": "6.74", "charge_ph7": "-0.15", "gravy": "2.5143", "instability": "-3.56", "hydrophobic": "0.8571", "boman": "-3.6314", "helix": "0.8571", "turn_pct": "0.0", "sheet": "0.7143" }, { "id": "aceip0599", "seq": "LLNP", "length": "4", "detail": "Antarctic krill", "source": "Shrimp", "ic50": ">1000 μM", "reference": "Inhibition of angiotensin-converting enzyme by synthetic peptide fragments of various beta-caseins.", "doi": "", "pubmedid": "1368548", "mw": "455.55", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "0.625", "instability": "0.3", "hydrophobic": "0.75", "boman": "-2.055", "helix": "0.5", "turn_pct": "0.5", "sheet": "0.5" }, { "id": "aceip0600", "seq": "LLNPPHQIYP", "length": "10", "detail": "Pork", "source": "Porcine", "ic50": "0 μM", "reference": "Inhibition of angiotensin-converting enzyme by synthetic peptide fragments of various beta-caseins.", "doi": "", "pubmedid": "1368548", "mw": "1191.38", "pi": "6.74", "charge_ph7": "-0.15", "gravy": "-0.42", "instability": "37.72", "hydrophobic": "0.6", "boman": "-1.065", "helix": "0.2", "turn_pct": "0.4", "sheet": "0.4" }, { "id": "aceip0601", "seq": "LLP", "length": "3", "detail": "Pork", "source": "Porcine", "ic50": "<20 mM", "reference": "Structures and activity of angiotensin-converting enzyme inhibitors in an alpha-zein hydrolysate.; Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Bioactive peptides in amaranth (Amaranthus hypochondriacus) seed.; Cellular membrane disruption by amyloid fibrils involved intermolecular disulfide cross-linking.; LC-MS\/MS quantification of bioactive angiotensin I-converting enzyme inhibitory peptides in rye malt sourdoughs.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1021\/jf051263l; 10.1021\/jf072911z; 10.1021\/bi900219c; 10.1021\/jf2033329; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "1368684 16448176 18211015 19449893 21985248 23871047", "mw": "341.45", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "2.0", "instability": "70.87", "hydrophobic": "1.0", "boman": "-3.28", "helix": "0.6667", "turn_pct": "0.3333", "sheet": "0.6667" }, { "id": "aceip0602", "seq": "LLQSW", "length": "5", "detail": "Pork", "source": "Porcine", "ic50": null, "reference": "Enterococcus faecalis strains from food, environmental, and clinical origin produce ACE-inhibitory peptides and other bioactive peptides during growth in bovine skim milk.", "doi": "10.1016\/j.ijfoodmicro.2013.06.019", "pubmedid": "23845432", "mw": "645.75", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "0.48", "instability": "161.08", "hydrophobic": "0.6", "boman": "-1.994", "helix": "0.4", "turn_pct": "0.2", "sheet": "0.6" }, { "id": "aceip0603", "seq": "LLRF", "length": "4", "detail": "ND", "source": "ND", "ic50": null, "reference": "Enterococcus faecalis strains from food, environmental, and clinical origin produce ACE-inhibitory peptides and other bioactive peptides during growth in bovine skim milk.", "doi": "10.1016\/j.ijfoodmicro.2013.06.019", "pubmedid": "23845432", "mw": "547.69", "pi": "9.75", "charge_ph7": "0.76", "gravy": "1.475", "instability": "55.65", "hydrophobic": "0.75", "boman": "-2.525", "helix": "0.5", "turn_pct": "0.0", "sheet": "0.75" }, { "id": "aceip0604", "seq": "LLYQEP", "length": "6", "detail": "Egg (Ovalbumin)", "source": "Egg", "ic50": null, "reference": "Enterococcus faecalis strains from food, environmental, and clinical origin produce ACE-inhibitory peptides and other bioactive peptides during growth in bovine skim milk.", "doi": "10.1016\/j.ijfoodmicro.2013.06.019", "pubmedid": "23845432", "mw": "761.86", "pi": "4.05", "charge_ph7": "-1.24", "gravy": "-0.3833", "instability": "72.53", "hydrophobic": "0.5", "boman": "-1.1167", "helix": "0.5", "turn_pct": "0.1667", "sheet": "0.5" }, { "id": "aceip0605", "seq": "LLYQEPVLGPVRGPFPIIV", "length": "19", "detail": "chicken", "source": "Chicken", "ic50": "21 mM\/L", "reference": "Antihypertensive effect of the peptides derived from casein by an extracellular proteinase from Lactobacillus helveticus CP790.", "doi": "10.3168\/jds.S0022-0302(94)77026-0", "pubmedid": "8201050", "mw": "2107.54", "pi": "6.0", "charge_ph7": "-0.24", "gravy": "0.8316", "instability": "61.36", "hydrophobic": "0.6842", "boman": "-1.88", "helix": "0.2105", "turn_pct": "0.3158", "sheet": "0.5263" }, { "id": "aceip0606", "seq": "LLYQQPV", "length": "7", "detail": "Bonito", "source": "Fish", "ic50": "1001 μM", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "23194537", "mw": "860.01", "pi": "5.52", "charge_ph7": "-0.24", "gravy": "0.2714", "instability": "91.11", "hydrophobic": "0.5714", "boman": "-1.5743", "helix": "0.2857", "turn_pct": "0.1429", "sheet": "0.5714" }, { "id": "aceip0607", "seq": "LLYQQPVLGPVRGPFPIIV", "length": "19", "detail": "Bonito", "source": "Fish", "ic50": null, "reference": "The potential role of milk-derived peptides in cardiovascular disease.", "doi": "10.1039\/c1fo10017c", "pubmedid": "21779574", "mw": "2106.55", "pi": "8.75", "charge_ph7": "0.76", "gravy": "0.8316", "instability": "61.36", "hydrophobic": "0.6842", "boman": "-1.8947", "helix": "0.1579", "turn_pct": "0.3158", "sheet": "0.5263" }, { "id": "aceip0608", "seq": "LN", "length": "2", "detail": "Bonito | Actin | Chicken", "source": "Fish | Chicken", "ic50": "0 0", "reference": "Application of at-line two-dimensional liquid chromatography-mass spectrometry for identification of small hydrophilic angiotensin I-inhibiting peptides in milk hydrolysates.; Vegetable foods: a cheap source of proteins and peptides with antihypertensive, antioxidant, and other less occurrence bioactivities.; Peptides with angiotensin I converting enzyme (ACE) inhibitory activity generated from porcine skeletal muscle proteins by the action of meat-borne Lactobacillus.", "doi": "10.1007\/s00216-008-1990-3; 10.1016\/j.talanta.2012.12.041; 10.1016\/j.jprot.2013.06.023", "pubmedid": "18392815 23598136 23806758", "mw": "245.28", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "0.15", "instability": "5.0", "hydrophobic": "0.5", "boman": "-1.65", "helix": "0.5", "turn_pct": "0.5", "sheet": "0.5" }, { "id": "aceip0609", "seq": "LNENLLRFFVAPFPEVFG", "length": "18", "detail": "Food-protein", "source": "Synthesized", "ic50": "280 μM", "reference": "Identification of angiotensin-I-converting enzyme inhibitory peptides derived from sodium caseinate hydrolysates produced by Lactobacillus helveticus NCC 2765.", "doi": "10.1021\/jf049510t", "pubmedid": "15537298", "mw": "2109.42", "pi": "4.53", "charge_ph7": "-1.23", "gravy": "0.5944", "instability": "61.9", "hydrophobic": "0.6667", "boman": "-1.5706", "helix": "0.3333", "turn_pct": "0.2778", "sheet": "0.5" }, { "id": "aceip0610", "seq": "LNP", "length": "3", "detail": "ND", "source": "ND", "ic50": "<10 μM", "reference": "Structures and activity of angiotensin-converting enzyme inhibitors in an alpha-zein hydrolysate.; Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Bioactive peptides in amaranth (Amaranthus hypochondriacus) seed.; Cellular membrane disruption by amyloid fibrils involved intermolecular disulfide cross-linking.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1021\/jf051263l; 10.1021\/jf072911z; 10.1021\/bi900219c; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "1368684 16448176 18211015 19449893 23871047", "mw": "342.39", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "-0.4333", "instability": "-2.93", "hydrophobic": "0.6667", "boman": "-1.1", "helix": "0.3333", "turn_pct": "0.6667", "sheet": "0.3333" }, { "id": "aceip0611", "seq": "LNPA", "length": "4", "detail": "Milk (bovine)", "source": "Milk", "ic50": "312 μM", "reference": "Isolation from alpha-zein of thermolysin peptides with angiotensin I-converting enzyme inhibitory activity.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1271\/bbb.60.661; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "8829536 23871047", "mw": "413.47", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "0.125", "instability": "48.45", "hydrophobic": "0.75", "boman": "-1.2775", "helix": "0.5", "turn_pct": "0.5", "sheet": "0.25" }, { "id": "aceip0612", "seq": "LNPPHQIYP", "length": "9", "detail": "ND", "source": "ND", "ic50": "0 μM", "reference": "Inhibition of angiotensin-converting enzyme by synthetic peptide fragments of various beta-caseins.", "doi": "", "pubmedid": "1368548", "mw": "1078.22", "pi": "6.74", "charge_ph7": "-0.15", "gravy": "-0.8889", "instability": "40.8", "hydrophobic": "0.5556", "boman": "-0.6367", "helix": "0.1111", "turn_pct": "0.4444", "sheet": "0.3333" }, { "id": "aceip0613", "seq": "LNQ", "length": "3", "detail": "Algae (Chlorella vulgaris)", "source": "Bacteria", "ic50": null, "reference": "Isolation from alpha-zein of thermolysin peptides with angiotensin I-converting enzyme inhibitory activity.", "doi": "10.1271\/bbb.60.661", "pubmedid": "8829536", "mw": "373.4", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "-1.0667", "instability": "-18.47", "hydrophobic": "0.3333", "boman": "-0.6467", "helix": "0.3333", "turn_pct": "0.3333", "sheet": "0.3333" }, { "id": "aceip0614", "seq": "LNVPGEIVE", "length": "9", "detail": "Sesame | Synthesized | Royal jelly | Cereals (Wheat)", "source": "Plants | Synthesized | Insect | Cereal", "ic50": "300 μM", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "23194537", "mw": "969.09", "pi": "4.24", "charge_ph7": "-2.23", "gravy": "0.4667", "instability": "33.88", "hydrophobic": "0.5556", "boman": "-1.5511", "helix": "0.3333", "turn_pct": "0.3333", "sheet": "0.4444" }, { "id": "aceip0615", "seq": "LNVVGETVE", "length": "9", "detail": "Milk (bovine) | Wakame | Synthesized | Bonito | Sardine | Salmon | Cereals (Wheat)", "source": "Milk | Plants | Synthesized | Fish | Cereal", "ic50": ">1000 μM", "reference": "Angiotensin-converting enzyme inhibitory activity of peptides derived from caprine kefir.", "doi": "10.3168\/jds.S0022-0302(05)73032-0", "pubmedid": "16162521", "mw": "959.05", "pi": "4.24", "charge_ph7": "-2.23", "gravy": "0.5333", "instability": "-8.92", "hydrophobic": "0.4444", "boman": "-1.4244", "helix": "0.3333", "turn_pct": "0.2222", "sheet": "0.5556" }, { "id": "aceip0616", "seq": "LNY", "length": "3", "detail": "Bonito | Actin | Cereals (Finnish)", "source": "Fish | Cereal", "ic50": "<20 mM", "reference": "Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.", "doi": "10.1021\/jf051263l", "pubmedid": "16448176", "mw": "408.45", "pi": "5.52", "charge_ph7": "-0.24", "gravy": "-0.3333", "instability": "6.67", "hydrophobic": "0.3333", "boman": "-1.0533", "helix": "0.3333", "turn_pct": "0.3333", "sheet": "0.6667" }, { "id": "aceip0617", "seq": "LP", "length": "2", "detail": "Bonito | Meat", "source": "Fish | Meat", "ic50": null, "reference": "Antihypertensive peptides derived from milk proteins.", "doi": "10.1002\/(SICI)1521-3803(19990601)43:3<159::AID-FOOD159>3.0.CO;2-R", "pubmedid": "10399348", "mw": "228.29", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "1.1", "instability": "101.3", "hydrophobic": "1.0", "boman": "-2.46", "helix": "0.5", "turn_pct": "0.5", "sheet": "0.5" }, { "id": "aceip0618", "seq": "LPF", "length": "3", "detail": "Milk (bovine) | Amaranth | Wakame | Rapeseed | Bonito | Sardine | Cereals (Wheat) | Cereals (Rice) | pea | Pork | Chicken | Chicken connectin", "source": "Milk | Plants | Fish | Cereal | Legume | Porcine | Chicken", "ic50": "<20 mM", "reference": "Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1021\/jf051263l; 10.1080\/10408398.2012.664829", "pubmedid": "16448176 24915368", "mw": "375.46", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "1.6667", "instability": "135.07", "hydrophobic": "1.0", "boman": "-2.6333", "helix": "0.3333", "turn_pct": "0.3333", "sheet": "0.6667" }, { "id": "aceip0619", "seq": "LPG", "length": "3", "detail": "Meat", "source": "Meat", "ic50": "5.73 μM", "reference": "Structure and activity of angiotensin I converting enzyme inhibitory peptides derived from Alaskan pollack skin.; Peptides with angiotensin I converting enzyme (ACE) inhibitory activity generated from porcine skeletal muscle proteins by the action of meat-borne Lactobacillus.", "doi": "10.5483\/bmbrep.2002.35.2.239; 10.1016\/j.jprot.2013.06.023", "pubmedid": "12297036 23806758", "mw": "285.34", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "0.6", "instability": "70.87", "hydrophobic": "0.6667", "boman": "-1.9533", "helix": "0.3333", "turn_pct": "0.6667", "sheet": "0.3333" }, { "id": "aceip0620", "seq": "LPHF", "length": "4", "detail": "ND", "source": "ND", "ic50": "670 μM", "reference": "What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1016\/j.foodchem.2013.05.140", "pubmedid": "23871047", "mw": "512.6", "pi": "6.74", "charge_ph7": "-0.15", "gravy": "0.45", "instability": "29.73", "hydrophobic": "0.75", "boman": "-1.7275", "helix": "0.25", "turn_pct": "0.25", "sheet": "0.5" }, { "id": "aceip0621", "seq": "LPLP", "length": "4", "detail": "Soybean", "source": "Legume", "ic50": "703 μM", "reference": "Inhibition of angiotensin-converting enzyme by synthetic peptide fragments of various beta-caseins.; The potential role of milk-derived peptides in cardiovascular disease.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.; Novel probiotic-fermented milk with angiotensin I-converting enzyme inhibitory peptides produced by Bifidobacterium bifidum MF 20\/5.", "doi": "10.1039\/c1fo10017c; 10.1016\/j.foodchem.2013.05.140; 10.1016\/j.ijfoodmicro.2013.09.002", "pubmedid": "1368548 21779574 23871047 24135669", "mw": "438.56", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "1.1", "instability": "103.8", "hydrophobic": "1.0", "boman": "-2.46", "helix": "0.5", "turn_pct": "0.5", "sheet": "0.5" }, { "id": "aceip0622", "seq": "LPN", "length": "3", "detail": "Milk (human) | Cereals", "source": "Milk | Cereal", "ic50": null, "reference": "Isolation from alpha-zein of thermolysin peptides with angiotensin I-converting enzyme inhibitory activity.", "doi": "10.1271\/bbb.60.661", "pubmedid": "8829536", "mw": "342.39", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "-0.4333", "instability": "70.87", "hydrophobic": "0.6667", "boman": "-1.1", "helix": "0.3333", "turn_pct": "0.6667", "sheet": "0.3333" }, { "id": "aceip0623", "seq": "LPP", "length": "3", "detail": "Sake", "source": "Cereal", "ic50": "<20 mM", "reference": "Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Bioactive peptides in amaranth (Amaranthus hypochondriacus) seed.; Peptides with angiotensin I converting enzyme (ACE) inhibitory activity generated from porcine skeletal muscle proteins by the action of meat-borne Lactobacillus.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1021\/jf051263l; 10.1021\/jf072911z; 10.1016\/j.jprot.2013.06.023; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "16448176 18211015 23806758 23871047", "mw": "325.4", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "0.2", "instability": "135.07", "hydrophobic": "1.0", "boman": "-1.64", "helix": "0.3333", "turn_pct": "0.6667", "sheet": "0.3333" }, { "id": "aceip0624", "seq": "LPQNILP", "length": "7", "detail": "Casein | Sake", "source": "Milk | Cereal", "ic50": "46 μM", "reference": "Inhibition of angiotensin-converting enzyme by synthetic peptide fragments of various beta-caseins.", "doi": "", "pubmedid": "1368548", "mw": "793.95", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "0.2714", "instability": "181.4", "hydrophobic": "0.7143", "boman": "-1.6829", "helix": "0.2857", "turn_pct": "0.4286", "sheet": "0.4286" }, { "id": "aceip0625", "seq": "LPQNIPPL", "length": "8", "detail": "Milk (human)", "source": "Milk", "ic50": null, "reference": "Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1080\/10408398.2012.664829", "pubmedid": "24915368", "mw": "891.07", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "0.0375", "instability": "132.3", "hydrophobic": "0.75", "boman": "-1.4725", "helix": "0.25", "turn_pct": "0.5", "sheet": "0.375" }, { "id": "aceip0626", "seq": "LPQYLKTVYQHQKA", "length": "14", "detail": "Soybean", "source": "Legume", "ic50": null, "reference": "Identification of angiotensin-I-converting enzyme inhibitory peptides derived from sodium caseinate hydrolysates produced by Lactobacillus helveticus NCC 2765.", "doi": "10.1021\/jf049510t", "pubmedid": "15537298", "mw": "1716.98", "pi": "9.53", "charge_ph7": "1.84", "gravy": "-0.9143", "instability": "19.96", "hydrophobic": "0.3571", "boman": "-0.4943", "helix": "0.3571", "turn_pct": "0.0714", "sheet": "0.4286" }, { "id": "aceip0627", "seq": "LPYPY", "length": "5", "detail": "Lachesis muta", "source": "Animal", "ic50": "10.0-848.0 μM", "reference": "Identification of novel angiotensin-converting enzyme-inhibitory peptides from ovine milk proteins by CE-MS and chromatographic techniques.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1002\/elps.200700324; 10.1016\/j.foodchem.2012.09.092", "pubmedid": "17948260 23194537", "mw": "651.75", "pi": "5.52", "charge_ph7": "-0.24", "gravy": "-0.4", "instability": "71.2", "hydrophobic": "0.6", "boman": "-0.928", "helix": "0.2", "turn_pct": "0.4", "sheet": "0.6" }, { "id": "aceip0628", "seq": "LPYPYY", "length": "6", "detail": "Jararaca", "source": "Animal", "ic50": null, "reference": "Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1080\/10408398.2012.664829", "pubmedid": "24915368", "mw": "814.92", "pi": "5.52", "charge_ph7": "-0.24", "gravy": "-0.55", "instability": "81.57", "hydrophobic": "0.5", "boman": "-0.75", "helix": "0.1667", "turn_pct": "0.3333", "sheet": "0.6667" }, { "id": "aceip0629", "seq": "LQ", "length": "2", "detail": "Chinese water mocassin", "source": "Animal", "ic50": "0 0", "reference": "Application of at-line two-dimensional liquid chromatography-mass spectrometry for identification of small hydrophilic angiotensin I-inhibiting peptides in milk hydrolysates.; Peptides with angiotensin I converting enzyme (ACE) inhibitory activity generated from porcine skeletal muscle proteins by the action of meat-borne Lactobacillus.", "doi": "10.1007\/s00216-008-1990-3; 10.1016\/j.jprot.2013.06.023", "pubmedid": "18392815 23806758", "mw": "259.3", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "0.15", "instability": "168.0", "hydrophobic": "0.5", "boman": "-1.78", "helix": "0.5", "turn_pct": "0.0", "sheet": "0.5" }, { "id": "aceip0630", "seq": "LQKW", "length": "4", "detail": "Jararaca", "source": "Animal", "ic50": "3.5 μM", "reference": "Camel (camelus dromedarius) milk PP3: evidence for an insertion in the amino-terminal sequence of the camel milk whey protein.; Angiotensin converting enzyme inhibitory peptides derived from food proteins: biochemistry, bioactivity and production.; Antihypertensive peptides: production, bioavailability and incorporation into foods.; Antihypertensive peptides from food proteins: a review.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1139\/o99-067; 10.2174\/138161207780363068; 10.1016\/j.cis.2010.11.001; 10.1039\/c2fo10192k; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "10735560 17430180 21185549 22249830 23871047", "mw": "573.68", "pi": "8.75", "charge_ph7": "0.76", "gravy": "-1.125", "instability": "89.0", "hydrophobic": "0.5", "boman": "-1.0775", "helix": "0.5", "turn_pct": "0.0", "sheet": "0.5" }, { "id": "aceip0631", "seq": "LQP", "length": "3", "detail": "Snake", "source": "Animal", "ic50": "0.33-5.80 mg\/ml", "reference": "Structures and activity of angiotensin-converting enzyme inhibitors in an alpha-zein hydrolysate.; Isolation from alpha-zein of thermolysin peptides with angiotensin I-converting enzyme inhibitory activity.; Antihypertensive effect of angiotensin I-converting enzyme inhibitory peptides from a sesame protein hydrolysate in spontaneously hypertensive rats.; Bioactive peptides in amaranth (Amaranthus hypochondriacus) seed.; Cellular membrane disruption by amyloid fibrils involved intermolecular disulfide cross-linking.; Angiotensin I converting enzyme inhibitory peptides produced by autolysis reactions from wheat bran.; LC-MS\/MS quantification of bioactive angiotensin I-converting enzyme inhibitory peptides in rye malt sourdoughs.; Vegetable foods: a cheap source of proteins and peptides with antihypertensive, antioxidant, and other less occurrence bioactivities.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1271\/bbb.60.661; 10.1271\/bbb.70.1118; 10.1021\/jf072911z; 10.1021\/bi900219c; 10.1021\/jf900857w; 10.1021\/jf2033329; 10.1016\/j.talanta.2012.12.041; 10.1016\/j.foodchem.2013.05.140; 10.1080\/10408398.2012.664829", "pubmedid": "1368684 8829536 16717411 18211015 19449893 19572648 21985248 23598136 23871047 24915368", "mw": "356.42", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "-0.4333", "instability": "179.53", "hydrophobic": "0.6667", "boman": "-1.1867", "helix": "0.3333", "turn_pct": "0.3333", "sheet": "0.3333" }, { "id": "aceip0632", "seq": "LQPEVMG", "length": "7", "detail": "Chinese water mocassin", "source": "Animal", "ic50": null, "reference": "Enterococcus faecalis strains from food, environmental, and clinical origin produce ACE-inhibitory peptides and other bioactive peptides during growth in bovine skim milk.", "doi": "10.1016\/j.ijfoodmicro.2013.06.019", "pubmedid": "23845432", "mw": "772.91", "pi": "4.05", "charge_ph7": "-1.24", "gravy": "0.1286", "instability": "107.49", "hydrophobic": "0.5714", "boman": "-1.3214", "helix": "0.4286", "turn_pct": "0.2857", "sheet": "0.2857" }, { "id": "aceip0633", "seq": "LQPEVMGVSK", "length": "10", "detail": "Lachesis muta", "source": "Animal", "ic50": null, "reference": "Enterococcus faecalis strains from food, environmental, and clinical origin produce ACE-inhibitory peptides and other bioactive peptides during growth in bovine skim milk.", "doi": "10.1016\/j.ijfoodmicro.2013.06.019", "pubmedid": "23845432", "mw": "1087.29", "pi": "6.0", "charge_ph7": "-0.24", "gravy": "0.04", "instability": "78.24", "hydrophobic": "0.5", "boman": "-1.087", "helix": "0.4", "turn_pct": "0.3", "sheet": "0.3" }, { "id": "aceip0634", "seq": "LQQ", "length": "3", "detail": "Lachesis muta", "source": "Animal", "ic50": "100 μM", "reference": "Structures and activity of angiotensin-converting enzyme inhibitors in an alpha-zein hydrolysate.; Isolation from alpha-zein of thermolysin peptides with angiotensin I-converting enzyme inhibitory activity.; Bioactive peptides in amaranth (Amaranthus hypochondriacus) seed.; Cellular membrane disruption by amyloid fibrils involved intermolecular disulfide cross-linking.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1271\/bbb.60.661; 10.1021\/jf072911z; 10.1021\/bi900219c; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "1368684 8829536 18211015 19449893 23871047", "mw": "387.43", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "-1.0667", "instability": "179.53", "hydrophobic": "0.3333", "boman": "-0.7333", "helix": "0.3333", "turn_pct": "0.0", "sheet": "0.3333" }, { "id": "aceip0635", "seq": "LQQQ", "length": "4", "detail": "Snake", "source": "Animal", "ic50": null, "reference": "Isolation from alpha-zein of thermolysin peptides with angiotensin I-converting enzyme inhibitory activity.", "doi": "10.1271\/bbb.60.661", "pubmedid": "8829536", "mw": "515.56", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "-1.675", "instability": "185.3", "hydrophobic": "0.25", "boman": "-0.21", "helix": "0.25", "turn_pct": "0.0", "sheet": "0.25" }, { "id": "aceip0636", "seq": "LQQQP", "length": "5", "detail": "Brazilian lancehead", "source": "Animal", "ic50": null, "reference": "Isolation from alpha-zein of thermolysin peptides with angiotensin I-converting enzyme inhibitory activity.", "doi": "10.1271\/bbb.60.661", "pubmedid": "8829536", "mw": "612.68", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "-1.66", "instability": "188.76", "hydrophobic": "0.4", "boman": "-0.168", "helix": "0.2", "turn_pct": "0.2", "sheet": "0.2" }, { "id": "aceip0637", "seq": "LQQQQ", "length": "5", "detail": "Snake", "source": "Animal", "ic50": null, "reference": "Isolation from alpha-zein of thermolysin peptides with angiotensin I-converting enzyme inhibitory activity.", "doi": "10.1271\/bbb.60.661", "pubmedid": "8829536", "mw": "643.69", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "-2.04", "instability": "188.76", "hydrophobic": "0.2", "boman": "0.104", "helix": "0.2", "turn_pct": "0.0", "sheet": "0.2" }, { "id": "aceip0638", "seq": "LQSW", "length": "4", "detail": "Lachesis muta", "source": "Animal", "ic50": "500 μM", "reference": "Identification of an antihypertensive peptide from casein hydrolysate produced by a proteinase from Lactobacillus helveticus CP790.; Identification of angiotensin-I-converting enzyme inhibitory peptides derived from sodium caseinate hydrolysates produced by Lactobacillus helveticus NCC 2765.; Antihypertensive peptides: production, bioavailability and incorporation into foods.; Antihypertensive peptides from food proteins: a review.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.3168\/jds.S0022-0302(96)76487-1; 10.1021\/jf049510t; 10.1016\/j.cis.2010.11.001; 10.1039\/c2fo10192k; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "8880454 15537298 21185549 22249830 23871047", "mw": "532.59", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "-0.35", "instability": "198.85", "hydrophobic": "0.5", "boman": "-1.2625", "helix": "0.25", "turn_pct": "0.25", "sheet": "0.5" }, { "id": "aceip0639", "seq": "LRIPVA", "length": "6", "detail": "Jararaca", "source": "Animal", "ic50": "0.38 μM", "reference": "Isolation and antihypertensive effect of angiotensin I-converting enzyme (ACE) inhibitory peptides from spinach Rubisco.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.; Vegetable foods: a cheap source of proteins and peptides with antihypertensive, antioxidant, and other less occurrence bioactivities.; Novel angiotensin I-converting enzyme inhibitory peptides derived from an edible mushroom, Pleurotus cystidiosus O.K. Miller identified by LC-MS\/MS.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1021\/jf026186y; 10.1016\/j.foodchem.2012.09.092; 10.1016\/j.talanta.2012.12.041; 10.1186\/1472-6882-13-313; 10.1080\/10408398.2012.664829", "pubmedid": "12903942 23194537 23598136 24215325 24915368", "mw": "667.84", "pi": "9.75", "charge_ph7": "0.76", "gravy": "1.3667", "instability": "67.73", "hydrophobic": "0.8333", "boman": "-2.1617", "helix": "0.3333", "turn_pct": "0.1667", "sheet": "0.5" }, { "id": "aceip0640", "seq": "LRP", "length": "3", "detail": "Chinese water mocassin", "source": "Animal", "ic50": "<10 μM", "reference": "Structures and activity of angiotensin-converting enzyme inhibitors in an alpha-zein hydrolysate.; Angiotensin I-converting enzyme inhibitory peptides derived from bonito bowels autolysate.; Production of bioactive peptides from corn endosperm proteins by some proteases.; Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Angiotensin converting enzyme inhibitory peptides derived from food proteins: biochemistry, bioactivity and production.; Bioactive peptides in amaranth (Amaranthus hypochondriacus) seed.; Cellular membrane disruption by amyloid fibrils involved intermolecular disulfide cross-linking.; Angiotensin I converting enzyme inhibitory peptides produced by autolysis reactions from wheat bran.; Inhibition strength of short peptides derived from an ACE inhibitory peptide.; Vegetable foods: a cheap source of proteins and peptides with antihypertensive, antioxidant, and other less occurrence bioactivities.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1271\/bbb.57.695; 10.1111\/j.1749-6632.1995.tb19990.x; 10.1021\/jf051263l; 10.2174\/138161207780363068; 10.1021\/jf072911z; 10.1021\/bi900219c; 10.1021\/jf900857w; 10.1021\/jf202902r; 10.1016\/j.talanta.2012.12.041; 10.1016\/j.foodchem.2013.05.140; 10.1080\/10408398.2012.664829", "pubmedid": "1368684 7763772 7785872 16448176 17430180 18211015 19449893 19572648 21923188 23598136 23871047 24915368", "mw": "384.47", "pi": "9.75", "charge_ph7": "0.76", "gravy": "-0.7667", "instability": "135.07", "hydrophobic": "0.6667", "boman": "-0.7333", "helix": "0.3333", "turn_pct": "0.3333", "sheet": "0.3333" }, { "id": "aceip0641", "seq": "LRW", "length": "3", "detail": "Brazilian lancehead", "source": "Animal", "ic50": "0 μM", "reference": "Restriction of the in vitro formation of angiotensin II by leucinyl-arginyl-tryptophan, a novel peptide with potent angiotensin I-converting enzyme inhibitory activity.", "doi": "10.1271\/bbb.70.1277", "pubmedid": "16717437", "mw": "473.57", "pi": "9.75", "charge_ph7": "0.76", "gravy": "-0.5333", "instability": "261.8", "hydrophobic": "0.6667", "boman": "-1.51", "helix": "0.3333", "turn_pct": "0.0", "sheet": "0.6667" }, { "id": "aceip0642", "seq": "LRY", "length": "3", "detail": "Brazilian lancehead", "source": "Animal", "ic50": "<10 μM", "reference": "Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.", "doi": "10.1021\/jf051263l", "pubmedid": "16448176", "mw": "450.53", "pi": "8.75", "charge_ph7": "0.76", "gravy": "-0.6667", "instability": "45.73", "hydrophobic": "0.3333", "boman": "-0.6867", "helix": "0.3333", "turn_pct": "0.0", "sheet": "0.6667" }, { "id": "aceip0643", "seq": "LSA", "length": "3", "detail": "Brazilian lancehead", "source": "Animal", "ic50": "0.33-5.80 mg\/ml", "reference": "Antihypertensive effect of angiotensin I-converting enzyme inhibitory peptides from a sesame protein hydrolysate in spontaneously hypertensive rats.; Vegetable foods: a cheap source of proteins and peptides with antihypertensive, antioxidant, and other less occurrence bioactivities.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1271\/bbb.70.1118; 10.1016\/j.talanta.2012.12.041; 10.1016\/j.foodchem.2013.05.140; 10.1080\/10408398.2012.664829", "pubmedid": "16717411 23598136 23871047 24915368", "mw": "289.33", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "1.6", "instability": "6.67", "hydrophobic": "0.6667", "boman": "-1.9633", "helix": "0.6667", "turn_pct": "0.3333", "sheet": "0.3333" }, { "id": "aceip0644", "seq": "LSKDIGSESTEDQAMED", "length": "17", "detail": "Brazilian lancehead", "source": "Animal", "ic50": null, "reference": "Casein fermentate of Lactobacillus animalis DPC6134 contains a range of novel propeptide angiotensin-converting enzyme inhibitors.", "doi": "10.1128\/AEM.00096-07", "pubmedid": "17483275", "mw": "1854.9", "pi": "4.05", "charge_ph7": "-5.23", "gravy": "-1.1706", "instability": "66.06", "hydrophobic": "0.2353", "boman": "0.0435", "helix": "0.4118", "turn_pct": "0.4118", "sheet": "0.1765" }, { "id": "aceip0645", "seq": "LSLP", "length": "4", "detail": "Brazilian lancehead", "source": "Animal", "ic50": null, "reference": "Isolation from alpha-zein of thermolysin peptides with angiotensin I-converting enzyme inhibitory activity.", "doi": "10.1271\/bbb.60.661", "pubmedid": "8829536", "mw": "428.52", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "1.3", "instability": "55.65", "hydrophobic": "0.75", "boman": "-2.25", "helix": "0.5", "turn_pct": "0.5", "sheet": "0.5" }, { "id": "aceip0646", "seq": "LSMGSASLSP", "length": "10", "detail": "Brazilian lancehead", "source": "Animal", "ic50": "0.19 mg\/ml", "reference": "Characterization of an antihypertensive angiotensin I-converting enzyme inhibitory peptide from the edible mushroom Hypsizygus marmoreus.", "doi": "10.1155\/2013\/283964", "pubmedid": "24380081", "mw": "949.08", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "0.61", "instability": "52.94", "hydrophobic": "0.5", "boman": "-1.158", "helix": "0.4", "turn_pct": "0.6", "sheet": "0.2" }, { "id": "aceip0647", "seq": "LSP", "length": "3", "detail": "Brazilian lancehead", "source": "Animal", "ic50": "<20 mM", "reference": "Structures and activity of angiotensin-converting enzyme inhibitors in an alpha-zein hydrolysate.; Production of bioactive peptides from corn endosperm proteins by some proteases.; Isolation from alpha-zein of thermolysin peptides with angiotensin I-converting enzyme inhibitory activity.; Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Bioactive peptides in amaranth (Amaranthus hypochondriacus) seed.; Cellular membrane disruption by amyloid fibrils involved intermolecular disulfide cross-linking.; Vegetable foods: a cheap source of proteins and peptides with antihypertensive, antioxidant, and other less occurrence bioactivities.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1111\/j.1749-6632.1995.tb19990.x; 10.1271\/bbb.60.661; 10.1021\/jf051263l; 10.1021\/jf072911z; 10.1021\/bi900219c; 10.1016\/j.talanta.2012.12.041; 10.1016\/j.foodchem.2013.05.140; 10.1080\/10408398.2012.664829", "pubmedid": "1368684 7785872 8829536 16448176 18211015 19449893 23598136 23871047 24915368", "mw": "315.37", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "0.4667", "instability": "153.13", "hydrophobic": "0.6667", "boman": "-1.36", "helix": "0.3333", "turn_pct": "0.6667", "sheet": "0.3333" }, { "id": "aceip0648", "seq": "LSPA", "length": "4", "detail": "Brazilian lancehead", "source": "Animal", "ic50": "315 μM", "reference": "Isolation from alpha-zein of thermolysin peptides with angiotensin I-converting enzyme inhibitory activity.; What are the ideal properties for functional food peptides with antihypertensive effect? 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What are the ideal properties for functional food peptides with antihypertensive effect? 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Antihypertensive effect of peptides obtained from Enterococcus faecalis-fermented milk in rats.; Antihypertensive peptides: production, bioavailability and incorporation into foods.; Antihypertensive peptides from food proteins: a review.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1128\/AEM.69.9.5297-5305.2003; 10.3168\/jds.S0022-0302(06)72372-4; 10.1016\/j.cis.2010.11.001; 10.1039\/c2fo10192k; 10.1016\/j.foodchem.2012.09.092", "pubmedid": "12957917 16899668 21185549 22249830 23194537", "mw": "2060.39", "pi": "5.52", "charge_ph7": "-0.24", "gravy": "-0.0316", "instability": "82.78", "hydrophobic": "0.6842", "boman": "-1.1611", "helix": "0.1053", "turn_pct": "0.5789", "sheet": "0.3684" }, { "id": "aceip0675", "seq": "LVYPFTGPIPN", "length": "11", "detail": "ND", "source": "ND", "ic50": "27.9 μM", "reference": "Angiotensin-converting enzyme inhibitory activity of peptides derived from caprine kefir.; Antihypertensive peptides from food proteins: a review.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.3168\/jds.S0022-0302(05)73032-0; 10.1039\/c2fo10192k; 10.1080\/10408398.2012.664829", "pubmedid": "16162521 22249830 24915368", "mw": "1217.41", "pi": "5.52", "charge_ph7": "-0.24", "gravy": "0.4182", "instability": "20.63", "hydrophobic": "0.6364", "boman": "-1.4345", "helix": "0.0909", "turn_pct": "0.4545", "sheet": "0.5455" }, { "id": "aceip0676", "seq": "LW", "length": "2", "detail": "Milk (whey)", "source": "Milk", "ic50": "<10 μM", "reference": "Angiotensin I-converting enzyme inhibitory peptides derived from wakame (Undaria pinnatifida) and their antihypertensive effect in spontaneously hypertensive rats.; Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Three-dimensional holograph vector of atomic interaction field (3D-HoVAIF): a novel rotation-translation invariant 3D structure descriptor and its applications to peptides.; Bioactive peptides in amaranth (Amaranthus hypochondriacus) seed.; Angiotensin I converting enzyme inhibitory peptides from simulated in vitro gastrointestinal digestion of cooked eggs.; Antihypertensive peptides from food proteins: a review.; Review on the angiotensin-I-converting enzyme (ACE) inhibitor peptides from marine proteins.; Vegetable foods: a cheap source of proteins and peptides with antihypertensive, antioxidant, and other less occurrence bioactivities.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1021\/jf020482t; 10.1021\/jf051263l; 10.1002\/psc.892; 10.1021\/jf072911z; 10.1021\/jf8028557; 10.1039\/c2fo10192k; 10.1007\/s12010-012-0024-y; 10.1016\/j.talanta.2012.12.041; 10.1016\/j.foodchem.2013.05.140; 10.1080\/10408398.2012.664829", "pubmedid": "12358510 16448176 17654623 18211015 19154160 22249830 23271625 23598136 23871047 24915368", "mw": "317.38", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "1.45", "instability": "123.4", "hydrophobic": "1.0", "boman": "-3.625", "helix": "0.5", "turn_pct": "0.0", "sheet": "1.0" }, { "id": "aceip0677", "seq": "LWA", "length": "3", "detail": "Milk (bovine)", "source": "Milk", "ic50": "<20 mM", "reference": "Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.", "doi": "10.1021\/jf051263l", "pubmedid": "16448176", "mw": "388.46", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "1.5667", "instability": "35.5", "hydrophobic": "1.0", "boman": "-3.02", "helix": "0.6667", "turn_pct": "0.0", "sheet": "0.6667" }, { "id": "aceip0678", "seq": "LY", "length": "2", "detail": "Milk (Fermented Milk)", "source": "Milk", "ic50": "<20 mM", "reference": "Angiotensin I-converting enzyme inhibitory peptides in an alkaline protease hydrolyzate derived from sardine muscle.; Isolation from alpha-zein of thermolysin peptides with angiotensin I-converting enzyme inhibitory activity.; Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Three-dimensional holograph vector of atomic interaction field (3D-HoVAIF): a novel rotation-translation invariant 3D structure descriptor and its applications to peptides.; Bioactive peptides in amaranth (Amaranthus hypochondriacus) seed.; Assessing the dependence of (51)V A(z) value on the aromatic ring orientation of V(IV)O(2+) pyridine complexes.; Review on the angiotensin-I-converting enzyme (ACE) inhibitor peptides from marine proteins.; Peptides with angiotensin I converting enzyme (ACE) inhibitory activity generated from porcine skeletal muscle proteins by the action of meat-borne Lactobacillus.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1271\/bbb.58.2244; 10.1271\/bbb.60.661; 10.1021\/jf051263l; 10.1002\/psc.892; 10.1021\/jf072911z; 10.1021\/ic9001779; 10.1007\/s12010-012-0024-y; 10.1016\/j.jprot.2013.06.023; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "7765718 8829536 16448176 17654623 18211015 19449891 23271625 23806758 23871047", "mw": "294.35", "pi": "5.52", "charge_ph7": "-0.24", "gravy": "1.25", "instability": "5.0", "hydrophobic": "0.5", "boman": "-2.39", "helix": "0.5", "turn_pct": "0.0", "sheet": "1.0" }, { "id": "aceip0679", "seq": "LYP", "length": "3", "detail": "Sweet-potato", "source": "Potato", "ic50": "<10 μM", "reference": "Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.", "doi": "10.1021\/jf051263l", "pubmedid": "16448176", "mw": "391.46", "pi": "5.52", "charge_ph7": "-0.24", "gravy": "0.3", "instability": "47.8", "hydrophobic": "0.6667", "boman": "-1.5933", "helix": "0.3333", "turn_pct": "0.3333", "sheet": "0.6667" }, { "id": "aceip0680", "seq": "LYPVK", "length": "5", "detail": "Milk (caprine kefir)", "source": "Milk", "ic50": "4.5 μM", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "23194537", "mw": "618.76", "pi": "8.59", "charge_ph7": "0.76", "gravy": "0.24", "instability": "65.44", "hydrophobic": "0.6", "boman": "-1.448", "helix": "0.4", "turn_pct": "0.2", "sheet": "0.6" }, { "id": "aceip0681", "seq": "LYQA", "length": "4", "detail": "Milk (bovine, buffalo and ovine)", "source": "Milk", "ic50": null, "reference": "Vegetable foods: a cheap source of proteins and peptides with antihypertensive, antioxidant, and other less occurrence bioactivities.", "doi": "10.1016\/j.talanta.2012.12.041", "pubmedid": "23598136", "mw": "493.55", "pi": "5.52", "charge_ph7": "-0.24", "gravy": "0.2", "instability": "7.5", "hydrophobic": "0.5", "boman": "-1.3075", "helix": "0.5", "turn_pct": "0.0", "sheet": "0.5" }, { "id": "aceip0682", "seq": "MA", "length": "2", "detail": "Milk (human)", "source": "Milk", "ic50": "152.0 μM", "reference": "Bioactive peptides in amaranth (Amaranthus hypochondriacus) seed.", "doi": "10.1021\/jf072911z", "pubmedid": "18211015", "mw": "220.29", "pi": "5.28", "charge_ph7": "-0.5", "gravy": "1.85", "instability": "66.7", "hydrophobic": "1.0", "boman": "-2.08", "helix": "1.0", "turn_pct": "0.0", "sheet": "0.0" }, { "id": "aceip0683", "seq": "MAIPPKK", "length": "7", "detail": "ND", "source": "ND", "ic50": "92 mg\/ml", "reference": "Antihypertensive peptides: production, bioavailability and incorporation into foods.", "doi": "10.1016\/j.cis.2010.11.001", "pubmedid": "21185549", "mw": "784.02", "pi": "10.0", "charge_ph7": "1.5", "gravy": "-0.4", "instability": "49.6", "hydrophobic": "0.7143", "boman": "-0.8457", "helix": "0.5714", "turn_pct": "0.2857", "sheet": "0.1429" }, { "id": "aceip0684", "seq": "MAP", "length": "3", "detail": "Milk", "source": "Milk", "ic50": "0.8 μM", "reference": "Antihypertensive peptides from food proteins: a review.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1039\/c2fo10192k; 10.1080\/10408398.2012.664829", "pubmedid": "22249830 24915368", "mw": "317.4", "pi": "5.28", "charge_ph7": "-0.5", "gravy": "0.7", "instability": "112.0", "hydrophobic": "1.0", "boman": "-1.3867", "helix": "0.6667", "turn_pct": "0.3333", "sheet": "0.0" }, { "id": "aceip0685", "seq": "MAW", "length": "3", "detail": "Cheese", "source": "Milk", "ic50": "0.0042 mg\/ml", "reference": "What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1016\/j.foodchem.2013.05.140", "pubmedid": "23871047", "mw": "406.5", "pi": "5.28", "charge_ph7": "-0.5", "gravy": "0.9333", "instability": "47.8", "hydrophobic": "1.0", "boman": "-2.1633", "helix": "0.6667", "turn_pct": "0.0", "sheet": "0.3333" }, { "id": "aceip0686", "seq": "MDFLI", "length": "5", "detail": "Milk (Casein) | Cheese (Manchego cheese)", "source": "Milk", "ic50": "0.01 μM", "reference": "Angiotensin converting enzyme inhibitory peptides derived from food proteins: biochemistry, bioactivity and production.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.; Vegetable foods: a cheap source of proteins and peptides with antihypertensive, antioxidant, and other less occurrence bioactivities.", "doi": "10.2174\/138161207780363068; 10.1016\/j.foodchem.2012.09.092; 10.1016\/j.talanta.2012.12.041", "pubmedid": "17430180 23194537 23598136", "mw": "637.79", "pi": "4.05", "charge_ph7": "-1.5", "gravy": "1.9", "instability": "-7.08", "hydrophobic": "0.8", "boman": "-2.698", "helix": "0.4", "turn_pct": "0.2", "sheet": "0.6" }, { "id": "aceip0687", "seq": "MDLA", "length": "4", "detail": "Milk (bovine) | Carp | Cereals | Pork | Chicken", "source": "Milk | Fish | Cereal | Porcine | Chicken", "ic50": "0.01 μM", "reference": "Angiotensin converting enzyme inhibitory peptides derived from food proteins: biochemistry, bioactivity and production.", "doi": "10.2174\/138161207780363068", "pubmedid": "17430180", "mw": "448.53", "pi": "4.05", "charge_ph7": "-1.5", "gravy": "1.0", "instability": "7.5", "hydrophobic": "0.75", "boman": "-1.85", "helix": "0.75", "turn_pct": "0.25", "sheet": "0.25" }, { "id": "aceip0688", "seq": "ME", "length": "2", "detail": "ND", "source": "ND", "ic50": "0 0", "reference": "Application of at-line two-dimensional liquid chromatography-mass spectrometry for identification of small hydrophilic angiotensin I-inhibiting peptides in milk hydrolysates.", "doi": "10.1007\/s00216-008-1990-3", "pubmedid": "18392815", "mw": "278.33", "pi": "4.6", "charge_ph7": "-1.49", "gravy": "-0.8", "instability": "5.0", "hydrophobic": "0.5", "boman": "-0.355", "helix": "1.0", "turn_pct": "0.0", "sheet": "0.0" }, { "id": "aceip0689", "seq": "MEGAQEAQGD", "length": "10", "detail": "Pork", "source": "Porcine", "ic50": "0.0165 mg\/ml", "reference": "Antihypertensive peptides from food proteins: a review.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1039\/c2fo10192k; 10.1080\/10408398.2012.664829", "pubmedid": "22249830 24915368", "mw": "1035.04", "pi": "4.05", "charge_ph7": "-3.49", "gravy": "-1.28", "instability": "19.77", "hydrophobic": "0.3", "boman": "-0.017", "helix": "0.5", "turn_pct": "0.3", "sheet": "0.0" }, { "id": "aceip0690", "seq": "MF", "length": "2", "detail": "Legume (Mung bean)", "source": "Legume", "ic50": "<20 mM", "reference": "Angiotensin I-converting enzyme inhibitory peptides in an alkaline protease hydrolyzate derived from sardine muscle.; Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Bioactive peptides in amaranth (Amaranthus hypochondriacus) seed.; Assessing the dependence of (51)V A(z) value on the aromatic ring orientation of V(IV)O(2+) pyridine complexes.; Review on the angiotensin-I-converting enzyme (ACE) inhibitor peptides from marine proteins.; Peptides with angiotensin I converting enzyme (ACE) inhibitory activity generated from porcine skeletal muscle proteins by the action of meat-borne Lactobacillus.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1271\/bbb.58.2244; 10.1021\/jf051263l; 10.1021\/jf072911z; 10.1021\/ic9001779; 10.1007\/s12010-012-0024-y; 10.1016\/j.jprot.2013.06.023; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "7765718 16448176 18211015 19449891 23271625 23806758 23871047", "mw": "296.39", "pi": "5.28", "charge_ph7": "-0.5", "gravy": "2.35", "instability": "5.0", "hydrophobic": "1.0", "boman": "-2.665", "helix": "0.5", "turn_pct": "0.0", "sheet": "0.5" }, { "id": "aceip0691", "seq": "MFDL", "length": "4", "detail": "Milk (bovine) | Anchovy (sauce) | Fermented fish sauce | Cereals (Wheat) | Pork", "source": "Milk | Fish | Cereal | Porcine", "ic50": "0.01 μM", "reference": "Angiotensin converting enzyme inhibitory peptides derived from food proteins: biochemistry, bioactivity and production.", "doi": "10.2174\/138161207780363068", "pubmedid": "17430180", "mw": "524.63", "pi": "4.05", "charge_ph7": "-1.5", "gravy": "1.25", "instability": "38.35", "hydrophobic": "0.75", "boman": "-2.1425", "helix": "0.5", "turn_pct": "0.25", "sheet": "0.5" }, { "id": "aceip0692", "seq": "MG", "length": "2", "detail": "ND", "source": "ND", "ic50": "<20 mM", "reference": "Binding of peptide substrates and inhibitors of angiotensin-converting enzyme. Importance of the COOH-terminal dipeptide sequence.; Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Three-dimensional holograph vector of atomic interaction field (3D-HoVAIF): a novel rotation-translation invariant 3D structure descriptor and its applications to peptides.; QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1021\/jf051263l; 10.1002\/psc.892; 10.1007\/s00894-010-0862-x; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "6243277 16448176 17654623 20941517 23871047", "mw": "206.26", "pi": "5.28", "charge_ph7": "-0.5", "gravy": "0.75", "instability": "5.0", "hydrophobic": "0.5", "boman": "-1.645", "helix": "0.5", "turn_pct": "0.5", "sheet": "0.0" }, { "id": "aceip0693", "seq": "MIFPGAGGPEL", "length": "11", "detail": "ND", "source": "ND", "ic50": "0.03 μM", "reference": "Angiotensin converting enzyme inhibitory peptides derived from food proteins: biochemistry, bioactivity and production.; Antihypertensive peptides from food proteins: a review.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.; Review on the angiotensin-I-converting enzyme (ACE) inhibitor peptides from marine proteins.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.2174\/138161207780363068; 10.1039\/c2fo10192k; 10.1016\/j.foodchem.2012.09.092; 10.1007\/s12010-012-0024-y; 10.1080\/10408398.2012.664829", "pubmedid": "17430180 22249830 23194537 23271625 24915368", "mw": "1088.28", "pi": "4.05", "charge_ph7": "-1.5", "gravy": "0.6273", "instability": "45.9", "hydrophobic": "0.6364", "boman": "-1.6509", "helix": "0.3636", "turn_pct": "0.4545", "sheet": "0.2727" }, { "id": "aceip0694", "seq": "MIFPGGPQL", "length": "9", "detail": "Shrimp", "source": "Shrimp", "ic50": "22.3 μM", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "23194537", "mw": "959.16", "pi": "5.28", "charge_ph7": "-0.5", "gravy": "0.6111", "instability": "65.4", "hydrophobic": "0.6667", "boman": "-1.7433", "helix": "0.2222", "turn_pct": "0.4444", "sheet": "0.3333" }, { "id": "aceip0695", "seq": "MIPAY", "length": "5", "detail": "Casein", "source": "Milk", "ic50": "8.7 μM", "reference": "Rational design of angiotensin-I-converting enzyme inhibitory peptides by integrating in silico modeling and an in vitro assay.", "doi": "10.1002\/cmdc.201300132", "pubmedid": "23740817", "mw": "593.74", "pi": "5.27", "charge_ph7": "-0.5", "gravy": "1.06", "instability": "40.76", "hydrophobic": "0.8", "boman": "-1.788", "helix": "0.4", "turn_pct": "0.2", "sheet": "0.4" }, { "id": "aceip0696", "seq": "MKPWIQPK", "length": "8", "detail": "Cheese (Manchego cheese)", "source": "Milk", "ic50": "300 μM", "reference": "Identification of an antihypertensive peptide from casein hydrolysate produced by a proteinase from Lactobacillus helveticus CP790.; Identification of angiotensin-I-converting enzyme inhibitory peptides derived from sodium caseinate hydrolysates produced by Lactobacillus helveticus NCC 2765.; Antihypertensive peptides: production, bioavailability and incorporation into foods.; Antihypertensive peptides from food proteins: a review.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.3168\/jds.S0022-0302(96)76487-1; 10.1021\/jf049510t; 10.1016\/j.cis.2010.11.001; 10.1039\/c2fo10192k; 10.1016\/j.foodchem.2012.09.092", "pubmedid": "8880454 15537298 21185549 22249830 23194537", "mw": "1027.28", "pi": "10.0", "charge_ph7": "1.5", "gravy": "-1.125", "instability": "19.8", "hydrophobic": "0.625", "boman": "-0.635", "helix": "0.375", "turn_pct": "0.25", "sheet": "0.25" }, { "id": "aceip0697", "seq": "MKR", "length": "3", "detail": "Cereals | Pork | Chicken", "source": "Cereal | Porcine | Chicken", "ic50": "25.7 μM", "reference": "ACE inhibitory peptides and antioxidant peptides derived from in vitro digestion hydrolysate of hen egg white lysozyme.", "doi": "10.1016\/j.foodchem.2012.05.059", "pubmedid": "22953850", "mw": "433.57", "pi": "11.0", "charge_ph7": "1.5", "gravy": "-2.1667", "instability": "115.33", "hydrophobic": "0.3333", "boman": "0.65", "helix": "0.6667", "turn_pct": "0.0", "sheet": "0.0" }, { "id": "aceip0698", "seq": "MKY", "length": "3", "detail": "Pork | Porcine", "source": "Porcine", "ic50": "<20 mM", "reference": "Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.", "doi": "10.1021\/jf051263l", "pubmedid": "16448176", "mw": "440.56", "pi": "8.34", "charge_ph7": "0.5", "gravy": "-1.1", "instability": "6.67", "hydrophobic": "0.3333", "boman": "-0.21", "helix": "0.6667", "turn_pct": "0.0", "sheet": "0.3333" }, { "id": "aceip0699", "seq": "MLGQTPT", "length": "7", "detail": "Pork", "source": "Porcine", "ic50": null, "reference": "Angiotensin I-converting enzyme inhibitory peptides generated from in vitro gastrointestinal digestion of pork meat.", "doi": "10.1021\/jf904204n", "pubmedid": "20151679", "mw": "746.87", "pi": "5.28", "charge_ph7": "-0.5", "gravy": "-0.1714", "instability": "8.57", "hydrophobic": "0.4286", "boman": "-0.9043", "helix": "0.2857", "turn_pct": "0.2857", "sheet": "0.4286" }, { "id": "aceip0700", "seq": "MLGQTPTK", "length": "8", "detail": "Milk (human)", "source": "Milk", "ic50": null, "reference": "Inhibitory profile of nonapeptide derived from porcine troponin C against angiotensin I-converting enzyme.", "doi": "10.1021\/jf0350865", "pubmedid": "14969529", "mw": "875.04", "pi": "8.5", "charge_ph7": "0.5", "gravy": "-0.6375", "instability": "8.75", "hydrophobic": "0.375", "boman": "-0.5937", "helix": "0.375", "turn_pct": "0.25", "sheet": "0.375" }, { "id": "aceip0701", "seq": "MLPAY", "length": "5", "detail": "Fungi (Agaricus bisporus)", "source": "Fungi", "ic50": "0.33-5.80 mg\/ml", "reference": "Antihypertensive effect of angiotensin I-converting enzyme inhibitory peptides from a sesame protein hydrolysate in spontaneously hypertensive rats.; Vegetable foods: a cheap source of proteins and peptides with antihypertensive, antioxidant, and other less occurrence bioactivities.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1271\/bbb.70.1118; 10.1016\/j.talanta.2012.12.041; 10.1080\/10408398.2012.664829", "pubmedid": "16717411 23598136 24915368", "mw": "593.74", "pi": "5.27", "charge_ph7": "-0.5", "gravy": "0.92", "instability": "85.04", "hydrophobic": "0.8", "boman": "-1.788", "helix": "0.6", "turn_pct": "0.2", "sheet": "0.4" }, { "id": "aceip0702", "seq": "MMVPI", "length": "5", "detail": "Milk (Sheep raw milk cheese (synthesised))", "source": "Milk", "ic50": "46.56>1000 μM", "reference": "Angiotensin I-converting enzyme inhibitory peptides generated from in vitro gastrointestinal digestion of pork meat.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1021\/jf904204n; 10.1080\/10408398.2012.664829", "pubmedid": "20151679 24915368", "mw": "589.81", "pi": "5.28", "charge_ph7": "-0.5", "gravy": "2.18", "instability": "40.76", "hydrophobic": "1.0", "boman": "-2.732", "helix": "0.4", "turn_pct": "0.2", "sheet": "0.4" }, { "id": "aceip0703", "seq": "MNP", "length": "3", "detail": "ND", "source": "ND", "ic50": "<20 mM", "reference": "Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Angiotensin-I converting enzyme inhibitory peptide derived from porcine skeletal muscle myosin and its antihypertensive activity in spontaneously hypertensive rats.; Peptide inhibitors for angiotensin I-converting enzyme from enzymatic hydrolysates of porcine skeletal muscle proteins.", "doi": "10.1021\/jf051263l; 10.1111\/j.1750-3841.2007.00571.x; 10.1016\/s0309-1740(00)00108-x", "pubmedid": "16448176 18034756 22061507", "mw": "360.43", "pi": "5.28", "charge_ph7": "-0.5", "gravy": "-1.0667", "instability": "-2.93", "hydrophobic": "0.6667", "boman": "-0.2433", "helix": "0.3333", "turn_pct": "0.6667", "sheet": "0.0" }, { "id": "aceip0704", "seq": "MNPPK", "length": "5", "detail": "Sardine", "source": "Fish", "ic50": "945.5 μM", "reference": "Angiotensin-I converting enzyme inhibitory peptide derived from porcine skeletal muscle myosin and its antihypertensive activity in spontaneously hypertensive rats.; Angiotensin I-converting enzyme-inhibitory peptides obtained from chicken collagen hydrolysate.; Peptide inhibitors for angiotensin I-converting enzyme from enzymatic hydrolysates of porcine skeletal muscle proteins.; Antihypertensive peptides from food proteins: a review.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1111\/j.1750-3841.2007.00571.x; 10.1021\/jf072669w; 10.1016\/s0309-1740(00)00108-x; 10.1039\/c2fo10192k; 10.1016\/j.foodchem.2012.09.092; 10.1080\/10408398.2012.664829", "pubmedid": "18034756 18808143 22061507 22249830 23194537 24915368", "mw": "585.72", "pi": "8.5", "charge_ph7": "0.5", "gravy": "-1.74", "instability": "40.76", "hydrophobic": "0.6", "boman": "0.17", "helix": "0.4", "turn_pct": "0.6", "sheet": "0.0" }, { "id": "aceip0705", "seq": "MNVKHWPWMK", "length": "10", "detail": "Milk (Casein)", "source": "Milk", "ic50": "228 μM", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "23194537", "mw": "1356.66", "pi": "10.0", "charge_ph7": "1.59", "gravy": "-0.99", "instability": "24.04", "hydrophobic": "0.6", "boman": "-0.763", "helix": "0.4", "turn_pct": "0.2", "sheet": "0.3" }, { "id": "aceip0706", "seq": "MPF", "length": "3", "detail": "Lactobacillus helveticus", "source": "Bacteria", "ic50": "6.59-27.38 μM", "reference": "Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1080\/10408398.2012.664829", "pubmedid": "24915368", "mw": "393.5", "pi": "5.28", "charge_ph7": "-0.5", "gravy": "1.0333", "instability": "217.33", "hydrophobic": "1.0", "boman": "-1.7767", "helix": "0.3333", "turn_pct": "0.3333", "sheet": "0.3333" }, { "id": "aceip0707", "seq": "MPFPKYPVEP", "length": "10", "detail": "Milk (bovine) | Casein | Lactobacillus helveticus | Clostripain", "source": "Milk | Bacteria", "ic50": "83 μM", "reference": "Casein fermentate of Lactobacillus animalis DPC6134 contains a range of novel propeptide angiotensin-converting enzyme inhibitors.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1128\/AEM.00096-07; 10.1016\/j.foodchem.2012.09.092", "pubmedid": "17483275 23194537", "mw": "1204.44", "pi": "5.75", "charge_ph7": "-0.5", "gravy": "-0.62", "instability": "142.32", "hydrophobic": "0.7", "boman": "-0.601", "helix": "0.3", "turn_pct": "0.4", "sheet": "0.3" }, { "id": "aceip0708", "seq": "MPFPKYPVQPF", "length": "11", "detail": "Milk (Fermented Milk) | Lactobacillus helveticus", "source": "Milk | Bacteria", "ic50": null, "reference": "Isolation and structural analysis of antihypertensive peptides that exist naturally in Gouda cheese.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.3168\/jds.S0022-0302(00)75013-2; 10.1080\/10408398.2012.664829", "pubmedid": "10908049 24915368", "mw": "1350.63", "pi": "8.34", "charge_ph7": "0.5", "gravy": "-0.3091", "instability": "147.8", "hydrophobic": "0.7273", "boman": "-0.8427", "helix": "0.1818", "turn_pct": "0.3636", "sheet": "0.3636" }, { "id": "aceip0709", "seq": "MPP", "length": "3", "detail": "Milk (bovine) | Casein | Milk (Casein) | Lactobacillus helveticus", "source": "Milk | Bacteria", "ic50": "<20 mM", "reference": "Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.", "doi": "10.1021\/jf051263l", "pubmedid": "16448176", "mw": "343.44", "pi": "5.28", "charge_ph7": "-0.5", "gravy": "-0.4333", "instability": "217.33", "hydrophobic": "1.0", "boman": "-0.7833", "helix": "0.3333", "turn_pct": "0.6667", "sheet": "0.0" }, { "id": "aceip0710", "seq": "MRW", "length": "3", "detail": "Egg (Ovalbumin)", "source": "Egg", "ic50": "<20 mM", "reference": "Isolation and antihypertensive effect of angiotensin I-converting enzyme (ACE) inhibitory peptides from spinach Rubisco.; Met-Arg-Trp derived from Rubisco lowers blood pressure via prostaglandin D(2)-dependent vasorelaxation in spontaneously hypertensive rats.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1021\/jf026186y; 10.1016\/j.peptides.2007.11.011; 10.1080\/10408398.2012.664829", "pubmedid": "12903942 18180074 24915368", "mw": "491.61", "pi": "9.5", "charge_ph7": "0.5", "gravy": "-1.1667", "instability": "172.47", "hydrophobic": "0.6667", "boman": "-0.6533", "helix": "0.3333", "turn_pct": "0.0", "sheet": "0.3333" }, { "id": "aceip0711", "seq": "MRWRD", "length": "5", "detail": "Egg (Ovalbumin)", "source": "Egg", "ic50": "2.09 μM", "reference": "Isolation and antihypertensive effect of angiotensin I-converting enzyme (ACE) inhibitory peptides from spinach Rubisco.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.; Vegetable foods: a cheap source of proteins and peptides with antihypertensive, antioxidant, and other less occurrence bioactivities.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1021\/jf026186y; 10.1016\/j.foodchem.2012.09.092; 10.1016\/j.talanta.2012.12.041; 10.1080\/10408398.2012.664829", "pubmedid": "12903942 23194537 23598136 24915368", "mw": "762.88", "pi": "9.35", "charge_ph7": "0.5", "gravy": "-2.3", "instability": "107.48", "hydrophobic": "0.4", "boman": "0.488", "helix": "0.2", "turn_pct": "0.2", "sheet": "0.2" }, { "id": "aceip0712", "seq": "MVGSAPGVL", "length": "9", "detail": "ND", "source": "ND", "ic50": "3.09 μM", "reference": "Active peptides from skate (Okamejei kenojei) skin gelatin diminish angiotensin-I converting enzyme activity and intracellular free radical-mediated oxidation.", "doi": "10.1016\/j.foodchem.2013.07.067", "pubmedid": "24054237", "mw": "830.0", "pi": "5.28", "charge_ph7": "-0.5", "gravy": "1.4111", "instability": "20.86", "hydrophobic": "0.6667", "boman": "-2.0222", "helix": "0.3333", "turn_pct": "0.4444", "sheet": "0.3333" }, { "id": "aceip0713", "seq": "MW", "length": "2", "detail": "Egg (Ovotransferrin)", "source": "Egg", "ic50": "<10 μM", "reference": "Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Antihypertensive peptides from food proteins: a review.; Review on the angiotensin-I-converting enzyme (ACE) inhibitor peptides from marine proteins.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1021\/jf051263l; 10.1039\/c2fo10192k; 10.1007\/s12010-012-0024-y; 10.1016\/j.foodchem.2013.05.140; 10.1080\/10408398.2012.664829", "pubmedid": "16448176 22249830 23271625 23871047 24915368", "mw": "335.42", "pi": "5.28", "charge_ph7": "-0.5", "gravy": "0.5", "instability": "5.0", "hydrophobic": "1.0", "boman": "-2.34", "helix": "0.5", "turn_pct": "0.0", "sheet": "0.5" }, { "id": "aceip0714", "seq": "MY", "length": "2", "detail": "ND", "source": "ND", "ic50": "<20 mM", "reference": "Angiotensin I-converting enzyme inhibitory peptides in an alkaline protease hydrolyzate derived from sardine muscle.; Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Bioactive peptides in amaranth (Amaranthus hypochondriacus) seed.; Review on the angiotensin-I-converting enzyme (ACE) inhibitor peptides from marine proteins.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1271\/bbb.58.2244; 10.1021\/jf051263l; 10.1021\/jf072911z; 10.1007\/s12010-012-0024-y; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "7765718 16448176 18211015 23271625 23871047", "mw": "312.38", "pi": "5.27", "charge_ph7": "-0.5", "gravy": "0.3", "instability": "123.4", "hydrophobic": "0.5", "boman": "-1.105", "helix": "0.5", "turn_pct": "0.0", "sheet": "0.5" }, { "id": "aceip0715", "seq": "MYPGIA", "length": "6", "detail": "Milk (bovine) | Wakame | Synthesized | Sardine | Cereals | Pork | Chicken", "source": "Milk | Plants | Synthesized | Fish | Cereal | Porcine | Chicken", "ic50": "641.02 μM", "reference": "Angiotensin I-converting enzyme inhibitory peptides generated from in vitro gastrointestinal digestion of pork meat.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1021\/jf904204n; 10.1016\/j.foodchem.2012.09.092; 10.1080\/10408398.2012.664829", "pubmedid": "20151679 23194537 24915368", "mw": "650.79", "pi": "5.27", "charge_ph7": "-0.5", "gravy": "0.8167", "instability": "54.22", "hydrophobic": "0.6667", "boman": "-1.6467", "helix": "0.3333", "turn_pct": "0.3333", "sheet": "0.3333" }, { "id": "aceip0716", "seq": "MYY", "length": "3", "detail": "Synthesized", "source": "Synthesized", "ic50": "9.6 μM", "reference": "Inhibition of angiotensin-converting enzyme by synthetic peptide fragments of human kappa-casein.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1016\/j.foodchem.2013.05.140", "pubmedid": "1368540 23871047", "mw": "475.56", "pi": "5.27", "charge_ph7": "-0.5", "gravy": "-0.2333", "instability": "126.73", "hydrophobic": "0.3333", "boman": "-0.69", "helix": "0.3333", "turn_pct": "0.0", "sheet": "0.6667" }, { "id": "aceip0717", "seq": "NAQRP", "length": "5", "detail": "Synthesized", "source": "Synthesized", "ic50": "32 μM", "reference": "Glycinyl-histidinyl-serine (GHS), a novel rapeseed protein-derived peptide has blood pressure-lowering effect in spontaneously hypertensive rats.", "doi": "10.1021\/jf400865m", "pubmedid": "23919612", "mw": "584.63", "pi": "9.75", "charge_ph7": "0.76", "gravy": "-2.26", "instability": "46.52", "hydrophobic": "0.4", "boman": "0.778", "helix": "0.2", "turn_pct": "0.4", "sheet": "0.0" }, { "id": "aceip0718", "seq": "NELSKDI", "length": "7", "detail": "Milk (bovine) | Wakame | Sardine | Cereals | Pork | Chicken", "source": "Milk | Plants | Fish | Cereal | Porcine | Chicken", "ic50": null, "reference": "Hot topic: Changes in angiotensin-converting enzyme inhibition and concentrations of the tripeptides Val-Pro-Pro and Ile-Pro-Pro during ripening of different Swiss cheese varieties.", "doi": "10.3168\/jds.2008-1531", "pubmedid": "19233775", "mw": "817.88", "pi": "4.37", "charge_ph7": "-1.24", "gravy": "-0.9857", "instability": "8.57", "hydrophobic": "0.2857", "boman": "-0.3543", "helix": "0.4286", "turn_pct": "0.4286", "sheet": "0.2857" }, { "id": "aceip0719", "seq": "NENLLRFFVAPFPE", "length": "14", "detail": "Milk", "source": "Milk", "ic50": null, "reference": "Identification of angiotensin-I-converting enzyme inhibitory peptides derived from sodium caseinate hydrolysates produced by Lactobacillus helveticus NCC 2765.", "doi": "10.1021\/jf049510t", "pubmedid": "15537298", "mw": "1692.91", "pi": "4.86", "charge_ph7": "-1.23", "gravy": "0.0214", "instability": "76.73", "hydrophobic": "0.6429", "boman": "-1.0993", "helix": "0.3571", "turn_pct": "0.2857", "sheet": "0.4286" }, { "id": "aceip0720", "seq": "NENLLRFFVAPFPEVFG", "length": "17", "detail": "Milk (bovine)", "source": "Milk", "ic50": "55 μM", "reference": "Identification of angiotensin-I-converting enzyme inhibitory peptides derived from sodium caseinate hydrolysates produced by Lactobacillus helveticus NCC 2765.", "doi": "10.1021\/jf049510t", "pubmedid": "15537298", "mw": "1996.27", "pi": "4.53", "charge_ph7": "-1.23", "gravy": "0.4059", "instability": "64.95", "hydrophobic": "0.6471", "boman": "-1.3735", "helix": "0.2941", "turn_pct": "0.2941", "sheet": "0.4706" }, { "id": "aceip0721", "seq": "NF", "length": "2", "detail": "Milk (Casein)", "source": "Milk", "ic50": "<20 mM", "reference": "Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Max-E47, a designed minimalist protein that targets the E-box DNA site in vivo and in vitro.; Vegetable foods: a cheap source of proteins and peptides with antihypertensive, antioxidant, and other less occurrence bioactivities.; Peptides with angiotensin I converting enzyme (ACE) inhibitory activity generated from porcine skeletal muscle proteins by the action of meat-borne Lactobacillus.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1021\/jf051263l; 10.1021\/ja901306q; 10.1016\/j.talanta.2012.12.041; 10.1016\/j.jprot.2013.06.023; 10.1080\/10408398.2012.664829", "pubmedid": "16448176 19449889 23598136 23806758 24915368", "mw": "279.29", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "-0.35", "instability": "-70.15", "hydrophobic": "0.5", "boman": "-0.68", "helix": "0.0", "turn_pct": "0.5", "sheet": "0.5" }, { "id": "aceip0722", "seq": "NHRNRMMDHVH", "length": "11", "detail": "Milk (bovine)", "source": "Milk", "ic50": "13.42 μM", "reference": "Identification of angiotensin I-converting enzyme inhibitory peptides from koumiss, a traditional fermented mare's milk.", "doi": "10.3168\/jds.2009-2672", "pubmedid": "20172208", "mw": "1446.62", "pi": "9.62", "charge_ph7": "1.02", "gravy": "-1.9182", "instability": "17.69", "hydrophobic": "0.2727", "boman": "0.4173", "helix": "0.1818", "turn_pct": "0.2727", "sheet": "0.0909" }, { "id": "aceip0723", "seq": "NIDTDI", "length": "6", "detail": "Milk (bovine)", "source": "Milk", "ic50": null, "reference": "Release of angiotensin I-converting enzyme inhibitory peptides from flaxseed (Linum usitatissimum L.) protein under simulated gastrointestinal digestion.", "doi": "10.1021\/jf202000e", "pubmedid": "21776963", "mw": "689.71", "pi": "4.05", "charge_ph7": "-2.24", "gravy": "-0.3667", "instability": "56.52", "hydrophobic": "0.3333", "boman": "-0.7667", "helix": "0.0", "turn_pct": "0.5", "sheet": "0.5" }, { "id": "aceip0724", "seq": "NIDTDL", "length": "6", "detail": "Milk (bovine) | Cereals (Wheat) | Chicken", "source": "Milk | Cereal | Chicken", "ic50": null, "reference": "Release of angiotensin I-converting enzyme inhibitory peptides from flaxseed (Linum usitatissimum L.) protein under simulated gastrointestinal digestion.", "doi": "10.1021\/jf202000e", "pubmedid": "21776963", "mw": "689.71", "pi": "4.05", "charge_ph7": "-2.24", "gravy": "-0.4833", "instability": "56.52", "hydrophobic": "0.3333", "boman": "-0.7667", "helix": "0.1667", "turn_pct": "0.5", "sheet": "0.5" }, { "id": "aceip0725", "seq": "NIFYCP", "length": "6", "detail": "Amaranth | Cereals (Maize) | Maize", "source": "Plants | Cereal", "ic50": "15 μM", "reference": "Angiotensin I converting enzyme inhibitory peptides from simulated in vitro gastrointestinal digestion of cooked eggs.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1021\/jf8028557; 10.1016\/j.foodchem.2012.09.092; 10.1080\/10408398.2012.664829", "pubmedid": "19154160 23194537 24915368", "mw": "755.88", "pi": "5.52", "charge_ph7": "-0.25", "gravy": "0.5667", "instability": "168.0", "hydrophobic": "0.5", "boman": "-1.2367", "helix": "0.0", "turn_pct": "0.3333", "sheet": "0.5" }, { "id": "aceip0726", "seq": "NIIPA", "length": "5", "detail": "Milk (bovine) | Milk (whey)", "source": "Milk", "ic50": "46.56>1000 μM", "reference": "Angiotensin I-converting enzyme inhibitory peptides generated from in vitro gastrointestinal digestion of pork meat.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1021\/jf904204n; 10.1080\/10408398.2012.664829", "pubmedid": "20151679 24915368", "mw": "526.63", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "1.14", "instability": "128.64", "hydrophobic": "0.8", "boman": "-2.006", "helix": "0.2", "turn_pct": "0.4", "sheet": "0.4" }, { "id": "aceip0727", "seq": "NILP", "length": "4", "detail": "Soybean", "source": "Legume", "ic50": "560 μM", "reference": "Inhibition of angiotensin-converting enzyme by synthetic peptide fragments of various beta-caseins.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1016\/j.foodchem.2013.05.140", "pubmedid": "1368548 23871047", "mw": "455.55", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "0.8", "instability": "213.65", "hydrophobic": "0.75", "boman": "-2.055", "helix": "0.25", "turn_pct": "0.5", "sheet": "0.5" }, { "id": "aceip0728", "seq": "NIPPLTQTPV", "length": "10", "detail": "Casein | Milk (human)", "source": "Milk", "ic50": "173 μM", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "23194537", "mw": "1079.25", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "-0.07", "instability": "81.04", "hydrophobic": "0.6", "boman": "-1.038", "helix": "0.1", "turn_pct": "0.4", "sheet": "0.5" }, { "id": "aceip0729", "seq": "NIPPLTQTPVVVPPFIQ", "length": "17", "detail": "Milk | Milk (whey) | Amaranth | Cereals", "source": "Milk | Plants | Cereal", "ic50": "450 μM", "reference": "Casein fermentate of Lactobacillus animalis DPC6134 contains a range of novel propeptide angiotensin-converting enzyme inhibitors.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1128\/AEM.00096-07; 10.1016\/j.foodchem.2012.09.092", "pubmedid": "17483275 23194537", "mw": "1860.2", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "0.4882", "instability": "85.78", "hydrophobic": "0.7059", "boman": "-1.4706", "helix": "0.0588", "turn_pct": "0.3529", "sheet": "0.5294" }, { "id": "aceip0730", "seq": "NIPPLTQTPVVVPPFIQPEVMGVSK", "length": "25", "detail": "Milk (bovine)", "source": "Milk", "ic50": null, "reference": "Casein fermentate of Lactobacillus animalis DPC6134 contains a range of novel propeptide angiotensin-converting enzyme inhibitors.", "doi": "10.1128\/AEM.00096-07", "pubmedid": "17483275", "mw": "2688.19", "pi": "6.0", "charge_ph7": "-0.24", "gravy": "0.336", "instability": "76.18", "hydrophobic": "0.64", "boman": "-1.2924", "helix": "0.16", "turn_pct": "0.36", "sheet": "0.44" }, { "id": "aceip0731", "seq": "NK", "length": "2", "detail": "Food-protein | Soybean | Chicken", "source": "Synthesized | Legume | Chicken", "ic50": "810 μM", "reference": "Peptides with angiotensin I converting enzyme (ACE) inhibitory activity generated from porcine skeletal muscle proteins by the action of meat-borne Lactobacillus.", "doi": "10.1016\/j.jprot.2013.06.023", "pubmedid": "23806758", "mw": "260.29", "pi": "8.75", "charge_ph7": "0.76", "gravy": "-3.7", "instability": "123.4", "hydrophobic": "0.0", "boman": "1.6", "helix": "0.5", "turn_pct": "0.5", "sheet": "0.0" }, { "id": "aceip0732", "seq": "NLAPFL", "length": "6", "detail": "Cereals (Maize)", "source": "Cereal", "ic50": null, "reference": "Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1080\/10408398.2012.664829", "pubmedid": "24915368", "mw": "673.8", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "1.1833", "instability": "72.53", "hydrophobic": "0.8333", "boman": "-2.1683", "helix": "0.5", "turn_pct": "0.3333", "sheet": "0.5" }, { "id": "aceip0733", "seq": "NLDTDI", "length": "6", "detail": "Milk | Amaranth | Cereals (Maize) | Maize", "source": "Milk | Plants | Cereal", "ic50": null, "reference": "Release of angiotensin I-converting enzyme inhibitory peptides from flaxseed (Linum usitatissimum L.) protein under simulated gastrointestinal digestion.", "doi": "10.1021\/jf202000e", "pubmedid": "21776963", "mw": "689.71", "pi": "4.05", "charge_ph7": "-2.24", "gravy": "-0.4833", "instability": "-16.72", "hydrophobic": "0.3333", "boman": "-0.7667", "helix": "0.1667", "turn_pct": "0.5", "sheet": "0.5" }, { "id": "aceip0734", "seq": "NLDTDL", "length": "6", "detail": "Milk (bovine)", "source": "Milk", "ic50": null, "reference": "Release of angiotensin I-converting enzyme inhibitory peptides from flaxseed (Linum usitatissimum L.) protein under simulated gastrointestinal digestion.", "doi": "10.1021\/jf202000e", "pubmedid": "21776963", "mw": "689.71", "pi": "4.05", "charge_ph7": "-2.24", "gravy": "-0.6", "instability": "-16.72", "hydrophobic": "0.3333", "boman": "-0.7667", "helix": "0.3333", "turn_pct": "0.5", "sheet": "0.5" }, { "id": "aceip0735", "seq": "NLHLP", "length": "5", "detail": "Casein", "source": "Milk", "ic50": "420 μM", "reference": "Inhibition of angiotensin-converting enzyme by synthetic peptide fragments of various beta-caseins.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "1368548 23194537", "mw": "592.69", "pi": "6.74", "charge_ph7": "-0.15", "gravy": "-0.14", "instability": "46.52", "hydrophobic": "0.6", "boman": "-1.446", "helix": "0.4", "turn_pct": "0.4", "sheet": "0.4" }, { "id": "aceip0736", "seq": "NLHLPLP", "length": "7", "detail": "Oat", "source": "Cereal", "ic50": "51 μM", "reference": "Inhibition of angiotensin-converting enzyme by synthetic peptide fragments of various beta-caseins.", "doi": "", "pubmedid": "1368548", "mw": "802.96", "pi": "6.74", "charge_ph7": "-0.15", "gravy": "0.2143", "instability": "63.6", "hydrophobic": "0.7143", "boman": "-1.7357", "helix": "0.4286", "turn_pct": "0.4286", "sheet": "0.4286" }, { "id": "aceip0737", "seq": "NLHLPLPLL", "length": "9", "detail": "Milk (whey) | Milk (Digested milk products)", "source": "Milk", "ic50": "15 μM", "reference": "Identification of angiotensin-I-converting enzyme inhibitory peptides derived from sodium caseinate hydrolysates produced by Lactobacillus helveticus NCC 2765.", "doi": "10.1021\/jf049510t", "pubmedid": "15537298", "mw": "1029.28", "pi": "6.74", "charge_ph7": "-0.15", "gravy": "1.0111", "instability": "51.69", "hydrophobic": "0.7778", "boman": "-2.4433", "helix": "0.5556", "turn_pct": "0.3333", "sheet": "0.5556" }, { "id": "aceip0738", "seq": "NMAINPSK", "length": "8", "detail": "Milk (whey)", "source": "Milk", "ic50": "60 μM", "reference": "Angiotensin converting enzyme inhibitory peptides derived from food proteins: biochemistry, bioactivity and production.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.2174\/138161207780363068; 10.1016\/j.foodchem.2012.09.092", "pubmedid": "17430180 23194537", "mw": "874.02", "pi": "8.75", "charge_ph7": "0.76", "gravy": "-0.6375", "instability": "44.65", "hydrophobic": "0.5", "boman": "-0.4275", "helix": "0.375", "turn_pct": "0.5", "sheet": "0.125" }, { "id": "aceip0739", "seq": "NNVMLQW", "length": "7", "detail": "ND", "source": "ND", "ic50": "40.74 μM", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "23194537", "mw": "904.04", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "-0.2143", "instability": "55.14", "hydrophobic": "0.5714", "boman": "-1.2914", "helix": "0.2857", "turn_pct": "0.2857", "sheet": "0.4286" }, { "id": "aceip0740", "seq": "NP", "length": "2", "detail": "ND", "source": "ND", "ic50": "<20 mM", "reference": "Angiotensin I-converting enzyme inhibitory activity and insulin secretion stimulative activity of fermented fish sauce.; Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1016\/S1389-1723(03)70138-8; 10.1021\/jf051263l; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "16233562 16448176 23871047", "mw": "229.23", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "-2.55", "instability": "-9.4", "hydrophobic": "0.5", "boman": "0.81", "helix": "0.0", "turn_pct": "1.0", "sheet": "0.0" }, { "id": "aceip0741", "seq": "NPAVVRP", "length": "7", "detail": "ND", "source": "ND", "ic50": "19 μM", "reference": "Inhibition of angiotensin-converting enzyme by synthetic peptide fragments of human kappa-casein.", "doi": "", "pubmedid": "1368540", "mw": "751.87", "pi": "9.75", "charge_ph7": "0.76", "gravy": "-0.1429", "instability": "59.49", "hydrophobic": "0.7143", "boman": "-0.7929", "helix": "0.1429", "turn_pct": "0.4286", "sheet": "0.2857" }, { "id": "aceip0742", "seq": "NPP", "length": "3", "detail": "Soybean", "source": "Legume", "ic50": "<20 mM", "reference": "Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Peptide inhibitors for angiotensin I-converting enzyme from enzymatic hydrolysates of porcine skeletal muscle proteins.", "doi": "10.1021\/jf051263l; 10.1016\/s0309-1740(00)00108-x", "pubmedid": "16448176 22061507", "mw": "326.35", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "-2.2333", "instability": "61.27", "hydrophobic": "0.6667", "boman": "0.54", "helix": "0.0", "turn_pct": "1.0", "sheet": "0.0" }, { "id": "aceip0743", "seq": "NPPHQIYP", "length": "8", "detail": "Meat", "source": "Meat", "ic50": "37 μM", "reference": "Inhibition of angiotensin-converting enzyme by synthetic peptide fragments of various beta-caseins.", "doi": "", "pubmedid": "1368548", "mw": "965.06", "pi": "6.74", "charge_ph7": "-0.15", "gravy": "-1.475", "instability": "44.65", "hydrophobic": "0.5", "boman": "-0.1012", "helix": "0.0", "turn_pct": "0.5", "sheet": "0.25" }, { "id": "aceip0744", "seq": "NRVYVHPF", "length": "8", "detail": "Brazilian lancehead", "source": "Animal", "ic50": "0 μM", "reference": "Spectrophotometric assay and properties of the angiotensin-converting enzyme of rabbit lung.", "doi": "10.1016\/0006-2952(71)90292-9", "pubmedid": "4355305", "mw": "1031.17", "pi": "8.75", "charge_ph7": "0.85", "gravy": "-0.3625", "instability": "19.8", "hydrophobic": "0.5", "boman": "-0.6987", "helix": "0.0", "turn_pct": "0.25", "sheet": "0.5" }, { "id": "aceip0745", "seq": "NSAEER", "length": "6", "detail": "Milk (bovine) | Cheese (Manchego cheese) | Milk (caprine kefir)", "source": "Milk", "ic50": null, "reference": "Hot topic: Changes in angiotensin-converting enzyme inhibition and concentrations of the tripeptides Val-Pro-Pro and Ile-Pro-Pro during ripening of different Swiss cheese varieties.", "doi": "10.3168\/jds.2008-1531", "pubmedid": "19233775", "mw": "704.69", "pi": "4.53", "charge_ph7": "-1.23", "gravy": "-2.3333", "instability": "62.67", "hydrophobic": "0.1667", "boman": "1.1083", "helix": "0.5", "turn_pct": "0.3333", "sheet": "0.0" }, { "id": "aceip0746", "seq": "NVPGEIVESL", "length": "10", "detail": "Synthesized", "source": "Synthesized", "ic50": null, "reference": "Casein fermentate of Lactobacillus animalis DPC6134 contains a range of novel propeptide angiotensin-converting enzyme inhibitors.", "doi": "10.1128\/AEM.00096-07", "pubmedid": "17483275", "mw": "1056.17", "pi": "4.05", "charge_ph7": "-2.23", "gravy": "0.34", "instability": "50.75", "hydrophobic": "0.5", "boman": "-1.312", "helix": "0.3", "turn_pct": "0.4", "sheet": "0.4" }, { "id": "aceip0747", "seq": "NVR", "length": "3", "detail": "Milk", "source": "Milk", "ic50": "382->1000 μM", "reference": "Angiotensin I-converting enzyme inhibitory peptides generated from in vitro gastrointestinal digestion of pork meat.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1021\/jf904204n; 10.1080\/10408398.2012.664829", "pubmedid": "20151679 24915368", "mw": "387.43", "pi": "9.75", "charge_ph7": "0.76", "gravy": "-1.2667", "instability": "6.67", "hydrophobic": "0.3333", "boman": "0.1", "helix": "0.0", "turn_pct": "0.3333", "sheet": "0.3333" }, { "id": "aceip0748", "seq": "NWGPLV", "length": "6", "detail": "ND", "source": "ND", "ic50": "21 μM", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.; Vegetable foods: a cheap source of proteins and peptides with antihypertensive, antioxidant, and other less occurrence bioactivities.", "doi": "10.1016\/j.foodchem.2012.09.092; 10.1016\/j.talanta.2012.12.041", "pubmedid": "23194537 23598136", "mw": "684.78", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "0.2667", "instability": "-26.23", "hydrophobic": "0.6667", "boman": "-1.7683", "helix": "0.1667", "turn_pct": "0.5", "sheet": "0.5" }, { "id": "aceip0749", "seq": "NY", "length": "2", "detail": "Meat", "source": "Meat", "ic50": "<20 mM", "reference": "Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Max-E47, a designed minimalist protein that targets the E-box DNA site in vivo and in vitro.; Vegetable foods: a cheap source of proteins and peptides with antihypertensive, antioxidant, and other less occurrence bioactivities.; Peptides with angiotensin I converting enzyme (ACE) inhibitory activity generated from porcine skeletal muscle proteins by the action of meat-borne Lactobacillus.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1021\/jf051263l; 10.1021\/ja901306q; 10.1016\/j.talanta.2012.12.041; 10.1016\/j.jprot.2013.06.023; 10.1016\/j.foodchem.2013.05.140; 10.1080\/10408398.2012.664829", "pubmedid": "16448176 19449889 23598136 23806758 23871047 24915368", "mw": "295.29", "pi": "5.52", "charge_ph7": "-0.24", "gravy": "-2.4", "instability": "5.0", "hydrophobic": "0.0", "boman": "0.88", "helix": "0.0", "turn_pct": "0.5", "sheet": "0.5" }, { "id": "aceip0750", "seq": "PA", "length": "2", "detail": "Milk (human)", "source": "Milk", "ic50": null, "reference": "Three-dimensional holograph vector of atomic interaction field (3D-HoVAIF): a novel rotation-translation invariant 3D structure descriptor and its applications to peptides.", "doi": "10.1002\/psc.892", "pubmedid": "17654623", "mw": "186.21", "pi": "5.95", "charge_ph7": "-0.04", "gravy": "0.1", "instability": "101.3", "hydrophobic": "1.0", "boman": "-0.905", "helix": "0.5", "turn_pct": "0.5", "sheet": "0.0" }, { "id": "aceip0751", "seq": "PAGPVG", "length": "6", "detail": "Milk (human)", "source": "Milk", "ic50": "382->1000 μM", "reference": "Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1080\/10408398.2012.664829", "pubmedid": "24915368", "mw": "496.56", "pi": "5.95", "charge_ph7": "-0.04", "gravy": "0.3333", "instability": "58.38", "hydrophobic": "0.6667", "boman": "-1.2883", "helix": "0.1667", "turn_pct": "0.6667", "sheet": "0.1667" }, { "id": "aceip0752", "seq": "PAHIAW", "length": "6", "detail": "Milk | Amaranth", "source": "Milk | Plants", "ic50": ">100 μM", "reference": "Potent synthetic analogues of angiotensin-converting enzyme inhibitor derived from Tuna muscle.", "doi": "", "pubmedid": "1368734", "mw": "693.79", "pi": "7.17", "charge_ph7": "0.05", "gravy": "0.4", "instability": "99.52", "hydrophobic": "0.8333", "boman": "-1.6467", "helix": "0.3333", "turn_pct": "0.1667", "sheet": "0.3333" }, { "id": "aceip0753", "seq": "PANIKWGD", "length": "8", "detail": "ND", "source": "ND", "ic50": "21 μM", "reference": "Induction of angiotensin-converting enzyme inhibitory activity by acid-limited proteolysis of glyceraldehyde 3-phosphate dehydrogenase.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/0006-291x(89)92620-x; 10.1016\/j.foodchem.2012.09.092", "pubmedid": "2660788 23194537", "mw": "899.99", "pi": "6.51", "charge_ph7": "-0.04", "gravy": "-0.9375", "instability": "64.18", "hydrophobic": "0.5", "boman": "-0.64", "helix": "0.25", "turn_pct": "0.5", "sheet": "0.25" }, { "id": "aceip0754", "seq": "PANLPWGSSNV", "length": "11", "detail": "Casein", "source": "Milk", "ic50": "18 μM", "reference": "Production of angiotensin-converting enzyme inhibitors from baker's yeast glyceraldehyde-3-phosphate dehydrogenase.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1248\/bpb1978.13.766; 10.1016\/j.foodchem.2012.09.092", "pubmedid": "2098549 23194537", "mw": "1141.23", "pi": "5.95", "charge_ph7": "-0.04", "gravy": "-0.3", "instability": "49.57", "hydrophobic": "0.5455", "boman": "-0.8291", "helix": "0.1818", "turn_pct": "0.6364", "sheet": "0.2727" }, { "id": "aceip0755", "seq": "PAP", "length": "3", "detail": "Soybean | Legume (Pea proteins)", "source": "Legume", "ic50": "87 μM", "reference": "Inhibition of angiotensin-converting enzyme by synthetic peptide fragments of human kappa-casein.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1016\/j.foodchem.2013.05.140", "pubmedid": "1368540 23871047", "mw": "283.32", "pi": "5.95", "charge_ph7": "-0.04", "gravy": "-0.4667", "instability": "135.07", "hydrophobic": "1.0", "boman": "-0.6033", "helix": "0.3333", "turn_pct": "0.6667", "sheet": "0.0" }, { "id": "aceip0756", "seq": "PAVVLP", "length": "6", "detail": "Milk (bovine) | Milk (caprine) | Amaranth | Carp | Cereals (Maize) | Cereals (Buckwheat) | Pork | Chicken | Chicken connectin", "source": "Milk | Plants | Fish | Cereal | Porcine | Chicken", "ic50": "45 μM", "reference": "Inhibition of angiotensin-converting enzyme by synthetic peptide fragments of various beta-caseins.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "1368548 23194537", "mw": "594.74", "pi": "5.95", "charge_ph7": "-0.04", "gravy": "1.8", "instability": "72.53", "hydrophobic": "1.0", "boman": "-2.4683", "helix": "0.3333", "turn_pct": "0.3333", "sheet": "0.5" }, { "id": "aceip0757", "seq": "PAVVRP", "length": "6", "detail": "Pork", "source": "Porcine", "ic50": "18 μM", "reference": "Inhibition of angiotensin-converting enzyme by synthetic peptide fragments of human kappa-casein.", "doi": "", "pubmedid": "1368540", "mw": "637.77", "pi": "10.18", "charge_ph7": "0.96", "gravy": "0.4167", "instability": "72.53", "hydrophobic": "0.8333", "boman": "-1.195", "helix": "0.1667", "turn_pct": "0.3333", "sheet": "0.3333" }, { "id": "aceip0758", "seq": "PCHIAW", "length": "6", "detail": "ND", "source": "ND", "ic50": ">100 μM", "reference": "Potent synthetic analogues of angiotensin-converting enzyme inhibitor derived from Tuna muscle.", "doi": "", "pubmedid": "1368734", "mw": "725.86", "pi": "7.12", "charge_ph7": "0.04", "gravy": "0.5167", "instability": "123.33", "hydrophobic": "0.6667", "boman": "-1.5583", "helix": "0.1667", "turn_pct": "0.1667", "sheet": "0.3333" }, { "id": "aceip0759", "seq": "PDHIAW", "length": "6", "detail": "Milk (bovine) | Cereals | Pork | Chicken", "source": "Milk | Cereal | Porcine | Chicken", "ic50": ">100 μM", "reference": "Potent synthetic analogues of angiotensin-converting enzyme inhibitor derived from Tuna muscle.", "doi": "", "pubmedid": "1368734", "mw": "737.8", "pi": "5.08", "charge_ph7": "-0.95", "gravy": "-0.4833", "instability": "69.0", "hydrophobic": "0.6667", "boman": "-1.065", "helix": "0.1667", "turn_pct": "0.3333", "sheet": "0.3333" }, { "id": "aceip0760", "seq": "PER", "length": "3", "detail": "Pork | Pork blood", "source": "Porcine", "ic50": "382->1000 μM", "reference": "Angiotensin I-converting enzyme inhibitory peptides generated from in vitro gastrointestinal digestion of pork meat.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1021\/jf904204n; 10.1080\/10408398.2012.664829", "pubmedid": "20151679 24915368", "mw": "400.43", "pi": "6.43", "charge_ph7": "-0.04", "gravy": "-3.2", "instability": "64.6", "hydrophobic": "0.3333", "boman": "1.4533", "helix": "0.3333", "turn_pct": "0.3333", "sheet": "0.0" }, { "id": "aceip0761", "seq": "PEW", "length": "3", "detail": "ND", "source": "ND", "ic50": "<10 μM", "reference": "The potential role of milk-derived peptides in cardiovascular disease.", "doi": "10.1039\/c1fo10017c", "pubmedid": "21779574", "mw": "430.45", "pi": "4.05", "charge_ph7": "-1.04", "gravy": "-2.0", "instability": "14.5", "hydrophobic": "0.6667", "boman": "-0.23", "helix": "0.3333", "turn_pct": "0.3333", "sheet": "0.3333" }, { "id": "aceip0762", "seq": "PFAQTQSLVYP", "length": "11", "detail": "Legume (Pea proteins)", "source": "Legume", "ic50": null, "reference": "Inhibition of angiotensin-converting enzyme by synthetic peptide fragments of various beta-caseins.", "doi": "", "pubmedid": "1368548", "mw": "1250.4", "pi": "5.95", "charge_ph7": "-0.04", "gravy": "-0.0364", "instability": "64.05", "hydrophobic": "0.5455", "boman": "-0.89", "helix": "0.1818", "turn_pct": "0.2727", "sheet": "0.4545" }, { "id": "aceip0763", "seq": "PFFDPQIP", "length": "8", "detail": "Cereals (Buckwheat)", "source": "Cereal", "ic50": "0 μM", "reference": "Inhibition of angiotensin-converting enzyme by synthetic peptide fragments of various beta-caseins.", "doi": "", "pubmedid": "1368548", "mw": "960.08", "pi": "4.05", "charge_ph7": "-1.04", "gravy": "-0.2125", "instability": "68.72", "hydrophobic": "0.75", "boman": "-0.98", "helix": "0.0", "turn_pct": "0.5", "sheet": "0.375" }, { "id": "aceip0764", "seq": "PFP", "length": "3", "detail": "ND", "source": "ND", "ic50": "144 μM", "reference": "Quantitative structure-activity relationship study of bitter di- and tri-peptides including relationship with angiotensin I-converting enzyme inhibitory activity.; QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1002\/psc.800; 10.1007\/s00894-010-0862-x; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "17117396 20941517 23871047", "mw": "359.42", "pi": "5.95", "charge_ph7": "-0.04", "gravy": "-0.1333", "instability": "135.07", "hydrophobic": "1.0", "boman": "-0.9933", "helix": "0.0", "turn_pct": "0.6667", "sheet": "0.3333" }, { "id": "aceip0765", "seq": "PG", "length": "2", "detail": "Milk (bovine) | Synthesized | Fish (Alaska pollack) | pea", "source": "Milk | Synthesized | Fish | Legume", "ic50": "<20 mM", "reference": "Binding of peptide substrates and inhibitors of angiotensin-converting enzyme. Importance of the COOH-terminal dipeptide sequence.; Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Three-dimensional holograph vector of atomic interaction field (3D-HoVAIF): a novel rotation-translation invariant 3D structure descriptor and its applications to peptides.; QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.; Peptides with angiotensin I converting enzyme (ACE) inhibitory activity generated from porcine skeletal muscle proteins by the action of meat-borne Lactobacillus.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1021\/jf051263l; 10.1002\/psc.892; 10.1007\/s00894-010-0862-x; 10.1016\/j.jprot.2013.06.023; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "6243277 16448176 17654623 20941517 23806758 23871047", "mw": "172.18", "pi": "5.95", "charge_ph7": "-0.04", "gravy": "-1.0", "instability": "5.0", "hydrophobic": "0.5", "boman": "-0.47", "helix": "0.0", "turn_pct": "1.0", "sheet": "0.0" }, { "id": "aceip0766", "seq": "PGG", "length": "3", "detail": "Fish (Skate)", "source": "Fish", "ic50": null, "reference": "Quantitative structure-activity relationship study of bitter di- and tri-peptides including relationship with angiotensin I-converting enzyme inhibitory activity.; QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.", "doi": "10.1002\/psc.800; 10.1007\/s00894-010-0862-x", "pubmedid": "17117396 20941517", "mw": "229.23", "pi": "5.95", "charge_ph7": "-0.04", "gravy": "-0.8", "instability": "47.8", "hydrophobic": "0.3333", "boman": "-0.6267", "helix": "0.0", "turn_pct": "1.0", "sheet": "0.0" }, { "id": "aceip0767", "seq": "PGI", "length": "3", "detail": "Milk (Casein)", "source": "Milk", "ic50": null, "reference": "Quantitative structure-activity relationship study of bitter di- and tri-peptides including relationship with angiotensin I-converting enzyme inhibitory activity.; QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1002\/psc.800; 10.1007\/s00894-010-0862-x; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "17117396 20941517 23871047", "mw": "285.34", "pi": "5.95", "charge_ph7": "-0.04", "gravy": "0.8333", "instability": "-21.63", "hydrophobic": "0.6667", "boman": "-1.9533", "helix": "0.0", "turn_pct": "0.6667", "sheet": "0.3333" }, { "id": "aceip0768", "seq": "PGL", "length": "3", "detail": "Pork", "source": "Porcine", "ic50": "13.93 μM", "reference": "Structure and activity of angiotensin I converting enzyme inhibitory peptides derived from Alaskan pollack skin.", "doi": "10.5483\/bmbrep.2002.35.2.239", "pubmedid": "12297036", "mw": "285.34", "pi": "5.95", "charge_ph7": "-0.04", "gravy": "0.6", "instability": "6.67", "hydrophobic": "0.6667", "boman": "-1.9533", "helix": "0.3333", "turn_pct": "0.6667", "sheet": "0.3333" }, { "id": "aceip0769", "seq": "PGP", "length": "3", "detail": "Milk (bovine)", "source": "Milk", "ic50": null, "reference": "Quantitative structure-activity relationship study of bitter di- and tri-peptides including relationship with angiotensin I-converting enzyme inhibitory activity.; QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1002\/psc.800; 10.1007\/s00894-010-0862-x; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "17117396 20941517 23871047", "mw": "269.3", "pi": "5.95", "charge_ph7": "-0.04", "gravy": "-1.2", "instability": "6.67", "hydrophobic": "0.6667", "boman": "-0.3133", "helix": "0.0", "turn_pct": "1.0", "sheet": "0.0" }, { "id": "aceip0770", "seq": "PGPIHN", "length": "6", "detail": "Milk (Casein)", "source": "Milk", "ic50": null, "reference": "Enterococcus faecalis strains from food, environmental, and clinical origin produce ACE-inhibitory peptides and other bioactive peptides during growth in bovine skim milk.", "doi": "10.1016\/j.ijfoodmicro.2013.06.019", "pubmedid": "23845432", "mw": "633.7", "pi": "7.17", "charge_ph7": "0.05", "gravy": "-0.9667", "instability": "68.37", "hydrophobic": "0.5", "boman": "-0.5417", "helix": "0.0", "turn_pct": "0.6667", "sheet": "0.1667" }, { "id": "aceip0771", "seq": "PGPIP", "length": "5", "detail": "Casein", "source": "Milk", "ic50": "0 0", "reference": "Putting microbes to work: dairy fermentation, cell factories and bioactive peptides. Part I: overview.", "doi": "10.1002\/biot.200600246", "pubmedid": "17407210", "mw": "479.57", "pi": "5.95", "charge_ph7": "-0.04", "gravy": "-0.14", "instability": "2.24", "hydrophobic": "0.8", "boman": "-1.172", "helix": "0.0", "turn_pct": "0.8", "sheet": "0.2" }, { "id": "aceip0772", "seq": "PGPLGLTGP", "length": "9", "detail": "Meat", "source": "Meat", "ic50": "0.21 mg\/ml", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.; Review on the angiotensin-I-converting enzyme (ACE) inhibitor peptides from marine proteins.", "doi": "10.1016\/j.foodchem.2012.09.092; 10.1007\/s12010-012-0024-y", "pubmedid": "23194537 23271625", "mw": "807.93", "pi": "5.95", "charge_ph7": "-0.04", "gravy": "0.1", "instability": "-0.54", "hydrophobic": "0.5556", "boman": "-1.3778", "helix": "0.2222", "turn_pct": "0.6667", "sheet": "0.3333" }, { "id": "aceip0773", "seq": "PGR", "length": "3", "detail": "ND", "source": "ND", "ic50": "382->1000 μM", "reference": "Quantitative structure-activity relationship study of bitter di- and tri-peptides including relationship with angiotensin I-converting enzyme inhibitory activity.; Angiotensin I-converting enzyme inhibitory peptides generated from in vitro gastrointestinal digestion of pork meat.; QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1002\/psc.800; 10.1021\/jf904204n; 10.1007\/s00894-010-0862-x; 10.1016\/j.foodchem.2013.05.140; 10.1080\/10408398.2012.664829", "pubmedid": "17117396 20151679 20941517 23871047 24915368", "mw": "328.37", "pi": "10.18", "charge_ph7": "0.96", "gravy": "-2.1667", "instability": "6.67", "hydrophobic": "0.3333", "boman": "0.5933", "helix": "0.0", "turn_pct": "0.6667", "sheet": "0.0" }, { "id": "aceip0774", "seq": "PGTAVFK", "length": "7", "detail": "Milk (bovine) | Milk (human)", "source": "Milk", "ic50": "26.5 μM", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "23194537", "mw": "718.84", "pi": "9.18", "charge_ph7": "0.96", "gravy": "0.3143", "instability": "-25.03", "hydrophobic": "0.5714", "boman": "-1.1329", "helix": "0.2857", "turn_pct": "0.2857", "sheet": "0.4286" }, { "id": "aceip0775", "seq": "PH", "length": "2", "detail": "Milk (Casein)", "source": "Milk", "ic50": "0 0", "reference": "Application of at-line two-dimensional liquid chromatography-mass spectrometry for identification of small hydrophilic angiotensin I-inhibiting peptides in milk hydrolysates.; Peptides with angiotensin I converting enzyme (ACE) inhibitory activity generated from porcine skeletal muscle proteins by the action of meat-borne Lactobacillus.", "doi": "10.1007\/s00216-008-1990-3; 10.1016\/j.jprot.2013.06.023", "pubmedid": "18392815 23806758", "mw": "252.27", "pi": "7.17", "charge_ph7": "0.05", "gravy": "-2.4", "instability": "5.0", "hydrophobic": "0.5", "boman": "0.495", "helix": "0.0", "turn_pct": "0.5", "sheet": "0.0" }, { "id": "aceip0776", "seq": "PHQIYP", "length": "6", "detail": "Milk (Casein)", "source": "Milk", "ic50": "30 μM", "reference": "Inhibition of angiotensin-converting enzyme by synthetic peptide fragments of various beta-caseins.", "doi": "", "pubmedid": "1368548", "mw": "753.84", "pi": "7.17", "charge_ph7": "0.04", "gravy": "-1.1167", "instability": "28.9", "hydrophobic": "0.5", "boman": "-0.405", "helix": "0.0", "turn_pct": "0.3333", "sheet": "0.3333" }, { "id": "aceip0777", "seq": "PI", "length": "2", "detail": "Milk (Casein)", "source": "Milk", "ic50": null, "reference": "Three-dimensional holograph vector of atomic interaction field (3D-HoVAIF): a novel rotation-translation invariant 3D structure descriptor and its applications to peptides.", "doi": "10.1002\/psc.892", "pubmedid": "17654623", "mw": "228.29", "pi": "5.95", "charge_ph7": "-0.04", "gravy": "1.45", "instability": "5.0", "hydrophobic": "1.0", "boman": "-2.46", "helix": "0.0", "turn_pct": "0.5", "sheet": "0.5" }, { "id": "aceip0778", "seq": "PIP", "length": "3", "detail": "Milk (bovine) | Casein | Milk (human) | Milk (Fermented Milk) | Enterococcus faecalis", "source": "Milk | Bacteria", "ic50": null, "reference": "Quantitative structure-activity relationship study of bitter di- and tri-peptides including relationship with angiotensin I-converting enzyme inhibitory activity.; QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1002\/psc.800; 10.1007\/s00894-010-0862-x; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "17117396 20941517 23871047", "mw": "325.4", "pi": "5.95", "charge_ph7": "-0.04", "gravy": "0.4333", "instability": "-2.93", "hydrophobic": "1.0", "boman": "-1.64", "helix": "0.0", "turn_pct": "0.6667", "sheet": "0.3333" }, { "id": "aceip0779", "seq": "PK", "length": "2", "detail": "Milk (bovine) | Casein | Milk (Fermented Milk) | Milk (Goat milk protein) | Enterococcus faecalis", "source": "Milk | Bacteria", "ic50": null, "reference": "Quantitative structure-activity relationship study of bitter di- and tri-peptides including relationship with angiotensin I-converting enzyme inhibitory activity.", "doi": "10.1002\/psc.800", "pubmedid": "17117396", "mw": "243.3", "pi": "9.18", "charge_ph7": "0.96", "gravy": "-2.75", "instability": "5.0", "hydrophobic": "0.5", "boman": "0.79", "helix": "0.5", "turn_pct": "0.5", "sheet": "0.0" }, { "id": "aceip0780", "seq": "PKAIP", "length": "5", "detail": "Milk (bovine) | Milk (Casein)", "source": "Milk", "ic50": "592.2 μM", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "23194537", "mw": "524.65", "pi": "9.18", "charge_ph7": "0.96", "gravy": "-0.16", "instability": "2.24", "hydrophobic": "0.8", "boman": "-1.03", "helix": "0.4", "turn_pct": "0.4", "sheet": "0.2" }, { "id": "aceip0781", "seq": "PKDLREN", "length": "7", "detail": "Milk (Casein)", "source": "Milk", "ic50": "9.82 μM", "reference": "Identification of angiotensin I-converting enzyme inhibitory peptides from koumiss, a traditional fermented mare's milk.", "doi": "10.3168\/jds.2009-2672", "pubmedid": "20172208", "mw": "870.95", "pi": "6.49", "charge_ph7": "-0.04", "gravy": "-2.3857", "instability": "36.09", "hydrophobic": "0.2857", "boman": "0.6171", "helix": "0.4286", "turn_pct": "0.4286", "sheet": "0.1429" }, { "id": "aceip0782", "seq": "PKHKEMPFPPKYPVEPFT", "length": "18", "detail": "Legume (Pea proteins)", "source": "Legume", "ic50": "0 0", "reference": "Putting microbes to work: dairy fermentation, cell factories and bioactive peptides. Part I: overview.; The potential role of milk-derived peptides in cardiovascular disease.", "doi": "10.1002\/biot.200600246; 10.1039\/c1fo10017c", "pubmedid": "17407210 21779574", "mw": "2169.54", "pi": "8.83", "charge_ph7": "1.05", "gravy": "-1.2111", "instability": "118.07", "hydrophobic": "0.5556", "boman": "-0.1633", "helix": "0.3333", "turn_pct": "0.3333", "sheet": "0.2778" }, { "id": "aceip0783", "seq": "PL", "length": "2", "detail": "Milk (Casein)", "source": "Milk", "ic50": "337.32 μM", "reference": "Structure and activity of angiotensin I converting enzyme inhibitory peptides derived from Alaskan pollack skin.; Three-dimensional holograph vector of atomic interaction field (3D-HoVAIF): a novel rotation-translation invariant 3D structure descriptor and its applications to peptides.; Peptides with angiotensin I converting enzyme (ACE) inhibitory activity generated from porcine skeletal muscle proteins by the action of meat-borne Lactobacillus.", "doi": "10.5483\/bmbrep.2002.35.2.239; 10.1002\/psc.892; 10.1016\/j.jprot.2013.06.023", "pubmedid": "12297036 17654623 23806758", "mw": "228.29", "pi": "5.95", "charge_ph7": "-0.04", "gravy": "1.1", "instability": "5.0", "hydrophobic": "1.0", "boman": "-2.46", "helix": "0.5", "turn_pct": "0.5", "sheet": "0.5" }, { "id": "aceip0784", "seq": "PLG", "length": "3", "detail": "Milk (Casein)", "source": "Milk", "ic50": "4.74 μM", "reference": "Structure and activity of angiotensin I converting enzyme inhibitory peptides derived from Alaskan pollack skin.", "doi": "10.5483\/bmbrep.2002.35.2.239", "pubmedid": "12297036", "mw": "285.34", "pi": "5.95", "charge_ph7": "-0.04", "gravy": "0.6", "instability": "6.67", "hydrophobic": "0.6667", "boman": "-1.9533", "helix": "0.3333", "turn_pct": "0.6667", "sheet": "0.3333" }, { "id": "aceip0785", "seq": "PLIYP", "length": "5", "detail": "Milk (Casein)", "source": "Milk", "ic50": "4.4 μM", "reference": "Inhibition of angiotensin-converting enzyme by synthetic peptide fragments of various beta-caseins.; The potential role of milk-derived peptides in cardiovascular disease.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1039\/c1fo10017c; 10.1016\/j.foodchem.2012.09.092", "pubmedid": "1368548 21779574 23194537", "mw": "601.73", "pi": "5.95", "charge_ph7": "-0.04", "gravy": "0.76", "instability": "32.68", "hydrophobic": "0.8", "boman": "-1.94", "helix": "0.2", "turn_pct": "0.4", "sheet": "0.6" }, { "id": "aceip0786", "seq": "PLP", "length": "3", "detail": "Soybean | Shrimp", "source": "Legume | Shrimp", "ic50": "430 μM", "reference": "Bioactive peptides in amaranth (Amaranthus hypochondriacus) seed.; Peptides with angiotensin I converting enzyme (ACE) inhibitory activity generated from porcine skeletal muscle proteins by the action of meat-borne Lactobacillus.", "doi": "10.1021\/jf072911z; 10.1016\/j.jprot.2013.06.023", "pubmedid": "18211015 23806758", "mw": "325.4", "pi": "5.95", "charge_ph7": "-0.04", "gravy": "0.2", "instability": "70.87", "hydrophobic": "1.0", "boman": "-1.64", "helix": "0.3333", "turn_pct": "0.6667", "sheet": "0.3333" }, { "id": "aceip0787", "seq": "PLPLL", "length": "5", "detail": "Meat", "source": "Meat", "ic50": "0.25 mg\/ml", "reference": "The potential role of milk-derived peptides in cardiovascular disease.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1039\/c1fo10017c; 10.1080\/10408398.2012.664829", "pubmedid": "21779574 24915368", "mw": "551.72", "pi": "5.95", "charge_ph7": "-0.04", "gravy": "1.64", "instability": "46.52", "hydrophobic": "1.0", "boman": "-2.952", "helix": "0.6", "turn_pct": "0.4", "sheet": "0.6" }, { "id": "aceip0788", "seq": "PLW", "length": "3", "detail": "Milk (bovine)", "source": "Milk", "ic50": "<20 mM", "reference": "Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.", "doi": "10.1021\/jf051263l", "pubmedid": "16448176", "mw": "414.5", "pi": "5.95", "charge_ph7": "-0.04", "gravy": "0.4333", "instability": "85.6", "hydrophobic": "1.0", "boman": "-2.4167", "helix": "0.3333", "turn_pct": "0.3333", "sheet": "0.6667" }, { "id": "aceip0789", "seq": "PNSHP", "length": "5", "detail": "ND", "source": "ND", "ic50": "1001 μM", "reference": "Inhibition of angiotensin-converting enzyme by synthetic peptide fragments of human kappa-casein.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "1368540 23194537", "mw": "550.56", "pi": "7.17", "charge_ph7": "0.05", "gravy": "-2.14", "instability": "2.24", "hydrophobic": "0.4", "boman": "0.69", "helix": "0.0", "turn_pct": "0.8", "sheet": "0.0" }, { "id": "aceip0790", "seq": "PP", "length": "2", "detail": "Wine", "source": "Cereal", "ic50": "0 0", "reference": "Quantitative structure-activity relationship study of bitter di- and tri-peptides including relationship with angiotensin I-converting enzyme inhibitory activity.; Application of at-line two-dimensional liquid chromatography-mass spectrometry for identification of small hydrophilic angiotensin I-inhibiting peptides in milk hydrolysates.; Peptides with angiotensin I converting enzyme (ACE) inhibitory activity generated from porcine skeletal muscle proteins by the action of meat-borne Lactobacillus.", "doi": "10.1002\/psc.800; 10.1007\/s00216-008-1990-3; 10.1016\/j.jprot.2013.06.023", "pubmedid": "17117396 18392815 23806758", "mw": "212.25", "pi": "5.95", "charge_ph7": "-0.04", "gravy": "-1.6", "instability": "101.3", "hydrophobic": "1.0", "boman": "0.0", "helix": "0.0", "turn_pct": "1.0", "sheet": "0.0" }, { "id": "aceip0791", "seq": "PPEIN", "length": "5", "detail": "Cereals (Maize)", "source": "Cereal", "ic50": "0.29 mg\/ml", "reference": "The potential role of milk-derived peptides in cardiovascular disease.", "doi": "10.1039\/c1fo10017c", "pubmedid": "21779574", "mw": "568.62", "pi": "4.05", "charge_ph7": "-1.04", "gravy": "-1.14", "instability": "119.8", "hydrophobic": "0.6", "boman": "-0.332", "helix": "0.2", "turn_pct": "0.6", "sheet": "0.2" }, { "id": "aceip0792", "seq": "PPF", "length": "3", "detail": "ND", "source": "ND", "ic50": null, "reference": "Quantitative structure-activity relationship study of bitter di- and tri-peptides including relationship with angiotensin I-converting enzyme inhibitory activity.; QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1002\/psc.800; 10.1007\/s00894-010-0862-x; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "17117396 20941517 23871047", "mw": "359.42", "pi": "5.95", "charge_ph7": "-0.04", "gravy": "-0.1333", "instability": "135.07", "hydrophobic": "1.0", "boman": "-0.9933", "helix": "0.0", "turn_pct": "0.6667", "sheet": "0.3333" }, { "id": "aceip0793", "seq": "PPG", "length": "3", "detail": "Synthesized | Human", "source": "Synthesized | Human", "ic50": null, "reference": "Quantitative structure-activity relationship study of bitter di- and tri-peptides including relationship with angiotensin I-converting enzyme inhibitory activity.; QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1002\/psc.800; 10.1007\/s00894-010-0862-x; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "17117396 20941517 23871047", "mw": "269.3", "pi": "5.95", "charge_ph7": "-0.04", "gravy": "-1.2", "instability": "70.87", "hydrophobic": "0.6667", "boman": "-0.3133", "helix": "0.0", "turn_pct": "1.0", "sheet": "0.0" }, { "id": "aceip0794", "seq": "PPK", "length": "3", "detail": "Milk (human)", "source": "Milk", "ic50": "<20 mM", "reference": "Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Angiotensin-I converting enzyme inhibitory peptide derived from porcine skeletal muscle myosin and its antihypertensive activity in spontaneously hypertensive rats.", "doi": "10.1021\/jf051263l; 10.1111\/j.1750-3841.2007.00571.x", "pubmedid": "16448176 18034756", "mw": "340.42", "pi": "9.18", "charge_ph7": "0.96", "gravy": "-2.3667", "instability": "70.87", "hydrophobic": "0.6667", "boman": "0.5267", "helix": "0.3333", "turn_pct": "0.6667", "sheet": "0.0" }, { "id": "aceip0795", "seq": "PPL", "length": "3", "detail": "Food-protein | Carp | Creatine kinase | Cereals | Chicken", "source": "Synthesized | Fish | Cereal | Chicken", "ic50": ">1000 μM", "reference": "Ala-Val-Phe and Val-Phe: ACE inhibitory peptides derived from insect protein with antihypertensive activity in spontaneously hypertensive rats.", "doi": "10.1016\/j.peptides.2009.05.029", "pubmedid": "19524628", "mw": "325.4", "pi": "5.95", "charge_ph7": "-0.04", "gravy": "0.2", "instability": "70.87", "hydrophobic": "1.0", "boman": "-1.64", "helix": "0.3333", "turn_pct": "0.6667", "sheet": "0.3333" }, { "id": "aceip0796", "seq": "PPP", "length": "3", "detail": "Fish", "source": "Fish", "ic50": null, "reference": "Quantitative structure-activity relationship study of bitter di- and tri-peptides including relationship with angiotensin I-converting enzyme inhibitory activity.; QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1002\/psc.800; 10.1007\/s00894-010-0862-x; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "17117396 20941517 23871047", "mw": "309.36", "pi": "5.95", "charge_ph7": "-0.04", "gravy": "-1.6", "instability": "135.07", "hydrophobic": "1.0", "boman": "0.0", "helix": "0.0", "turn_pct": "1.0", "sheet": "0.0" }, { "id": "aceip0797", "seq": "PPPVHL", "length": "6", "detail": "ND", "source": "ND", "ic50": "0 μM", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "23194537", "mw": "658.79", "pi": "7.17", "charge_ph7": "0.05", "gravy": "0.0", "instability": "104.63", "hydrophobic": "0.8333", "boman": "-1.3283", "helix": "0.1667", "turn_pct": "0.5", "sheet": "0.3333" }, { "id": "aceip0798", "seq": "PPQSVLSLSQSKVLPVPQ", "length": "18", "detail": "Meat", "source": "Meat", "ic50": "25 mM\/L", "reference": "Antihypertensive effect of the peptides derived from casein by an extracellular proteinase from Lactobacillus helveticus CP790.", "doi": "10.3168\/jds.S0022-0302(94)77026-0", "pubmedid": "8201050", "mw": "1904.21", "pi": "9.18", "charge_ph7": "0.96", "gravy": "0.0", "instability": "128.45", "hydrophobic": "0.5556", "boman": "-0.9922", "helix": "0.2222", "turn_pct": "0.4444", "sheet": "0.3333" }, { "id": "aceip0799", "seq": "PQ", "length": "2", "detail": "Meat", "source": "Meat", "ic50": "0 0", "reference": "Application of at-line two-dimensional liquid chromatography-mass spectrometry for identification of small hydrophilic angiotensin I-inhibiting peptides in milk hydrolysates.; Peptides with angiotensin I converting enzyme (ACE) inhibitory activity generated from porcine skeletal muscle proteins by the action of meat-borne Lactobacillus.", "doi": "10.1007\/s00216-008-1990-3; 10.1016\/j.jprot.2013.06.023", "pubmedid": "18392815 23806758", "mw": "243.26", "pi": "5.95", "charge_ph7": "-0.04", "gravy": "-2.55", "instability": "101.3", "hydrophobic": "0.5", "boman": "0.68", "helix": "0.0", "turn_pct": "0.5", "sheet": "0.0" }, { "id": "aceip0800", "seq": "PQAFP", "length": "5", "detail": "Milk (caprine)", "source": "Milk", "ic50": "585 μM", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "23194537", "mw": "558.63", "pi": "5.95", "charge_ph7": "-0.04", "gravy": "-0.42", "instability": "85.04", "hydrophobic": "0.8", "boman": "-0.686", "helix": "0.2", "turn_pct": "0.4", "sheet": "0.2" }, { "id": "aceip0801", "seq": "PQEVLP", "length": "6", "detail": "Cheese (Manchego cheese) | Milk-Cheese (Sheep milk and cheeses proteins)", "source": "Milk", "ic50": "800 μM", "reference": "Inhibition of angiotensin-converting enzyme by synthetic peptide fragments of various beta-caseins.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "1368548 23194537", "mw": "681.78", "pi": "4.05", "charge_ph7": "-1.04", "gravy": "-0.3667", "instability": "104.63", "hydrophobic": "0.6667", "boman": "-0.9933", "helix": "0.3333", "turn_pct": "0.3333", "sheet": "0.3333" }, { "id": "aceip0802", "seq": "PQNILP", "length": "6", "detail": "Milk (bovine)", "source": "Milk", "ic50": "177.33 μM", "reference": "Inhibition of angiotensin-converting enzyme by synthetic peptide fragments of various beta-caseins.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "1368548 23194537", "mw": "680.79", "pi": "5.95", "charge_ph7": "-0.04", "gravy": "-0.3167", "instability": "177.87", "hydrophobic": "0.6667", "boman": "-1.1433", "helix": "0.1667", "turn_pct": "0.5", "sheet": "0.3333" }, { "id": "aceip0803", "seq": "PQPIP", "length": "5", "detail": "Sardine | Carp", "source": "Fish", "ic50": "340 μM", "reference": "Inhibition of angiotensin-converting enzyme by synthetic peptide fragments of various beta-caseins.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "1368548 23194537", "mw": "550.65", "pi": "5.95", "charge_ph7": "-0.04", "gravy": "-0.76", "instability": "79.28", "hydrophobic": "0.8", "boman": "-0.712", "helix": "0.0", "turn_pct": "0.6", "sheet": "0.2" }, { "id": "aceip0804", "seq": "PQPLIYP", "length": "7", "detail": "Milk | Meat", "source": "Milk | Meat", "ic50": "3 μM", "reference": "Inhibition of angiotensin-converting enzyme by synthetic peptide fragments of various beta-caseins.", "doi": "", "pubmedid": "1368548", "mw": "826.98", "pi": "5.95", "charge_ph7": "-0.04", "gravy": "-0.1857", "instability": "81.23", "hydrophobic": "0.7143", "boman": "-1.1914", "helix": "0.1429", "turn_pct": "0.4286", "sheet": "0.4286" }, { "id": "aceip0805", "seq": "PQR", "length": "3", "detail": "Milk | Synthesized | Food-protein | Bonito | Fish | Aldolase | Cereals | Oat | Soybean | pea | Chicken | Egg (Ovotransferrin) | Meat", "source": "Milk | Synthesized | Fish | Cereal | Legume | Chicken | Egg | Meat", "ic50": "401 μM", "reference": "Bioactive peptides in amaranth (Amaranthus hypochondriacus) seed.; Evaluation of the allergenicity of goat milk, cow milk, and their lactosera in a guinea pig model.", "doi": "10.1021\/jf072911z; 10.3168\/jds.2008-1125", "pubmedid": "18211015 19233776", "mw": "399.45", "pi": "10.18", "charge_ph7": "0.96", "gravy": "-3.2", "instability": "70.87", "hydrophobic": "0.3333", "boman": "1.36", "helix": "0.0", "turn_pct": "0.3333", "sheet": "0.0" }, { "id": "aceip0806", "seq": "PQRDMP", "length": "6", "detail": "ND", "source": "ND", "ic50": null, "reference": "Enterococcus faecalis strains from food, environmental, and clinical origin produce ACE-inhibitory peptides and other bioactive peptides during growth in bovine skim milk.", "doi": "10.1016\/j.ijfoodmicro.2013.06.019", "pubmedid": "23845432", "mw": "742.84", "pi": "6.27", "charge_ph7": "-0.04", "gravy": "-2.1333", "instability": "113.67", "hydrophobic": "0.5", "boman": "0.5683", "helix": "0.1667", "turn_pct": "0.5", "sheet": "0.0" }, { "id": "aceip0807", "seq": "PQTLALP", "length": "7", "detail": "Egg (Ovalbumin)", "source": "Egg", "ic50": "110 μM", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "23194537", "mw": "738.87", "pi": "5.95", "charge_ph7": "-0.04", "gravy": "0.2857", "instability": "63.6", "hydrophobic": "0.7143", "boman": "-1.4329", "helix": "0.4286", "turn_pct": "0.2857", "sheet": "0.4286" }, { "id": "aceip0808", "seq": "PR", "length": "2", "detail": "ND", "source": "ND", "ic50": "<20 mM", "reference": "Structure and activity of angiotensin I converting enzyme inhibitory peptides from sake and sake lees.; Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Quantitative structure-activity relationship study of bitter di- and tri-peptides including relationship with angiotensin I-converting enzyme inhibitory activity.; Bioactive peptides in amaranth (Amaranthus hypochondriacus) seed.", "doi": "10.1271\/bbb.58.1767; 10.1021\/jf051263l; 10.1002\/psc.800; 10.1021\/jf072911z", "pubmedid": "7765503 16448176 17117396 18211015", "mw": "271.32", "pi": "10.18", "charge_ph7": "0.96", "gravy": "-3.05", "instability": "-32.7", "hydrophobic": "0.5", "boman": "1.36", "helix": "0.0", "turn_pct": "0.5", "sheet": "0.0" }, { "id": "aceip0809", "seq": "PRHQG", "length": "5", "detail": "Bonito | Fish | Aldolase", "source": "Fish", "ic50": "20.67 μM", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "23194537", "mw": "593.64", "pi": "10.18", "charge_ph7": "1.05", "gravy": "-2.64", "instability": "31.44", "hydrophobic": "0.2", "boman": "0.826", "helix": "0.0", "turn_pct": "0.4", "sheet": "0.0" }, { "id": "aceip0810", "seq": "PRY", "length": "3", "detail": "Milk (caprine)", "source": "Milk", "ic50": "<20 mM", "reference": "Structure and activity of angiotensin I converting enzyme inhibitory peptides from sake and sake lees.; Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Bioactive peptides in amaranth (Amaranthus hypochondriacus) seed.", "doi": "10.1271\/bbb.58.1767; 10.1021\/jf051263l; 10.1021\/jf072911z", "pubmedid": "7765503 16448176 18211015", "mw": "434.49", "pi": "9.18", "charge_ph7": "0.96", "gravy": "-2.4667", "instability": "-43.6", "hydrophobic": "0.3333", "boman": "0.9533", "helix": "0.0", "turn_pct": "0.3333", "sheet": "0.3333" }, { "id": "aceip0811", "seq": "PSFQP", "length": "5", "detail": "Milk (whey)", "source": "Milk", "ic50": "73 μM", "reference": "Inhibition of angiotensin-converting enzyme by synthetic peptide fragments of various beta-caseins.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "1368548 23194537", "mw": "574.63", "pi": "5.95", "charge_ph7": "-0.04", "gravy": "-0.94", "instability": "85.04", "hydrophobic": "0.6", "boman": "-0.156", "helix": "0.0", "turn_pct": "0.6", "sheet": "0.2" }, { "id": "aceip0812", "seq": "PSFQPQPLIYP", "length": "11", "detail": "Soybean", "source": "Legume", "ic50": "2.7 μM", "reference": "Inhibition of angiotensin-converting enzyme by synthetic peptide fragments of various beta-caseins.", "doi": "", "pubmedid": "1368548", "mw": "1286.47", "pi": "5.95", "charge_ph7": "-0.04", "gravy": "-0.4", "instability": "90.35", "hydrophobic": "0.6364", "boman": "-0.8291", "helix": "0.0909", "turn_pct": "0.4545", "sheet": "0.3636" }, { "id": "aceip0813", "seq": "PSGQYY", "length": "6", "detail": "Sardine", "source": "Fish", "ic50": "100 μM", "reference": "Angiotensin converting enzyme inhibitory peptides derived from food proteins: biochemistry, bioactivity and production.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.2174\/138161207780363068; 10.1016\/j.foodchem.2012.09.092", "pubmedid": "17430180 23194537", "mw": "713.73", "pi": "5.95", "charge_ph7": "-0.04", "gravy": "-1.4833", "instability": "48.43", "hydrophobic": "0.1667", "boman": "0.2567", "helix": "0.0", "turn_pct": "0.5", "sheet": "0.3333" }, { "id": "aceip0814", "seq": "PSSNK", "length": "5", "detail": "ND", "source": "ND", "ic50": "129 μM", "reference": "Novel angiotensin I-converting enzyme inhibitory peptides derived from edible mushroom Agaricus bisporus (J.E. Lange) Imbach identified by LC-MS\/MS.", "doi": "10.1016\/j.foodchem.2013.10.053", "pubmedid": "24262574", "mw": "531.56", "pi": "9.18", "charge_ph7": "0.96", "gravy": "-2.12", "instability": "132.4", "hydrophobic": "0.2", "boman": "0.976", "helix": "0.2", "turn_pct": "0.8", "sheet": "0.0" }, { "id": "aceip0815", "seq": "PSY", "length": "3", "detail": "Sesame | Antarctic krill", "source": "Plants | Shrimp", "ic50": "<20 mM", "reference": "Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1021\/jf051263l; 10.1080\/10408398.2012.664829", "pubmedid": "16448176 24915368", "mw": "365.38", "pi": "5.95", "charge_ph7": "-0.04", "gravy": "-1.2333", "instability": "70.87", "hydrophobic": "0.3333", "boman": "0.3267", "helix": "0.0", "turn_pct": "0.6667", "sheet": "0.3333" }, { "id": "aceip0816", "seq": "PT", "length": "2", "detail": "ND", "source": "ND", "ic50": "0 0", "reference": "Peptides with angiotensin I converting enzyme (ACE) inhibitory activity generated from porcine skeletal muscle proteins by the action of meat-borne Lactobacillus.", "doi": "10.1016\/j.jprot.2013.06.023", "pubmedid": "23806758", "mw": "216.23", "pi": "5.95", "charge_ph7": "-0.04", "gravy": "-1.15", "instability": "5.0", "hydrophobic": "0.5", "boman": "0.13", "helix": "0.0", "turn_pct": "0.5", "sheet": "0.5" }, { "id": "aceip0817", "seq": "PTFIAW", "length": "6", "detail": "Milk | Milk (whey) | Milk (caprine) | Milk-Cheese (Sheep milk and cheeses proteins) | Synthesized | Hydrolysis | Cereals | Soybean", "source": "Milk | Synthesized | Cereal | Legume", "ic50": ">100 μM", "reference": "Potent synthetic analogues of angiotensin-converting enzyme inhibitor derived from Tuna muscle.", "doi": "", "pubmedid": "1368734", "mw": "733.85", "pi": "5.95", "charge_ph7": "-0.04", "gravy": "0.9833", "instability": "28.9", "hydrophobic": "0.8333", "boman": "-1.9633", "helix": "0.1667", "turn_pct": "0.1667", "sheet": "0.6667" }, { "id": "aceip0818", "seq": "PTHDAW", "length": "6", "detail": "ND", "source": "ND", "ic50": ">100 μM", "reference": "Potent synthetic analogues of angiotensin-converting enzyme inhibitor derived from Tuna muscle.", "doi": "", "pubmedid": "1368734", "mw": "725.75", "pi": "5.08", "charge_ph7": "-0.95", "gravy": "-1.35", "instability": "8.33", "hydrophobic": "0.5", "boman": "-0.2017", "helix": "0.1667", "turn_pct": "0.3333", "sheet": "0.3333" }, { "id": "aceip0819", "seq": "PTHGAW", "length": "6", "detail": "ND", "source": "ND", "ic50": ">100 μM", "reference": "Potent synthetic analogues of angiotensin-converting enzyme inhibitor derived from Tuna muscle.", "doi": "", "pubmedid": "1368734", "mw": "667.71", "pi": "7.17", "charge_ph7": "0.05", "gravy": "-0.8333", "instability": "-23.1", "hydrophobic": "0.5", "boman": "-0.6383", "helix": "0.1667", "turn_pct": "0.3333", "sheet": "0.3333" }, { "id": "aceip0820", "seq": "PTHIAW", "length": "6", "detail": "ND", "source": "ND", "ic50": "0.39 μM", "reference": "Potent synthetic analogues of angiotensin-converting enzyme inhibitor derived from Tuna muscle.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "1368734 23194537", "mw": "723.82", "pi": "7.17", "charge_ph7": "0.05", "gravy": "-0.0167", "instability": "81.57", "hydrophobic": "0.6667", "boman": "-1.3017", "helix": "0.1667", "turn_pct": "0.1667", "sheet": "0.5" }, { "id": "aceip0821", "seq": "PTHIDW", "length": "6", "detail": "Fish | Pacific cod", "source": "Fish", "ic50": "12.88 μM", "reference": "Potent synthetic analogues of angiotensin-converting enzyme inhibitor derived from Tuna muscle.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "1368734 23194537", "mw": "767.83", "pi": "5.08", "charge_ph7": "-0.95", "gravy": "-0.9", "instability": "81.57", "hydrophobic": "0.5", "boman": "-0.72", "helix": "0.0", "turn_pct": "0.3333", "sheet": "0.5" }, { "id": "aceip0822", "seq": "PTHIK", "length": "5", "detail": "Milk (human)", "source": "Milk", "ic50": ">100 μM", "reference": "Potent synthetic analogues of angiotensin-converting enzyme inhibitor derived from Tuna muscle.", "doi": "", "pubmedid": "1368734", "mw": "594.7", "pi": "9.18", "charge_ph7": "1.04", "gravy": "-0.98", "instability": "78.9", "hydrophobic": "0.4", "boman": "-0.418", "helix": "0.2", "turn_pct": "0.2", "sheet": "0.4" }, { "id": "aceip0823", "seq": "PTHIKW", "length": "6", "detail": "Casein | Milk (human)", "source": "Milk", "ic50": "1.8 μM", "reference": "Potent synthetic analogues of angiotensin-converting enzyme inhibitor derived from Tuna muscle.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "1368734 23194537", "mw": "780.91", "pi": "9.18", "charge_ph7": "1.04", "gravy": "-0.9667", "instability": "67.42", "hydrophobic": "0.5", "boman": "-0.7367", "helix": "0.1667", "turn_pct": "0.1667", "sheet": "0.5" }, { "id": "aceip0824", "seq": "PTHIKWD", "length": "7", "detail": "Amaranth | Cereals (Maize) | Cereals (Wheat) | Cereals (Rye)", "source": "Plants | Cereal", "ic50": "38 μM", "reference": "Potent synthetic analogues of angiotensin-converting enzyme inhibitor derived from Tuna muscle.", "doi": "", "pubmedid": "1368734", "mw": "896.0", "pi": "7.18", "charge_ph7": "0.05", "gravy": "-1.3286", "instability": "59.21", "hydrophobic": "0.4286", "boman": "-0.3914", "helix": "0.1429", "turn_pct": "0.2857", "sheet": "0.4286" }, { "id": "aceip0825", "seq": "PTHIKWG", "length": "7", "detail": "Milk (bovine)", "source": "Milk", "ic50": "7.59 μM", "reference": "Potent synthetic analogues of angiotensin-converting enzyme inhibitor derived from Tuna muscle.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "1368734 23194537", "mw": "837.96", "pi": "9.18", "charge_ph7": "1.04", "gravy": "-0.8857", "instability": "44.4", "hydrophobic": "0.4286", "boman": "-0.7657", "helix": "0.1429", "turn_pct": "0.2857", "sheet": "0.4286" }, { "id": "aceip0826", "seq": "PTHIKWGD", "length": "8", "detail": "Cheese (Fresco)", "source": "Milk", "ic50": "0.9 μM", "reference": "Isolation of angiotensin-converting enzyme inhibitor from tuna muscle.; Review on the angiotensin-I-converting enzyme (ACE) inhibitor peptides from marine proteins.", "doi": "10.1016\/s0006-291x(88)81089-1; 10.1007\/s12010-012-0024-y", "pubmedid": "3415688 23271625", "mw": "953.05", "pi": "7.18", "charge_ph7": "0.05", "gravy": "-1.2125", "instability": "40.1", "hydrophobic": "0.375", "boman": "-0.46", "helix": "0.125", "turn_pct": "0.375", "sheet": "0.375" }, { "id": "aceip0827", "seq": "PTHIKWN", "length": "7", "detail": "Milk (bovine)", "source": "Milk", "ic50": "38.02 μM", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "23194537", "mw": "895.02", "pi": "9.18", "charge_ph7": "1.04", "gravy": "-1.3286", "instability": "76.84", "hydrophobic": "0.4286", "boman": "-0.4", "helix": "0.1429", "turn_pct": "0.2857", "sheet": "0.4286" }, { "id": "aceip0828", "seq": "PTHIW", "length": "5", "detail": "Milk (bovine)", "source": "Milk", "ic50": ">100 μM", "reference": "Potent synthetic analogues of angiotensin-converting enzyme inhibitor derived from Tuna muscle.", "doi": "", "pubmedid": "1368734", "mw": "652.74", "pi": "7.17", "charge_ph7": "0.05", "gravy": "-0.38", "instability": "95.88", "hydrophobic": "0.6", "boman": "-1.2", "helix": "0.0", "turn_pct": "0.2", "sheet": "0.6" }, { "id": "aceip0829", "seq": "PTHKAW", "length": "6", "detail": "Bovine", "source": "Bovine", "ic50": ">100 μM", "reference": "Potent synthetic analogues of angiotensin-converting enzyme inhibitor derived from Tuna muscle.", "doi": "", "pubmedid": "1368734", "mw": "738.83", "pi": "9.18", "charge_ph7": "1.04", "gravy": "-1.4167", "instability": "47.8", "hydrophobic": "0.5", "boman": "-0.2183", "helix": "0.3333", "turn_pct": "0.1667", "sheet": "0.3333" }, { "id": "aceip0830", "seq": "PTHVAW", "length": "6", "detail": "Milk (bovine)", "source": "Milk", "ic50": "1.5 μM", "reference": "Potent synthetic analogues of angiotensin-converting enzyme inhibitor derived from Tuna muscle.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "1368734 23194537", "mw": "709.79", "pi": "7.17", "charge_ph7": "0.05", "gravy": "-0.0667", "instability": "8.33", "hydrophobic": "0.6667", "boman": "-1.155", "helix": "0.1667", "turn_pct": "0.1667", "sheet": "0.5" }, { "id": "aceip0831", "seq": "PTPAP", "length": "5", "detail": "Milk (bovine)", "source": "Milk", "ic50": "33 μM", "reference": "Inhibition of angiotensin-converting enzyme by synthetic peptide fragments of human kappa-casein.", "doi": "", "pubmedid": "1368540", "mw": "481.54", "pi": "5.95", "charge_ph7": "-0.04", "gravy": "-0.74", "instability": "85.04", "hydrophobic": "0.8", "boman": "-0.31", "helix": "0.2", "turn_pct": "0.6", "sheet": "0.2" }, { "id": "aceip0832", "seq": "PTPVP", "length": "5", "detail": "Milk (bovine) | Cereals (Wheat) | Soybean | Pork | Chicken", "source": "Milk | Cereal | Legume | Porcine | Chicken", "ic50": "256.41 μM", "reference": "Angiotensin I-converting enzyme inhibitory peptides generated from in vitro gastrointestinal digestion of pork meat.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1021\/jf904204n; 10.1016\/j.foodchem.2012.09.092; 10.1080\/10408398.2012.664829", "pubmedid": "20151679 23194537 24915368", "mw": "509.6", "pi": "5.95", "charge_ph7": "-0.04", "gravy": "-0.26", "instability": "85.04", "hydrophobic": "0.8", "boman": "-0.756", "helix": "0.0", "turn_pct": "0.6", "sheet": "0.4" }, { "id": "aceip0833", "seq": "PVPQP", "length": "5", "detail": "Soybean", "source": "Legume", "ic50": "110 μM", "reference": "Inhibition of angiotensin-converting enzyme by synthetic peptide fragments of various beta-caseins.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "1368548 23194537", "mw": "536.62", "pi": "5.95", "charge_ph7": "-0.04", "gravy": "-0.82", "instability": "162.08", "hydrophobic": "0.8", "boman": "-0.536", "helix": "0.0", "turn_pct": "0.6", "sheet": "0.2" }, { "id": "aceip0834", "seq": "PVQALLLNQELLLNP", "length": "15", "detail": "Milk (bovine)", "source": "Milk", "ic50": null, "reference": "Inhibition of angiotensin-converting enzyme by synthetic peptide fragments of various beta-caseins.", "doi": "", "pubmedid": "1368548", "mw": "1674.98", "pi": "4.05", "charge_ph7": "-1.04", "gravy": "0.54", "instability": "28.07", "hydrophobic": "0.6667", "boman": "-1.8513", "helix": "0.5333", "turn_pct": "0.2667", "sheet": "0.4667" }, { "id": "aceip0835", "seq": "PVRAVP", "length": "6", "detail": "ND", "source": "ND", "ic50": "170 μM", "reference": "Inhibition of angiotensin-converting enzyme by synthetic peptide fragments of various beta-caseins.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "1368548 23194537", "mw": "637.77", "pi": "10.18", "charge_ph7": "0.96", "gravy": "0.4167", "instability": "72.53", "hydrophobic": "0.8333", "boman": "-1.195", "helix": "0.1667", "turn_pct": "0.3333", "sheet": "0.3333" }, { "id": "aceip0836", "seq": "PY", "length": "2", "detail": "Milk | Amaranth | Cereals (Maize) | Cereals (Wheat) | Maize | Meat", "source": "Milk | Plants | Cereal | Meat", "ic50": null, "reference": "Three-dimensional holograph vector of atomic interaction field (3D-HoVAIF): a novel rotation-translation invariant 3D structure descriptor and its applications to peptides.", "doi": "10.1002\/psc.892", "pubmedid": "17654623", "mw": "278.3", "pi": "5.95", "charge_ph7": "-0.04", "gravy": "-1.45", "instability": "5.0", "hydrophobic": "0.5", "boman": "0.07", "helix": "0.0", "turn_pct": "0.5", "sheet": "0.5" }, { "id": "aceip0837", "seq": "PYK", "length": "3", "detail": "Cereals (Maize)", "source": "Cereal", "ic50": "2400 μM", "reference": "Inhibition strength of short peptides derived from an ACE inhibitory peptide.", "doi": "10.1021\/jf202902r", "pubmedid": "21923188", "mw": "406.48", "pi": "9.01", "charge_ph7": "0.96", "gravy": "-2.2667", "instability": "6.67", "hydrophobic": "0.3333", "boman": "0.5733", "helix": "0.3333", "turn_pct": "0.3333", "sheet": "0.3333" }, { "id": "aceip0838", "seq": "PYKW", "length": "4", "detail": "Casein | Milk (human)", "source": "Milk", "ic50": "17.2 μM", "reference": "Inhibition strength of short peptides derived from an ACE inhibitory peptide.", "doi": "10.1021\/jf202902r", "pubmedid": "21923188", "mw": "592.69", "pi": "9.01", "charge_ph7": "0.96", "gravy": "-1.925", "instability": "7.5", "hydrophobic": "0.5", "boman": "-0.1525", "helix": "0.25", "turn_pct": "0.25", "sheet": "0.5" }, { "id": "aceip0839", "seq": "PYKWLP", "length": "6", "detail": "Cereals (Maize)", "source": "Cereal", "ic50": "5.5 μM", "reference": "Inhibition strength of short peptides derived from an ACE inhibitory peptide.", "doi": "10.1021\/jf202902r", "pubmedid": "21923188", "mw": "802.96", "pi": "9.01", "charge_ph7": "0.96", "gravy": "-0.9167", "instability": "61.0", "hydrophobic": "0.6667", "boman": "-0.9217", "helix": "0.3333", "turn_pct": "0.3333", "sheet": "0.5" }, { "id": "aceip0840", "seq": "PYP", "length": "3", "detail": "Casein", "source": "Milk", "ic50": "<20 mM", "reference": "Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Evaluation of the allergenicity of goat milk, cow milk, and their lactosera in a guinea pig model.", "doi": "10.1021\/jf051263l; 10.3168\/jds.2008-1125", "pubmedid": "16448176 19233776", "mw": "375.42", "pi": "5.95", "charge_ph7": "-0.04", "gravy": "-1.5", "instability": "47.8", "hydrophobic": "0.6667", "boman": "0.0467", "helix": "0.0", "turn_pct": "0.6667", "sheet": "0.3333" }, { "id": "aceip0841", "seq": "PYVRYL", "length": "6", "detail": "Milk (bovine) | Milk (whey) | Milk (Fermented Milk)", "source": "Milk", "ic50": "1.9 μM", "reference": "Angiotensin-converting enzyme inhibitory activity of peptides derived from caprine kefir.; Antihypertensive peptides: production, bioavailability and incorporation into foods.; Antihypertensive peptides from food proteins: a review.; Novel angiotensin I-converting enzyme inhibitory peptides derived from an edible mushroom, Pleurotus cystidiosus O.K. Miller identified by LC-MS\/MS.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.3168\/jds.S0022-0302(05)73032-0; 10.1016\/j.cis.2010.11.001; 10.1039\/c2fo10192k; 10.1186\/1472-6882-13-313; 10.1080\/10408398.2012.664829", "pubmedid": "16162521 21185549 22249830 24215325 24915368", "mw": "809.95", "pi": "9.0", "charge_ph7": "0.96", "gravy": "-0.1167", "instability": "-4.23", "hydrophobic": "0.5", "boman": "-0.9933", "helix": "0.1667", "turn_pct": "0.1667", "sheet": "0.6667" }, { "id": "aceip0842", "seq": "QEVLP", "length": "5", "detail": "Milk (caprine kefir)", "source": "Milk", "ic50": ">1000 μM", "reference": "Inhibition of angiotensin-converting enzyme by synthetic peptide fragments of various beta-caseins.", "doi": "", "pubmedid": "1368548", "mw": "584.66", "pi": "4.05", "charge_ph7": "-1.24", "gravy": "-0.12", "instability": "85.04", "hydrophobic": "0.6", "boman": "-1.192", "helix": "0.4", "turn_pct": "0.2", "sheet": "0.4" }, { "id": "aceip0843", "seq": "QF", "length": "2", "detail": "Synthesized", "source": "Synthesized", "ic50": null, "reference": "Peptides with angiotensin I converting enzyme (ACE) inhibitory activity generated from porcine skeletal muscle proteins by the action of meat-borne Lactobacillus.", "doi": "10.1016\/j.jprot.2013.06.023", "pubmedid": "23806758", "mw": "293.32", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "-0.35", "instability": "-32.7", "hydrophobic": "0.5", "boman": "-0.81", "helix": "0.0", "turn_pct": "0.0", "sheet": "0.5" }, { "id": "aceip0844", "seq": "QFYQLD", "length": "6", "detail": "Milk (Casein)", "source": "Milk", "ic50": null, "reference": "Hot topic: Changes in angiotensin-converting enzyme inhibition and concentrations of the tripeptides Val-Pro-Pro and Ile-Pro-Pro during ripening of different Swiss cheese varieties.", "doi": "10.3168\/jds.2008-1531", "pubmedid": "19233775", "mw": "812.87", "pi": "4.3", "charge_ph7": "-1.24", "gravy": "-0.8667", "instability": "50.1", "hydrophobic": "0.3333", "boman": "-0.56", "helix": "0.1667", "turn_pct": "0.1667", "sheet": "0.5" }, { "id": "aceip0845", "seq": "QG", "length": "2", "detail": "Egg (Ovalbumin)", "source": "Egg", "ic50": "<20 mM", "reference": "Binding of peptide substrates and inhibitors of angiotensin-converting enzyme. Importance of the COOH-terminal dipeptide sequence.; Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Three-dimensional holograph vector of atomic interaction field (3D-HoVAIF): a novel rotation-translation invariant 3D structure descriptor and its applications to peptides.; QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1021\/jf051263l; 10.1002\/psc.892; 10.1007\/s00894-010-0862-x; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "6243277 16448176 17654623 20941517 23871047", "mw": "203.2", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "-1.95", "instability": "5.0", "hydrophobic": "0.0", "boman": "0.21", "helix": "0.0", "turn_pct": "0.5", "sheet": "0.0" }, { "id": "aceip0846", "seq": "QK", "length": "2", "detail": "Synthesized | Fish (Alaska pollack) | Cereals | Pork", "source": "Synthesized | Fish | Cereal | Porcine", "ic50": "<20 mM", "reference": "Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Model of the exofacial substrate-binding site and helical folding of the human Glut1 glucose transporter based on scanning mutagenesis.; Peptides with angiotensin I converting enzyme (ACE) inhibitory activity generated from porcine skeletal muscle proteins by the action of meat-borne Lactobacillus.", "doi": "10.1021\/jf051263l; 10.1021\/bi900521n; 10.1016\/j.jprot.2013.06.023", "pubmedid": "16448176 19449892 23806758", "mw": "274.32", "pi": "8.75", "charge_ph7": "0.76", "gravy": "-3.7", "instability": "5.0", "hydrophobic": "0.0", "boman": "1.47", "helix": "0.5", "turn_pct": "0.0", "sheet": "0.0" }, { "id": "aceip0847", "seq": "QKAVPYPQRDMPI", "length": "13", "detail": "Soybean", "source": "Legume", "ic50": null, "reference": "Identification of angiotensin-I-converting enzyme inhibitory peptides derived from sodium caseinate hydrolysates produced by Lactobacillus helveticus NCC 2765.", "doi": "10.1021\/jf049510t", "pubmedid": "15537298", "mw": "1542.8", "pi": "8.59", "charge_ph7": "0.76", "gravy": "-0.9692", "instability": "82.15", "hydrophobic": "0.5385", "boman": "-0.3292", "helix": "0.2308", "turn_pct": "0.3077", "sheet": "0.2308" }, { "id": "aceip0848", "seq": "QKTAP", "length": "5", "detail": "Milk (bovine) | Milk (human)", "source": "Milk", "ic50": "30 μM", "reference": "Inhibition of angiotensin-converting enzyme by synthetic peptide fragments of human kappa-casein.", "doi": "", "pubmedid": "1368540", "mw": "543.61", "pi": "8.75", "charge_ph7": "0.76", "gravy": "-1.58", "instability": "46.52", "hydrophobic": "0.4", "boman": "0.278", "helix": "0.4", "turn_pct": "0.2", "sheet": "0.2" }, { "id": "aceip0849", "seq": "QLGFLGPR", "length": "8", "detail": "Cereals (Maize)", "source": "Cereal", "ic50": "0.21 mg\/ml", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.; Review on the angiotensin-I-converting enzyme (ACE) inhibitor peptides from marine proteins.", "doi": "10.1016\/j.foodchem.2012.09.092; 10.1007\/s12010-012-0024-y", "pubmedid": "23194537 23271625", "mw": "887.04", "pi": "9.75", "charge_ph7": "0.76", "gravy": "0.0", "instability": "-0.68", "hydrophobic": "0.5", "boman": "-1.3275", "helix": "0.25", "turn_pct": "0.375", "sheet": "0.375" }, { "id": "aceip0850", "seq": "QLLKLK", "length": "6", "detail": "Milk (bovine) | Milk | Amaranth | Cereals (Maize) | Cereals (Wheat) | Pork", "source": "Milk | Plants | Cereal | Porcine", "ic50": "342.4 μM", "reference": "Angiotensin-converting enzyme inhibitory activity of peptides derived from caprine kefir.", "doi": "10.3168\/jds.S0022-0302(05)73032-0", "pubmedid": "16162521", "mw": "741.96", "pi": "10.0", "charge_ph7": "1.76", "gravy": "0.0167", "instability": "-34.12", "hydrophobic": "0.5", "boman": "-1.7067", "helix": "0.8333", "turn_pct": "0.0", "sheet": "0.5" }, { "id": "aceip0851", "seq": "QNILP", "length": "5", "detail": "Cereals (Maize)", "source": "Cereal", "ic50": ">1000 μM", "reference": "Inhibition of angiotensin-converting enzyme by synthetic peptide fragments of various beta-caseins.", "doi": "", "pubmedid": "1368548", "mw": "583.68", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "-0.06", "instability": "172.92", "hydrophobic": "0.6", "boman": "-1.372", "helix": "0.2", "turn_pct": "0.4", "sheet": "0.4" }, { "id": "aceip0852", "seq": "QNLLRF", "length": "6", "detail": "Cereals (Maize)", "source": "Cereal", "ic50": "82.4 mg\/ml", "reference": "Milk protein peptides with angiotensin I-converting enzyme inhibitory (ACEI) activity.", "doi": "10.1080\/10408390802304198", "pubmedid": "20373185", "mw": "789.92", "pi": "9.75", "charge_ph7": "0.76", "gravy": "-0.1833", "instability": "40.43", "hydrophobic": "0.5", "boman": "-1.1867", "helix": "0.3333", "turn_pct": "0.1667", "sheet": "0.5" }, { "id": "aceip0853", "seq": "QPIP", "length": "4", "detail": "Milk (human)", "source": "Milk", "ic50": "860 μM", "reference": "Inhibition of angiotensin-converting enzyme by synthetic peptide fragments of various beta-caseins.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1016\/j.foodchem.2013.05.140", "pubmedid": "1368548 23871047", "mw": "453.53", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "-0.55", "instability": "48.45", "hydrophobic": "0.75", "boman": "-0.89", "helix": "0.0", "turn_pct": "0.5", "sheet": "0.25" }, { "id": "aceip0854", "seq": "QPLIYP", "length": "6", "detail": "Milk (Casein)", "source": "Milk", "ic50": "3.6 μM", "reference": "Inhibition of angiotensin-converting enzyme by synthetic peptide fragments of various beta-caseins.", "doi": "", "pubmedid": "1368548", "mw": "729.86", "pi": "5.52", "charge_ph7": "-0.24", "gravy": "0.05", "instability": "61.0", "hydrophobic": "0.6667", "boman": "-1.39", "helix": "0.1667", "turn_pct": "0.3333", "sheet": "0.5" }, { "id": "aceip0855", "seq": "QPQ", "length": "3", "detail": "Milk (bovine)", "source": "Milk", "ic50": null, "reference": "Angiotensin I-converting-enzyme-inhibitory and antibacterial peptides from Lactobacillus helveticus PR4 proteinase-hydrolyzed caseins of milk from six species.", "doi": "10.1128\/AEM.69.9.5297-5305.2003", "pubmedid": "12957917", "mw": "371.39", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "-2.8667", "instability": "135.07", "hydrophobic": "0.3333", "boman": "0.9067", "helix": "0.0", "turn_pct": "0.3333", "sheet": "0.0" }, { "id": "aceip0856", "seq": "QPQPLIYP", "length": "8", "detail": "Milk (Casein)", "source": "Milk", "ic50": "4 μM", "reference": "Inhibition of angiotensin-converting enzyme by synthetic peptide fragments of various beta-caseins.", "doi": "", "pubmedid": "1368548", "mw": "955.11", "pi": "5.52", "charge_ph7": "-0.24", "gravy": "-0.6", "instability": "96.4", "hydrophobic": "0.625", "boman": "-0.8725", "helix": "0.125", "turn_pct": "0.375", "sheet": "0.375" }, { "id": "aceip0857", "seq": "QSLVYP", "length": "6", "detail": "Milk-Cheese (Sheep milk and cheeses proteins) | Milk (Ovine milk proteins)", "source": "Milk", "ic50": "41 μM", "reference": "Inhibition of angiotensin-converting enzyme by synthetic peptide fragments of various beta-caseins.; Evaluation of the allergenicity of goat milk, cow milk, and their lactosera in a guinea pig model.", "doi": "10.3168\/jds.2008-1125", "pubmedid": "1368548 19233776", "mw": "705.8", "pi": "5.52", "charge_ph7": "-0.24", "gravy": "0.1333", "instability": "89.57", "hydrophobic": "0.5", "boman": "-1.1033", "helix": "0.1667", "turn_pct": "0.3333", "sheet": "0.5" }, { "id": "aceip0858", "seq": "QTQSLVYP", "length": "8", "detail": "Milk (Casein)", "source": "Milk", "ic50": "73 μM", "reference": "Inhibition of angiotensin-converting enzyme by synthetic peptide fragments of various beta-caseins.; Evaluation of the allergenicity of goat milk, cow milk, and their lactosera in a guinea pig model.", "doi": "10.3168\/jds.2008-1125", "pubmedid": "1368548 19233776", "mw": "935.03", "pi": "5.52", "charge_ph7": "-0.24", "gravy": "-0.425", "instability": "60.25", "hydrophobic": "0.375", "boman": "-0.625", "helix": "0.125", "turn_pct": "0.25", "sheet": "0.5" }, { "id": "aceip0859", "seq": "QTQYTDAPSFSDIPNPIGSENSEKTTMPLW", "length": "30", "detail": "Milk (bovine) | Carp | Cereals (Wheat) | Pork | Chicken", "source": "Milk | Fish | Cereal | Porcine | Chicken", "ic50": "346 mM\/L", "reference": "Antihypertensive effect of the peptides derived from casein by an extracellular proteinase from Lactobacillus helveticus CP790.", "doi": "10.3168\/jds.S0022-0302(94)77026-0", "pubmedid": "8201050", "mw": "3355.59", "pi": "4.05", "charge_ph7": "-3.23", "gravy": "-0.92", "instability": "48.11", "hydrophobic": "0.3667", "boman": "-0.215", "helix": "0.2", "turn_pct": "0.4333", "sheet": "0.3333" }, { "id": "aceip0860", "seq": "QVPQPIP", "length": "7", "detail": "Milk", "source": "Milk", "ic50": "660 μM", "reference": "Inhibition of angiotensin-converting enzyme by synthetic peptide fragments of various beta-caseins.", "doi": "", "pubmedid": "1368548", "mw": "777.91", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "-0.4429", "instability": "76.23", "hydrophobic": "0.7143", "boman": "-0.8914", "helix": "0.0", "turn_pct": "0.4286", "sheet": "0.2857" }, { "id": "aceip0861", "seq": "QVSLNSGYY", "length": "9", "detail": "Milk", "source": "Milk", "ic50": "0 μM", "reference": "QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1007\/s00894-010-0862-x; 10.1016\/j.foodchem.2012.09.092", "pubmedid": "20941517 23194537", "mw": "1030.09", "pi": "5.52", "charge_ph7": "-0.24", "gravy": "-0.4", "instability": "4.79", "hydrophobic": "0.2222", "boman": "-0.5511", "helix": "0.1111", "turn_pct": "0.4444", "sheet": "0.4444" }, { "id": "aceip0862", "seq": "RA", "length": "2", "detail": "Milk | Milk (caprine) | Milk-Cheese (Sheep milk and cheeses proteins) | Hydrolysis", "source": "Milk | Synthesized", "ic50": "460 μM", "reference": "Three-dimensional holograph vector of atomic interaction field (3D-HoVAIF): a novel rotation-translation invariant 3D structure descriptor and its applications to peptides.; QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.; Peptides with angiotensin I converting enzyme (ACE) inhibitory activity generated from porcine skeletal muscle proteins by the action of meat-borne Lactobacillus.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1002\/psc.892; 10.1007\/s00894-010-0862-x; 10.1016\/j.jprot.2013.06.023; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "17654623 20941517 23806758 23871047", "mw": "245.28", "pi": "9.75", "charge_ph7": "0.76", "gravy": "-1.35", "instability": "5.0", "hydrophobic": "0.5", "boman": "0.455", "helix": "0.5", "turn_pct": "0.0", "sheet": "0.0" }, { "id": "aceip0863", "seq": "RADHPFL", "length": "7", "detail": "Milk (whey)", "source": "Milk", "ic50": null, "reference": "Antihypertensive peptides: production, bioavailability and incorporation into foods.; Antihypertensive peptides from food proteins: a review.", "doi": "10.1016\/j.cis.2010.11.001; 10.1039\/c2fo10192k", "pubmedid": "21185549 22249830", "mw": "854.95", "pi": "6.74", "charge_ph7": "-0.15", "gravy": "-0.6286", "instability": "19.84", "hydrophobic": "0.5714", "boman": "-0.6171", "helix": "0.2857", "turn_pct": "0.2857", "sheet": "0.2857" }, { "id": "aceip0864", "seq": "RALP", "length": "4", "detail": "Milk (bovine) | Milk | Cheese | Amaranth | Sesame | Cereals (Maize) | Cereals (Wheat) | Maize | Cereals (Rye)", "source": "Milk | Plants | Cereal", "ic50": "0.65 mM", "reference": "Glycinyl-histidinyl-serine (GHS), a novel rapeseed protein-derived peptide has blood pressure-lowering effect in spontaneously hypertensive rats.", "doi": "10.1021\/jf400865m", "pubmedid": "23919612", "mw": "455.55", "pi": "9.75", "charge_ph7": "0.76", "gravy": "-0.125", "instability": "55.65", "hydrophobic": "0.75", "boman": "-1.0025", "helix": "0.5", "turn_pct": "0.25", "sheet": "0.25" }, { "id": "aceip0865", "seq": "RDMPIQAF", "length": "8", "detail": "Milk (bovine)", "source": "Milk", "ic50": "197.46 μM", "reference": "Identification of angiotensin-I-converting enzyme inhibitory peptides derived from sodium caseinate hydrolysates produced by Lactobacillus helveticus NCC 2765.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1021\/jf049510t; 10.1016\/j.foodchem.2012.09.092", "pubmedid": "15537298 23194537", "mw": "977.14", "pi": "5.84", "charge_ph7": "-0.24", "gravy": "-0.2625", "instability": "63.67", "hydrophobic": "0.625", "boman": "-0.7875", "helix": "0.25", "turn_pct": "0.25", "sheet": "0.25" }, { "id": "aceip0866", "seq": "RELEE", "length": "5", "detail": "Milk (bovine)", "source": "Milk", "ic50": null, "reference": "Enterococcus faecalis strains from food, environmental, and clinical origin produce ACE-inhibitory peptides and other bioactive peptides during growth in bovine skim milk.", "doi": "10.1016\/j.ijfoodmicro.2013.06.019", "pubmedid": "23845432", "mw": "674.7", "pi": "4.52", "charge_ph7": "-2.23", "gravy": "-2.24", "instability": "73.2", "hydrophobic": "0.2", "boman": "0.544", "helix": "0.8", "turn_pct": "0.0", "sheet": "0.2" }, { "id": "aceip0867", "seq": "RELEEL", "length": "6", "detail": "Fish", "source": "Fish", "ic50": "1000 μM", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "23194537", "mw": "787.86", "pi": "4.25", "charge_ph7": "-2.23", "gravy": "-1.2333", "instability": "62.67", "hydrophobic": "0.3333", "boman": "-0.3667", "helix": "0.8333", "turn_pct": "0.0", "sheet": "0.3333" }, { "id": "aceip0868", "seq": "RF", "length": "2", "detail": "Cereals (Barley)", "source": "Cereal", "ic50": "<20 mM", "reference": "Structure and activity of angiotensin I converting enzyme inhibitory peptides from sake and sake lees.; Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Quantitative structure-activity relationship study of bitter di- and tri-peptides including relationship with angiotensin I-converting enzyme inhibitory activity.; Three-dimensional holograph vector of atomic interaction field (3D-HoVAIF): a novel rotation-translation invariant 3D structure descriptor and its applications to peptides.; Bioactive peptides in amaranth (Amaranthus hypochondriacus) seed.; QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.; Antihypertensive peptides from food proteins: a review.; Vegetable foods: a cheap source of proteins and peptides with antihypertensive, antioxidant, and other less occurrence bioactivities.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1271\/bbb.58.1767; 10.1021\/jf051263l; 10.1002\/psc.800; 10.1002\/psc.892; 10.1021\/jf072911z; 10.1007\/s00894-010-0862-x; 10.1039\/c2fo10192k; 10.1016\/j.talanta.2012.12.041; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "7765503 16448176 17117396 17654623 18211015 20941517 22249830 23598136 23871047", "mw": "321.37", "pi": "9.75", "charge_ph7": "0.76", "gravy": "-0.85", "instability": "5.0", "hydrophobic": "0.5", "boman": "-0.13", "helix": "0.0", "turn_pct": "0.0", "sheet": "0.5" }, { "id": "aceip0869", "seq": "RFH", "length": "3", "detail": "Milk", "source": "Milk", "ic50": "<20 mM", "reference": "Angiotensin I-converting enzyme inhibitory peptides in an alkaline protease hydrolyzate derived from sardine muscle.; Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Review on the angiotensin-I-converting enzyme (ACE) inhibitor peptides from marine proteins.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1271\/bbb.58.2244; 10.1021\/jf051263l; 10.1007\/s12010-012-0024-y; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "7765718 16448176 23271625 23871047", "mw": "458.51", "pi": "9.76", "charge_ph7": "0.85", "gravy": "-1.6333", "instability": "6.67", "hydrophobic": "0.3333", "boman": "0.2433", "helix": "0.0", "turn_pct": "0.0", "sheet": "0.3333" }, { "id": "aceip0870", "seq": "RG", "length": "2", "detail": "Amaranth | Cereals (Maize) | Cereals (Wheat) | Maize | Soybean", "source": "Plants | Cereal | Legume", "ic50": "<20 mM", "reference": "Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Quantitative structure-activity relationship study of bitter di- and tri-peptides including relationship with angiotensin I-converting enzyme inhibitory activity.", "doi": "10.1021\/jf051263l; 10.1002\/psc.800", "pubmedid": "16448176 17117396", "mw": "231.25", "pi": "9.75", "charge_ph7": "0.76", "gravy": "-2.45", "instability": "-37.45", "hydrophobic": "0.0", "boman": "0.89", "helix": "0.0", "turn_pct": "0.5", "sheet": "0.0" }, { "id": "aceip0871", "seq": "RGP", "length": "3", "detail": "Cereals (Maize)", "source": "Cereal", "ic50": null, "reference": "Quantitative structure-activity relationship study of bitter di- and tri-peptides including relationship with angiotensin I-converting enzyme inhibitory activity.; QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1002\/psc.800; 10.1007\/s00894-010-0862-x; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "17117396 20941517 23871047", "mw": "328.37", "pi": "9.75", "charge_ph7": "0.76", "gravy": "-2.1667", "instability": "-21.63", "hydrophobic": "0.3333", "boman": "0.5933", "helix": "0.0", "turn_pct": "0.6667", "sheet": "0.0" }, { "id": "aceip0872", "seq": "RGPFPIIV", "length": "8", "detail": "Cereals (Maize)", "source": "Cereal", "ic50": "0 0", "reference": "Putting microbes to work: dairy fermentation, cell factories and bioactive peptides. Part I: overview.", "doi": "10.1002\/biot.200600246", "pubmedid": "17407210", "mw": "898.1", "pi": "9.75", "charge_ph7": "0.76", "gravy": "0.9875", "instability": "35.67", "hydrophobic": "0.75", "boman": "-1.885", "helix": "0.0", "turn_pct": "0.375", "sheet": "0.5" }, { "id": "aceip0873", "seq": "RGY", "length": "3", "detail": "Cereals (Maize)", "source": "Cereal", "ic50": "61.9 μM", "reference": "ACE inhibitory peptides and antioxidant peptides derived from in vitro digestion hydrolysate of hen egg white lysozyme.", "doi": "10.1016\/j.foodchem.2012.05.059", "pubmedid": "22953850", "mw": "394.43", "pi": "8.75", "charge_ph7": "0.76", "gravy": "-2.0667", "instability": "-49.93", "hydrophobic": "0.0", "boman": "0.64", "helix": "0.0", "turn_pct": "0.3333", "sheet": "0.3333" }, { "id": "aceip0874", "seq": "RIGLF", "length": "5", "detail": "Milk (bovine) | Casein | Milk (Casein) | Lactobacillus helveticus", "source": "Milk | Bacteria", "ic50": "116 μM", "reference": "Novel angiotensin I-converting enzyme inhibitory peptides derived from edible mushroom Agaricus bisporus (J.E. Lange) Imbach identified by LC-MS\/MS.", "doi": "10.1016\/j.foodchem.2013.10.053", "pubmedid": "24262574", "mw": "604.74", "pi": "9.75", "charge_ph7": "0.76", "gravy": "1.24", "instability": "8.0", "hydrophobic": "0.6", "boman": "-2.208", "helix": "0.2", "turn_pct": "0.2", "sheet": "0.6" }, { "id": "aceip0875", "seq": "RIY", "length": "3", "detail": "Milk | Casein", "source": "Milk", "ic50": "<20 mM", "reference": "New antihypertensive peptides isolated from rapeseed.; Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Angiotensin converting enzyme inhibitory peptides derived from food proteins: biochemistry, bioactivity and production.; Antihypertensive peptides from food proteins: a review.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.; Glycinyl-histidinyl-serine (GHS), a novel rapeseed protein-derived peptide has blood pressure-lowering effect in spontaneously hypertensive rats.", "doi": "10.1016\/s0196-9781(03)00174-8; 10.1021\/jf051263l; 10.2174\/138161207780363068; 10.1039\/c2fo10192k; 10.1016\/j.foodchem.2013.05.140; 10.1021\/jf400865m", "pubmedid": "12948830 16448176 17430180 22249830 23871047 23919612", "mw": "450.53", "pi": "8.75", "charge_ph7": "0.76", "gravy": "-0.4333", "instability": "6.67", "hydrophobic": "0.3333", "boman": "-0.6867", "helix": "0.0", "turn_pct": "0.0", "sheet": "0.6667" }, { "id": "aceip0876", "seq": "RL", "length": "2", "detail": "Milk", "source": "Milk", "ic50": "<20 mM", "reference": "Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Bioactive peptides in amaranth (Amaranthus hypochondriacus) seed.; Quality and acceptability of a set-type yogurt made from camel milk.; Peptides with angiotensin I converting enzyme (ACE) inhibitory activity generated from porcine skeletal muscle proteins by the action of meat-borne Lactobacillus.", "doi": "10.1021\/jf051263l; 10.1021\/jf072911z; 10.3168\/jds.2008-1408; 10.1016\/j.jprot.2013.06.023", "pubmedid": "16448176 18211015 19233778 23806758", "mw": "287.36", "pi": "9.75", "charge_ph7": "0.76", "gravy": "-0.35", "instability": "5.0", "hydrophobic": "0.5", "boman": "-1.1", "helix": "0.5", "turn_pct": "0.0", "sheet": "0.5" }, { "id": "aceip0877", "seq": "RLPSEFDLSAFLRA", "length": "14", "detail": "Milk", "source": "Milk", "ic50": "0.46 mg\/ml", "reference": "Characterisation of a new antihypertensive angiotensin I-converting enzyme inhibitory peptide from Pleurotus cornucopiae.; Vegetable foods: a cheap source of proteins and peptides with antihypertensive, antioxidant, and other less occurrence bioactivities.; Characterization of an antihypertensive angiotensin I-converting enzyme inhibitory peptide from the edible mushroom Hypsizygus marmoreus.", "doi": "10.1016\/j.foodchem.2011.01.010; 10.1016\/j.talanta.2012.12.041; 10.1155\/2013\/283964", "pubmedid": "23140680 23598136 24380081", "mw": "1621.83", "pi": "6.07", "charge_ph7": "-0.24", "gravy": "0.1", "instability": "73.13", "hydrophobic": "0.5714", "boman": "-0.9929", "helix": "0.4286", "turn_pct": "0.2857", "sheet": "0.3571" }, { "id": "aceip0878", "seq": "RLSGQTIEVTSEYLFRH", "length": "17", "detail": "Salmon", "source": "Fish", "ic50": "1.14 mg\/ml", "reference": "Antihypertensive peptides from food proteins: a review.; Characterisation of a new antihypertensive angiotensin I-converting enzyme inhibitory peptide from Pleurotus cornucopiae.; Vegetable foods: a cheap source of proteins and peptides with antihypertensive, antioxidant, and other less occurrence bioactivities.; Characterization of an antihypertensive angiotensin I-converting enzyme inhibitory peptide from the edible mushroom Hypsizygus marmoreus.", "doi": "10.1039\/c2fo10192k; 10.1016\/j.foodchem.2011.01.010; 10.1016\/j.talanta.2012.12.041; 10.1155\/2013\/283964", "pubmedid": "22249830 23140680 23598136 24380081", "mw": "2036.25", "pi": "6.76", "charge_ph7": "-0.15", "gravy": "-0.4882", "instability": "52.92", "hydrophobic": "0.2941", "boman": "-0.5476", "helix": "0.2353", "turn_pct": "0.1765", "sheet": "0.4706" }, { "id": "aceip0879", "seq": "RML", "length": "3", "detail": "Milk", "source": "Milk", "ic50": "<20 mM", "reference": "Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.", "doi": "10.1021\/jf051263l", "pubmedid": "16448176", "mw": "418.55", "pi": "9.75", "charge_ph7": "0.76", "gravy": "0.4", "instability": "6.67", "hydrophobic": "0.6667", "boman": "-1.5167", "helix": "0.6667", "turn_pct": "0.0", "sheet": "0.3333" }, { "id": "aceip0880", "seq": "RMLGNTPTK", "length": "9", "detail": "Spinach", "source": "Plants", "ic50": "0 μM", "reference": "Strategies for designing novel functional meat products.", "doi": "10.1016\/j.meatsci.2006.04.028", "pubmedid": "22062731", "mw": "1017.2", "pi": "11.0", "charge_ph7": "1.76", "gravy": "-1.0667", "instability": "-9.98", "hydrophobic": "0.3333", "boman": "-0.1967", "helix": "0.3333", "turn_pct": "0.3333", "sheet": "0.3333" }, { "id": "aceip0881", "seq": "RMLGQ", "length": "5", "detail": "Salmon", "source": "Fish", "ic50": "354.81 μM", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "23194537", "mw": "603.74", "pi": "9.75", "charge_ph7": "0.76", "gravy": "-0.54", "instability": "8.0", "hydrophobic": "0.4", "boman": "-0.826", "helix": "0.4", "turn_pct": "0.2", "sheet": "0.2" }, { "id": "aceip0882", "seq": "RMLGQTP", "length": "7", "detail": "Fish", "source": "Fish", "ic50": "501.19 μM", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "23194537", "mw": "801.95", "pi": "9.75", "charge_ph7": "0.76", "gravy": "-0.7143", "instability": "8.57", "hydrophobic": "0.4286", "boman": "-0.5529", "helix": "0.2857", "turn_pct": "0.2857", "sheet": "0.2857" }, { "id": "aceip0883", "seq": "RMLGQTPTK", "length": "9", "detail": "Milk (bovine) | Milk | Amaranth | Synthesized | Bonito | Tuna | Sardine | Cereals (Maize) | Cereals (Wheat) | Squid | Egg (Ovalbumin)", "source": "Milk | Plants | Synthesized | Fish | Cereal | Animal | Egg", "ic50": "34 μM", "reference": "QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1007\/s00894-010-0862-x; 10.1016\/j.foodchem.2012.09.092", "pubmedid": "20941517 23194537", "mw": "1031.23", "pi": "11.0", "charge_ph7": "1.76", "gravy": "-1.0667", "instability": "8.89", "hydrophobic": "0.3333", "boman": "-0.2256", "helix": "0.3333", "turn_pct": "0.2222", "sheet": "0.3333" }, { "id": "aceip0884", "seq": "RMLGQTPWK", "length": "9", "detail": "Legume (Pea proteins)", "source": "Legume", "ic50": "34 μM", "reference": "Angiotensin-I converting enzyme inhibitory peptide derived from porcine skeletal muscle myosin and its antihypertensive activity in spontaneously hypertensive rats.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1111\/j.1750-3841.2007.00571.x; 10.1016\/j.foodchem.2012.09.092", "pubmedid": "18034756 23194537", "mw": "1116.34", "pi": "11.0", "charge_ph7": "1.76", "gravy": "-1.0889", "instability": "5.69", "hydrophobic": "0.4444", "boman": "-0.5133", "helix": "0.3333", "turn_pct": "0.2222", "sheet": "0.3333" }, { "id": "aceip0885", "seq": "RMLGQYPYK", "length": "9", "detail": "Soybean", "source": "Legume", "ic50": "34 μM", "reference": "Angiotensin I-converting enzyme-inhibitory peptides obtained from chicken collagen hydrolysate.", "doi": "10.1021\/jf072669w", "pubmedid": "18808143", "mw": "1155.37", "pi": "9.7", "charge_ph7": "1.76", "gravy": "-1.2", "instability": "14.22", "hydrophobic": "0.3333", "boman": "-0.2522", "helix": "0.3333", "turn_pct": "0.2222", "sheet": "0.3333" }, { "id": "aceip0886", "seq": "RP", "length": "2", "detail": "Oat", "source": "Cereal", "ic50": "<20 mM", "reference": "Binding of peptide substrates and inhibitors of angiotensin-converting enzyme. Importance of the COOH-terminal dipeptide sequence.; Angiotensin I-converting enzyme inhibitory activity and insulin secretion stimulative activity of fermented fish sauce.; Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Quantitative structure-activity relationship study of bitter di- and tri-peptides including relationship with angiotensin I-converting enzyme inhibitory activity.; Three-dimensional holograph vector of atomic interaction field (3D-HoVAIF): a novel rotation-translation invariant 3D structure descriptor and its applications to peptides.; QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.; Review on the angiotensin-I-converting enzyme (ACE) inhibitor peptides from marine proteins.; Peptides with angiotensin I converting enzyme (ACE) inhibitory activity generated from porcine skeletal muscle proteins by the action of meat-borne Lactobacillus.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1016\/S1389-1723(03)70138-8; 10.1021\/jf051263l; 10.1002\/psc.800; 10.1002\/psc.892; 10.1007\/s00894-010-0862-x; 10.1007\/s12010-012-0024-y; 10.1016\/j.jprot.2013.06.023; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "6243277 16233562 16448176 17117396 17654623 20941517 23271625 23806758 23871047", "mw": "271.32", "pi": "9.75", "charge_ph7": "0.76", "gravy": "-3.05", "instability": "101.3", "hydrophobic": "0.5", "boman": "1.36", "helix": "0.0", "turn_pct": "0.5", "sheet": "0.0" }, { "id": "aceip0887", "seq": "RPF", "length": "3", "detail": "Soybean", "source": "Legume", "ic50": null, "reference": "Quantitative structure-activity relationship study of bitter di- and tri-peptides including relationship with angiotensin I-converting enzyme inhibitory activity.; QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1002\/psc.800; 10.1007\/s00894-010-0862-x; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "17117396 20941517 23871047", "mw": "418.49", "pi": "9.75", "charge_ph7": "0.76", "gravy": "-1.1", "instability": "135.07", "hydrophobic": "0.6667", "boman": "-0.0867", "helix": "0.0", "turn_pct": "0.3333", "sheet": "0.3333" }, { "id": "aceip0888", "seq": "RPG", "length": "3", "detail": "Legume (Pea proteins)", "source": "Legume", "ic50": null, "reference": "Quantitative structure-activity relationship study of bitter di- and tri-peptides including relationship with angiotensin I-converting enzyme inhibitory activity.; QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1002\/psc.800; 10.1007\/s00894-010-0862-x; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "17117396 20941517 23871047", "mw": "328.37", "pi": "9.75", "charge_ph7": "0.76", "gravy": "-2.1667", "instability": "70.87", "hydrophobic": "0.3333", "boman": "0.5933", "helix": "0.0", "turn_pct": "0.6667", "sheet": "0.0" }, { "id": "aceip0889", "seq": "RPK", "length": "3", "detail": "Legume (Pea proteins)", "source": "Legume", "ic50": "<20 mM", "reference": "Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Bioactive peptides in ovine and caprine cheeselike systems prepared with proteases from Cynara cardunculus.", "doi": "10.1021\/jf051263l; 10.3168\/jds.S0022-0302(06)72370-0", "pubmedid": "16448176 16899666", "mw": "399.49", "pi": "11.0", "charge_ph7": "1.76", "gravy": "-3.3333", "instability": "70.87", "hydrophobic": "0.3333", "boman": "1.4333", "helix": "0.3333", "turn_pct": "0.3333", "sheet": "0.0" }, { "id": "aceip0890", "seq": "RPKH", "length": "4", "detail": "Sesame", "source": "Plants", "ic50": ">1863 μM", "reference": "Angiotensin I-converting-enzyme-inhibitory and antibacterial peptides from Lactobacillus helveticus PR4 proteinase-hydrolyzed caseins of milk from six species.", "doi": "10.1128\/AEM.69.9.5297-5305.2003", "pubmedid": "12957917", "mw": "536.63", "pi": "11.0", "charge_ph7": "1.85", "gravy": "-3.3", "instability": "55.65", "hydrophobic": "0.25", "boman": "1.3225", "helix": "0.25", "turn_pct": "0.25", "sheet": "0.0" }, { "id": "aceip0891", "seq": "RPKHP", "length": "5", "detail": "Milk (bovine)", "source": "Milk", "ic50": null, "reference": "Enterococcus faecalis strains from food, environmental, and clinical origin produce ACE-inhibitory peptides and other bioactive peptides during growth in bovine skim milk.", "doi": "10.1016\/j.ijfoodmicro.2013.06.019", "pubmedid": "23845432", "mw": "633.74", "pi": "11.0", "charge_ph7": "1.85", "gravy": "-2.96", "instability": "40.76", "hydrophobic": "0.4", "boman": "1.058", "helix": "0.2", "turn_pct": "0.4", "sheet": "0.0" }, { "id": "aceip0892", "seq": "RPKHPI", "length": "6", "detail": "Cereals (Maize)", "source": "Cereal", "ic50": "40.3 μM", "reference": "Angiotensin I-converting-enzyme-inhibitory and antibacterial peptides from Lactobacillus helveticus PR4 proteinase-hydrolyzed caseins of milk from six species.; Identification of angiotensin-I-converting enzyme inhibitory peptides derived from sodium caseinate hydrolysates produced by Lactobacillus helveticus NCC 2765.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1128\/AEM.69.9.5297-5305.2003; 10.1021\/jf049510t; 10.1016\/j.foodchem.2012.09.092", "pubmedid": "12957917 15537298 23194537", "mw": "746.9", "pi": "11.0", "charge_ph7": "1.85", "gravy": "-1.7167", "instability": "35.63", "hydrophobic": "0.5", "boman": "0.0617", "helix": "0.1667", "turn_pct": "0.3333", "sheet": "0.1667" }, { "id": "aceip0893", "seq": "RPKHPIKH", "length": "8", "detail": "Fungi (Hypsizygus marmoreus)", "source": "Fungi", "ic50": "892.83 mg\/ml", "reference": "Bioactive peptides in ovine and caprine cheeselike systems prepared with proteases from Cynara cardunculus.", "doi": "10.3168\/jds.S0022-0302(06)72370-0", "pubmedid": "16899666", "mw": "1012.21", "pi": "11.17", "charge_ph7": "2.93", "gravy": "-2.175", "instability": "18.61", "hydrophobic": "0.375", "boman": "0.3675", "helix": "0.25", "turn_pct": "0.25", "sheet": "0.125" }, { "id": "aceip0894", "seq": "RPKHPIKHQ", "length": "9", "detail": "Milk | Amaranth | Cereals (Maize)", "source": "Milk | Plants | Cereal", "ic50": "13 μM", "reference": "Isolation and structural analysis of antihypertensive peptides that exist naturally in Gouda cheese.; Identification of angiotensin-I-converting enzyme inhibitory peptides derived from sodium caseinate hydrolysates produced by Lactobacillus helveticus NCC 2765.; QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.; Antihypertensive peptides: production, bioavailability and incorporation into foods.; Antihypertensive peptides from food proteins: a review.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.3168\/jds.S0022-0302(00)75013-2; 10.1021\/jf049510t; 10.1007\/s00894-010-0862-x; 10.1016\/j.cis.2010.11.001; 10.1039\/c2fo10192k; 10.1016\/j.foodchem.2012.09.092; 10.1080\/10408398.2012.664829", "pubmedid": "10908049 15537298 20941517 21185549 22249830 23194537 24915368", "mw": "1140.34", "pi": "11.17", "charge_ph7": "2.93", "gravy": "-2.3222", "instability": "17.66", "hydrophobic": "0.3333", "boman": "0.4778", "helix": "0.2222", "turn_pct": "0.2222", "sheet": "0.1111" }, { "id": "aceip0895", "seq": "RPKHPIKHQGLPQ", "length": "13", "detail": "Cereals (Maize)", "source": "Cereal", "ic50": null, "reference": "Isolation and structural analysis of antihypertensive peptides that exist naturally in Gouda cheese.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.3168\/jds.S0022-0302(00)75013-2; 10.1080\/10408398.2012.664829", "pubmedid": "10908049 24915368", "mw": "1535.79", "pi": "11.17", "charge_ph7": "2.93", "gravy": "-1.7385", "instability": "44.93", "hydrophobic": "0.3846", "boman": "-0.0154", "helix": "0.2308", "turn_pct": "0.3077", "sheet": "0.1538" }, { "id": "aceip0896", "seq": "RPP", "length": "3", "detail": "Cereals (Maize)", "source": "Cereal", "ic50": "<20 mM", "reference": "Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.", "doi": "10.1021\/jf051263l", "pubmedid": "16448176", "mw": "368.43", "pi": "9.75", "charge_ph7": "0.76", "gravy": "-2.5667", "instability": "135.07", "hydrophobic": "0.6667", "boman": "0.9067", "helix": "0.0", "turn_pct": "0.6667", "sheet": "0.0" }, { "id": "aceip0897", "seq": "RPQIPP", "length": "6", "detail": "Cereals (Maize) | alpha-zein", "source": "Cereal", "ic50": "166 μM", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "23194537", "mw": "706.83", "pi": "9.75", "charge_ph7": "0.76", "gravy": "-1.3833", "instability": "99.83", "hydrophobic": "0.6667", "boman": "-0.14", "helix": "0.0", "turn_pct": "0.5", "sheet": "0.1667" }, { "id": "aceip0898", "seq": "RPR", "length": "3", "detail": "Milk (bovine)", "source": "Milk", "ic50": "382 μM", "reference": "Angiotensin I-converting enzyme inhibitory peptides generated from in vitro gastrointestinal digestion of pork meat.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1021\/jf904204n; 10.1016\/j.foodchem.2013.05.140; 10.1080\/10408398.2012.664829", "pubmedid": "20151679 23871047 24915368", "mw": "427.5", "pi": "12.0", "charge_ph7": "1.76", "gravy": "-3.5333", "instability": "45.73", "hydrophobic": "0.3333", "boman": "1.8133", "helix": "0.0", "turn_pct": "0.3333", "sheet": "0.0" }, { "id": "aceip0899", "seq": "RR", "length": "2", "detail": "Legume (Pea proteins)", "source": "Legume", "ic50": "267.1 μM", "reference": "Quantitative structure-activity relationship study of bitter di- and tri-peptides including relationship with angiotensin I-converting enzyme inhibitory activity.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1002\/psc.800; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "17117396 23871047", "mw": "330.39", "pi": "12.0", "charge_ph7": "1.76", "gravy": "-4.5", "instability": "291.4", "hydrophobic": "0.0", "boman": "2.72", "helix": "0.0", "turn_pct": "0.0", "sheet": "0.0" }, { "id": "aceip0900", "seq": "RRR", "length": "3", "detail": "ND", "source": "ND", "ic50": null, "reference": "Quantitative structure-activity relationship study of bitter di- and tri-peptides including relationship with angiotensin I-converting enzyme inhibitory activity.; QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1002\/psc.800; 10.1007\/s00894-010-0862-x; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "17117396 20941517 23871047", "mw": "486.57", "pi": "12.0", "charge_ph7": "2.76", "gravy": "-4.5", "instability": "388.53", "hydrophobic": "0.0", "boman": "2.72", "helix": "0.0", "turn_pct": "0.0", "sheet": "0.0" }, { "id": "aceip0901", "seq": "RRWQWR", "length": "6", "detail": "Soybean", "source": "Legume", "ic50": null, "reference": "Antihypertensive peptides from food proteins: a review.", "doi": "10.1039\/c2fo10192k", "pubmedid": "22249830", "mw": "987.12", "pi": "12.0", "charge_ph7": "2.76", "gravy": "-3.1333", "instability": "199.27", "hydrophobic": "0.3333", "boman": "0.81", "helix": "0.0", "turn_pct": "0.0", "sheet": "0.3333" }, { "id": "aceip0902", "seq": "RVAPEEHPT", "length": "9", "detail": "Milk", "source": "Milk", "ic50": null, "reference": "Angiotensin I-converting enzyme inhibitory peptides generated from in vitro gastrointestinal digestion of pork meat.", "doi": "10.1021\/jf904204n", "pubmedid": "20151679", "mw": "1035.11", "pi": "5.4", "charge_ph7": "-1.15", "gravy": "-1.4", "instability": "74.24", "hydrophobic": "0.4444", "boman": "0.1556", "helix": "0.3333", "turn_pct": "0.2222", "sheet": "0.2222" }, { "id": "aceip0903", "seq": "RVY", "length": "3", "detail": "Milk (human)", "source": "Milk", "ic50": "<20 mM", "reference": "Angiotensin I-converting enzyme inhibitory peptides in an alkaline protease hydrolyzate derived from sardine muscle.; Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Review on the angiotensin-I-converting enzyme (ACE) inhibitor peptides from marine proteins.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1271\/bbb.58.2244; 10.1021\/jf051263l; 10.1007\/s12010-012-0024-y; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "7765718 16448176 23271625 23871047", "mw": "436.51", "pi": "8.75", "charge_ph7": "0.76", "gravy": "-0.5333", "instability": "-18.47", "hydrophobic": "0.3333", "boman": "-0.3933", "helix": "0.0", "turn_pct": "0.0", "sheet": "0.6667" }, { "id": "aceip0904", "seq": "RW", "length": "2", "detail": "Milk (bovine)", "source": "Milk", "ic50": "<10 μM", "reference": "Binding of peptide substrates and inhibitors of angiotensin-converting enzyme. Importance of the COOH-terminal dipeptide sequence.; Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Three-dimensional holograph vector of atomic interaction field (3D-HoVAIF): a novel rotation-translation invariant 3D structure descriptor and its applications to peptides.; QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.; Inhibition strength of short peptides derived from an ACE inhibitory peptide.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1021\/jf051263l; 10.1002\/psc.892; 10.1007\/s00894-010-0862-x; 10.1021\/jf202902r; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "6243277 16448176 17654623 20941517 21923188 23871047", "mw": "360.41", "pi": "9.75", "charge_ph7": "0.76", "gravy": "-2.7", "instability": "291.4", "hydrophobic": "0.5", "boman": "0.195", "helix": "0.0", "turn_pct": "0.0", "sheet": "0.5" }, { "id": "aceip0905", "seq": "RY", "length": "2", "detail": "Royal jelly | Tuna | Cereals | Chicken", "source": "Insect | Fish | Cereal | Chicken", "ic50": "<20 mM", "reference": "Angiotensin I-converting enzyme inhibitory peptides in an alkaline protease hydrolyzate derived from sardine muscle.; Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Bioactive peptides in amaranth (Amaranthus hypochondriacus) seed.; Review on the angiotensin-I-converting enzyme (ACE) inhibitor peptides from marine proteins.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1271\/bbb.58.2244; 10.1021\/jf051263l; 10.1021\/jf072911z; 10.1007\/s12010-012-0024-y; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "7765718 16448176 18211015 23271625 23871047", "mw": "337.37", "pi": "8.75", "charge_ph7": "0.76", "gravy": "-2.9", "instability": "-32.7", "hydrophobic": "0.0", "boman": "1.43", "helix": "0.0", "turn_pct": "0.0", "sheet": "0.5" }, { "id": "aceip0906", "seq": "RYLGY", "length": "5", "detail": "Casein", "source": "Milk", "ic50": "0.71 μM", "reference": "Antihypertensive peptides: production, bioavailability and incorporation into foods.; Antihypertensive peptides from food proteins: a review.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.; Glycinyl-histidinyl-serine (GHS), a novel rapeseed protein-derived peptide has blood pressure-lowering effect in spontaneously hypertensive rats.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1016\/j.cis.2010.11.001; 10.1039\/c2fo10192k; 10.1016\/j.foodchem.2012.09.092; 10.1021\/jf400865m; 10.1080\/10408398.2012.664829", "pubmedid": "21185549 22249830 23194537 23919612 24915368", "mw": "670.76", "pi": "8.59", "charge_ph7": "0.76", "gravy": "-0.74", "instability": "-24.06", "hydrophobic": "0.2", "boman": "-0.572", "helix": "0.2", "turn_pct": "0.2", "sheet": "0.6" }, { "id": "aceip0907", "seq": "RYPSYG", "length": "6", "detail": "Milk (bovine)", "source": "Milk", "ic50": null, "reference": "Antihypertensive peptides from food proteins: a review.", "doi": "10.1039\/c2fo10192k", "pubmedid": "22249830", "mw": "741.79", "pi": "8.59", "charge_ph7": "0.76", "gravy": "-1.65", "instability": "34.28", "hydrophobic": "0.1667", "boman": "0.4833", "helix": "0.0", "turn_pct": "0.5", "sheet": "0.3333" }, { "id": "aceip0908", "seq": "SF", "length": "2", "detail": "ND", "source": "ND", "ic50": "<20 mM", "reference": "Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Max-E47, a designed minimalist protein that targets the E-box DNA site in vivo and in vitro.; Vegetable foods: a cheap source of proteins and peptides with antihypertensive, antioxidant, and other less occurrence bioactivities.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1021\/jf051263l; 10.1021\/ja901306q; 10.1016\/j.talanta.2012.12.041; 10.1016\/j.foodchem.2013.05.140; 10.1080\/10408398.2012.664829", "pubmedid": "16448176 19449889 23598136 23871047 24915368", "mw": "252.27", "pi": "5.24", "charge_ph7": "-0.54", "gravy": "1.0", "instability": "5.0", "hydrophobic": "0.5", "boman": "-1.07", "helix": "0.0", "turn_pct": "0.5", "sheet": "0.5" }, { "id": "aceip0909", "seq": "SFQPQPLIYP", "length": "10", "detail": "Milk", "source": "Milk", "ic50": "1.4 μM", "reference": "Inhibition of angiotensin-converting enzyme by synthetic peptide fragments of various beta-caseins.", "doi": "", "pubmedid": "1368548", "mw": "1189.36", "pi": "5.24", "charge_ph7": "-0.54", "gravy": "-0.28", "instability": "79.12", "hydrophobic": "0.6", "boman": "-0.912", "helix": "0.1", "turn_pct": "0.4", "sheet": "0.4" }, { "id": "aceip0910", "seq": "SG", "length": "2", "detail": "Milk", "source": "Milk", "ic50": "<20 mM", "reference": "Binding of peptide substrates and inhibitors of angiotensin-converting enzyme. Importance of the COOH-terminal dipeptide sequence.; Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Three-dimensional holograph vector of atomic interaction field (3D-HoVAIF): a novel rotation-translation invariant 3D structure descriptor and its applications to peptides.; Model of the exofacial substrate-binding site and helical folding of the human Glut1 glucose transporter based on scanning mutagenesis.; QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.; Peptides with angiotensin I converting enzyme (ACE) inhibitory activity generated from porcine skeletal muscle proteins by the action of meat-borne Lactobacillus.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1021\/jf051263l; 10.1002\/psc.892; 10.1021\/bi900521n; 10.1007\/s00894-010-0862-x; 10.1016\/j.jprot.2013.06.023; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "6243277 16448176 17654623 19449892 20941517 23806758 23871047", "mw": "162.14", "pi": "5.24", "charge_ph7": "-0.54", "gravy": "-0.6", "instability": "5.0", "hydrophobic": "0.0", "boman": "-0.05", "helix": "0.0", "turn_pct": "1.0", "sheet": "0.0" }, { "id": "aceip0911", "seq": "SHP", "length": "3", "detail": "ND", "source": "ND", "ic50": "280 μM", "reference": "Inhibition of angiotensin-converting enzyme by synthetic peptide fragments of human kappa-casein.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1016\/j.foodchem.2013.05.140", "pubmedid": "1368540 23871047", "mw": "339.35", "pi": "6.46", "charge_ph7": "-0.45", "gravy": "-1.8667", "instability": "-2.93", "hydrophobic": "0.3333", "boman": "0.61", "helix": "0.0", "turn_pct": "0.6667", "sheet": "0.0" }, { "id": "aceip0912", "seq": "SKVLPVPE", "length": "8", "detail": "Bulfrog | Cereals", "source": "Amphibian | Cereal", "ic50": "0 μM", "reference": "Antihypertensive effect of the peptides derived from casein by an extracellular proteinase from Lactobacillus helveticus CP790.", "doi": "10.3168\/jds.S0022-0302(94)77026-0", "pubmedid": "8201050", "mw": "868.03", "pi": "5.94", "charge_ph7": "-0.53", "gravy": "0.1", "instability": "92.09", "hydrophobic": "0.625", "boman": "-1.1175", "helix": "0.375", "turn_pct": "0.375", "sheet": "0.375" }, { "id": "aceip0913", "seq": "SKVLPVPQ", "length": "8", "detail": "Milk (bovine) | Amaranth | Cereals (Wheat) | Porcine | Chicken connectin", "source": "Milk | Plants | Cereal | Porcine | Chicken", "ic50": null, "reference": "Identification of angiotensin-I-converting enzyme inhibitory peptides derived from sodium caseinate hydrolysates produced by Lactobacillus helveticus NCC 2765.", "doi": "10.1021\/jf049510t", "pubmedid": "15537298", "mw": "867.04", "pi": "8.47", "charge_ph7": "0.46", "gravy": "0.1", "instability": "94.44", "hydrophobic": "0.625", "boman": "-1.1525", "helix": "0.25", "turn_pct": "0.375", "sheet": "0.375" }, { "id": "aceip0914", "seq": "SKVLPVPQK", "length": "9", "detail": "Mushroom", "source": "Fungi", "ic50": null, "reference": "Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1080\/10408398.2012.664829", "pubmedid": "24915368", "mw": "995.22", "pi": "10.0", "charge_ph7": "1.46", "gravy": "-0.3444", "instability": "85.06", "hydrophobic": "0.5556", "boman": "-0.8489", "helix": "0.3333", "turn_pct": "0.3333", "sheet": "0.3333" }, { "id": "aceip0915", "seq": "SKVPP", "length": "5", "detail": "Milk | Cereals (Maize) | Legume (Pea proteins)", "source": "Milk | Cereal | Legume", "ic50": "74.13 μM", "reference": "Effects of angiotensin I-converting enzyme inhibitory substances derived from Indonesian dried-salted fish on blood pressure of rats.", "doi": "10.1271\/bbb.59.425", "pubmedid": "7766180", "mw": "526.63", "pi": "8.47", "charge_ph7": "0.46", "gravy": "-0.74", "instability": "68.06", "hydrophobic": "0.6", "boman": "-0.324", "helix": "0.2", "turn_pct": "0.6", "sheet": "0.2" }, { "id": "aceip0916", "seq": "SKVYP", "length": "5", "detail": "ND", "source": "ND", "ic50": "1.4 μM", "reference": "Technological options for the production of health-promoting proteins and peptides derived from milk and colostrum.; Antihypertensive peptides: production, bioavailability and incorporation into foods.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.; The impact of milk proteins and peptides on blood pressure and vascular function: a review of evidence from human intervention studies.", "doi": "10.2174\/138161207780363112; 10.1016\/j.cis.2010.11.001; 10.1016\/j.foodchem.2012.09.092; 10.1017\/S0954422413000139", "pubmedid": "17430184 21185549 23194537 24135454", "mw": "592.68", "pi": "8.31", "charge_ph7": "0.46", "gravy": "-0.68", "instability": "0.62", "hydrophobic": "0.4", "boman": "-0.296", "helix": "0.2", "turn_pct": "0.4", "sheet": "0.4" }, { "id": "aceip0917", "seq": "SKVYPFPGPI", "length": "10", "detail": "Soybean (Fermented)", "source": "Legume", "ic50": "1.7 mg\/ml", "reference": "Technological options for the production of health-promoting proteins and peptides derived from milk and colostrum.", "doi": "10.2174\/138161207780363112", "pubmedid": "17430184", "mw": "1104.3", "pi": "8.31", "charge_ph7": "0.46", "gravy": "0.03", "instability": "43.83", "hydrophobic": "0.6", "boman": "-1.032", "helix": "0.1", "turn_pct": "0.5", "sheet": "0.4" }, { "id": "aceip0918", "seq": "SL", "length": "2", "detail": "Cereals (Maize) | Chicken connectin", "source": "Cereal | Chicken", "ic50": null, "reference": "Three-dimensional holograph vector of atomic interaction field (3D-HoVAIF): a novel rotation-translation invariant 3D structure descriptor and its applications to peptides.", "doi": "10.1002\/psc.892", "pubmedid": "17654623", "mw": "218.25", "pi": "5.24", "charge_ph7": "-0.54", "gravy": "1.5", "instability": "5.0", "hydrophobic": "0.5", "boman": "-2.04", "helix": "0.5", "turn_pct": "0.5", "sheet": "0.5" }, { "id": "aceip0919", "seq": "SLPQ", "length": "4", "detail": "Milk (caprine)", "source": "Milk", "ic50": "330 μM", "reference": "Identification and characterization of novel angiotensin-converting enzyme inhibitors obtained from goat milk.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.3168\/jds.S0022-0302(06)72369-4; 10.1016\/j.foodchem.2013.05.140; 10.1080\/10408398.2012.664829", "pubmedid": "16899665 23871047 24915368", "mw": "443.49", "pi": "5.24", "charge_ph7": "-0.54", "gravy": "-0.525", "instability": "103.8", "hydrophobic": "0.5", "boman": "-0.68", "helix": "0.25", "turn_pct": "0.5", "sheet": "0.25" }, { "id": "aceip0920", "seq": "SLVLPVPE", "length": "8", "detail": "Milk (whey)", "source": "Milk", "ic50": "39 μM", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "23194537", "mw": "853.01", "pi": "4.6", "charge_ph7": "-1.53", "gravy": "1.0625", "instability": "102.7", "hydrophobic": "0.75", "boman": "-1.93", "helix": "0.375", "turn_pct": "0.375", "sheet": "0.5" }, { "id": "aceip0921", "seq": "SLVYP", "length": "5", "detail": "Hemoglobulin", "source": "Synthesized", "ic50": "40 μM", "reference": "Inhibition of angiotensin-converting enzyme by synthetic peptide fragments of various beta-caseins.; Evaluation of the allergenicity of goat milk, cow milk, and their lactosera in a guinea pig model.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.3168\/jds.2008-1125; 10.1016\/j.foodchem.2012.09.092", "pubmedid": "1368548 19233776 23194537", "mw": "577.67", "pi": "5.24", "charge_ph7": "-0.54", "gravy": "0.86", "instability": "17.6", "hydrophobic": "0.6", "boman": "-1.596", "helix": "0.2", "turn_pct": "0.4", "sheet": "0.6" }, { "id": "aceip0922", "seq": "SPPPFYL", "length": "7", "detail": "Milk (Fermented Milk) | Sesame", "source": "Milk | Plants", "ic50": "63.1 μM", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "23194537", "mw": "819.94", "pi": "5.24", "charge_ph7": "-0.54", "gravy": "-0.0429", "instability": "200.46", "hydrophobic": "0.7143", "boman": "-0.9886", "helix": "0.1429", "turn_pct": "0.5714", "sheet": "0.4286" }, { "id": "aceip0923", "seq": "SPYP", "length": "4", "detail": "Milk (bovine, buffalo and ovine)", "source": "Milk", "ic50": "850 μM", "reference": "What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1016\/j.foodchem.2013.05.140", "pubmedid": "23871047", "mw": "462.5", "pi": "5.24", "charge_ph7": "-0.54", "gravy": "-1.325", "instability": "148.2", "hydrophobic": "0.5", "boman": "0.245", "helix": "0.0", "turn_pct": "0.75", "sheet": "0.25" }, { "id": "aceip0924", "seq": "SQPK", "length": "4", "detail": "ND", "source": "ND", "ic50": "354 μM", "reference": "Identification and characterization of novel angiotensin-converting enzyme inhibitors obtained from goat milk.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.3168\/jds.S0022-0302(06)72369-4; 10.1016\/j.foodchem.2013.05.140; 10.1080\/10408398.2012.664829", "pubmedid": "16899665 23871047 24915368", "mw": "458.51", "pi": "8.47", "charge_ph7": "0.46", "gravy": "-2.45", "instability": "103.8", "hydrophobic": "0.25", "boman": "0.945", "helix": "0.25", "turn_pct": "0.5", "sheet": "0.0" }, { "id": "aceip0925", "seq": "SQSKVLPVPQ", "length": "10", "detail": "Milk (Casein) | Milk-Cheese (Goat milk protein and cheeses)", "source": "Milk", "ic50": "92 μM", "reference": "Casein fermentate of Lactobacillus animalis DPC6134 contains a range of novel propeptide angiotensin-converting enzyme inhibitors.", "doi": "10.1128\/AEM.00096-07", "pubmedid": "17483275", "mw": "1082.25", "pi": "8.47", "charge_ph7": "0.46", "gravy": "-0.35", "instability": "140.75", "hydrophobic": "0.5", "boman": "-0.702", "helix": "0.2", "turn_pct": "0.4", "sheet": "0.3" }, { "id": "aceip0926", "seq": "SSIQSQPQAFT", "length": "11", "detail": "Milk (Casein)", "source": "Milk", "ic50": "1001 μM", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "23194537", "mw": "1193.26", "pi": "5.24", "charge_ph7": "-0.54", "gravy": "-0.5545", "instability": "119.07", "hydrophobic": "0.3636", "boman": "-0.2591", "helix": "0.0909", "turn_pct": "0.3636", "sheet": "0.2727" }, { "id": "aceip0927", "seq": "ST", "length": "2", "detail": "Milk (Fermented Milk)", "source": "Milk", "ic50": "4.03 μM", "reference": "Review on the angiotensin-I-converting enzyme (ACE) inhibitor peptides from marine proteins.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1007\/s12010-012-0024-y; 10.1080\/10408398.2012.664829", "pubmedid": "23271625 24915368", "mw": "206.2", "pi": "5.24", "charge_ph7": "-0.54", "gravy": "-0.75", "instability": "5.0", "hydrophobic": "0.0", "boman": "0.55", "helix": "0.0", "turn_pct": "0.5", "sheet": "0.5" }, { "id": "aceip0928", "seq": "SVAKL", "length": "5", "detail": "Milk (Fermented Milk)", "source": "Milk", "ic50": "891.25 μM", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "23194537", "mw": "516.63", "pi": "8.47", "charge_ph7": "0.46", "gravy": "1.02", "instability": "-8.98", "hydrophobic": "0.6", "boman": "-1.67", "helix": "0.6", "turn_pct": "0.2", "sheet": "0.4" }, { "id": "aceip0929", "seq": "SVAKLE", "length": "6", "detail": "Milk", "source": "Milk", "ic50": "2187.76 μM", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "23194537", "mw": "645.75", "pi": "5.94", "charge_ph7": "-0.53", "gravy": "0.2667", "instability": "-5.82", "hydrophobic": "0.5", "boman": "-1.1183", "helix": "0.6667", "turn_pct": "0.1667", "sheet": "0.3333" }, { "id": "aceip0930", "seq": "SVAKLEK", "length": "7", "detail": "Milk (Fermented Milk)", "source": "Milk", "ic50": "82 μM", "reference": "Isolation and characterization of angiotensin I-converting enzyme inhibitory peptides derived from bonito bowels.", "doi": "10.1271\/bbb.57.1743", "pubmedid": "7764272", "mw": "773.92", "pi": "8.31", "charge_ph7": "0.46", "gravy": "-0.3286", "instability": "-3.56", "hydrophobic": "0.4286", "boman": "-0.7329", "helix": "0.7143", "turn_pct": "0.1429", "sheet": "0.2857" }, { "id": "aceip0931", "seq": "SVY", "length": "3", "detail": "Milk (bovine) | Casein | Milk (Casein) | Milk (Fermented Milk)", "source": "Milk", "ic50": "<20 mM", "reference": "Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.", "doi": "10.1021\/jf051263l", "pubmedid": "16448176", "mw": "367.4", "pi": "5.24", "charge_ph7": "-0.54", "gravy": "0.7", "instability": "-18.47", "hydrophobic": "0.3333", "boman": "-1.02", "helix": "0.0", "turn_pct": "0.3333", "sheet": "0.6667" }, { "id": "aceip0932", "seq": "SWSF", "length": "4", "detail": "Casein | Milk-Cheese (Goat milk protein and cheeses) | Milk (Caprine Kefir) | Egg (Ovalbumin)", "source": "Milk | Egg", "ic50": "76.3 μM", "reference": "Vegetable foods: a cheap source of proteins and peptides with antihypertensive, antioxidant, and other less occurrence bioactivities.", "doi": "10.1016\/j.talanta.2012.12.041", "pubmedid": "23598136", "mw": "525.55", "pi": "5.24", "charge_ph7": "-0.54", "gravy": "0.075", "instability": "7.5", "hydrophobic": "0.5", "boman": "-0.9075", "helix": "0.0", "turn_pct": "0.5", "sheet": "0.5" }, { "id": "aceip0933", "seq": "SY", "length": "2", "detail": "Milk (bovine) | Milk (Casein) | Amaranth | Wakame | Salmon | Cereals (Wheat) | Soybean | Egg (Ovalbumin) | Meat", "source": "Milk | Plants | Fish | Cereal | Legume | Egg | Meat", "ic50": "<20 mM", "reference": "Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Max-E47, a designed minimalist protein that targets the E-box DNA site in vivo and in vitro.; Antihypertensive effect of peptide-enriched soy sauce-like seasoning and identification of its angiotensin I-converting enzyme inhibitory substances.; Vegetable foods: a cheap source of proteins and peptides with antihypertensive, antioxidant, and other less occurrence bioactivities.; Peptides with angiotensin I converting enzyme (ACE) inhibitory activity generated from porcine skeletal muscle proteins by the action of meat-borne Lactobacillus.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1021\/jf051263l; 10.1021\/ja901306q; 10.1021\/jf903261h; 10.1016\/j.talanta.2012.12.041; 10.1016\/j.jprot.2013.06.023; 10.1016\/j.foodchem.2013.05.140; 10.1080\/10408398.2012.664829", "pubmedid": "16448176 19449889 19994857 23598136 23806758 23871047 24915368", "mw": "268.27", "pi": "5.24", "charge_ph7": "-0.54", "gravy": "-1.05", "instability": "5.0", "hydrophobic": "0.0", "boman": "0.49", "helix": "0.0", "turn_pct": "0.5", "sheet": "0.5" }, { "id": "aceip0934", "seq": "TAP", "length": "3", "detail": "ND", "source": "ND", "ic50": "<20 mM", "reference": "Inhibition of angiotensin-converting enzyme by synthetic peptide fragments of human kappa-casein.; Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Bioactive peptides in amaranth (Amaranthus hypochondriacus) seed.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1021\/jf051263l; 10.1021\/jf072911z; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "1368540 16448176 18211015 23871047", "mw": "287.31", "pi": "5.18", "charge_ph7": "-0.6", "gravy": "-0.1667", "instability": "70.87", "hydrophobic": "0.6667", "boman": "-0.5167", "helix": "0.3333", "turn_pct": "0.3333", "sheet": "0.3333" }, { "id": "aceip0935", "seq": "TAPY", "length": "4", "detail": "Milk (bovine) | Amaranth | Rapeseed | Sardine | Cereals (Maize) | pea | Pork | Egg (Ovalbumin)", "source": "Milk | Plants | Fish | Cereal | Legume | Porcine | Egg", "ic50": null, "reference": "Preparation and characterization of novel bioactive peptides responsible for angiotensin I-converting enzyme inhibition from wheat germ.", "doi": "10.1002\/(SICI)1099-1387(199907)5:7<289::AID-PSC196>3.0.CO;2-6", "pubmedid": "10442764", "mw": "450.49", "pi": "5.18", "charge_ph7": "-0.6", "gravy": "-0.45", "instability": "55.65", "hydrophobic": "0.5", "boman": "-0.3525", "helix": "0.25", "turn_pct": "0.25", "sheet": "0.5" }, { "id": "aceip0936", "seq": "TAQVTSTEV", "length": "9", "detail": "Soybean", "source": "Legume", "ic50": null, "reference": "Sheep kappa-casein peptides inhibit platelet aggregation.", "doi": "10.1016\/0304-4165(95)00047-f", "pubmedid": "7599162", "mw": "934.99", "pi": "4.05", "charge_ph7": "-1.6", "gravy": "0.0333", "instability": "12.48", "hydrophobic": "0.3333", "boman": "-0.5856", "helix": "0.2222", "turn_pct": "0.1111", "sheet": "0.5556" }, { "id": "aceip0937", "seq": "TCSP", "length": "4", "detail": "Synthesized | Fish | Cereals (Finnish)", "source": "Synthesized | Fish | Cereal", "ic50": "68.00 %", "reference": "Free radical scavenging and angiotensin-I converting enzyme inhibitory peptides from Pacific cod (Gadus macrocephalus) skin gelatin.", "doi": "10.1016\/j.ijbiomac.2011.09.009", "pubmedid": "21945677", "mw": "406.45", "pi": "5.18", "charge_ph7": "-0.61", "gravy": "-0.15", "instability": "117.35", "hydrophobic": "0.25", "boman": "-0.045", "helix": "0.0", "turn_pct": "0.5", "sheet": "0.25" }, { "id": "aceip0938", "seq": "TDQHQDKIYP", "length": "10", "detail": "ND", "source": "ND", "ic50": "380 μM", "reference": "Inhibition of angiotensin-converting enzyme by synthetic peptide fragments of various beta-caseins.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "1368548 23194537", "mw": "1244.31", "pi": "5.18", "charge_ph7": "-1.51", "gravy": "-2.02", "instability": "23.62", "hydrophobic": "0.2", "boman": "0.413", "helix": "0.1", "turn_pct": "0.3", "sheet": "0.3" }, { "id": "aceip0939", "seq": "TE", "length": "2", "detail": "Soybean", "source": "Legume", "ic50": "0 0", "reference": "Application of at-line two-dimensional liquid chromatography-mass spectrometry for identification of small hydrophilic angiotensin I-inhibiting peptides in milk hydrolysates.; Peptides with angiotensin I converting enzyme (ACE) inhibitory activity generated from porcine skeletal muscle proteins by the action of meat-borne Lactobacillus.", "doi": "10.1007\/s00216-008-1990-3; 10.1016\/j.jprot.2013.06.023", "pubmedid": "18392815 23806758", "mw": "248.23", "pi": "4.59", "charge_ph7": "-1.59", "gravy": "-2.1", "instability": "101.3", "hydrophobic": "0.0", "boman": "0.95", "helix": "0.5", "turn_pct": "0.0", "sheet": "0.5" }, { "id": "aceip0940", "seq": "TEDELQDKIHP", "length": "11", "detail": "Meat", "source": "Meat", "ic50": null, "reference": "Casein fermentate of Lactobacillus animalis DPC6134 contains a range of novel propeptide angiotensin-converting enzyme inhibitors.", "doi": "10.1128\/AEM.00096-07", "pubmedid": "17483275", "mw": "1324.39", "pi": "4.31", "charge_ph7": "-3.51", "gravy": "-1.6909", "instability": "84.42", "hydrophobic": "0.2727", "boman": "0.09", "helix": "0.3636", "turn_pct": "0.2727", "sheet": "0.2727" }, { "id": "aceip0941", "seq": "TF", "length": "2", "detail": "Soybean | Legume (Pea proteins)", "source": "Legume", "ic50": "<20 mM", "reference": "Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Angiotensin I converting enzyme inhibitory peptides produced by autolysis reactions from wheat bran.; Vegetable foods: a cheap source of proteins and peptides with antihypertensive, antioxidant, and other less occurrence bioactivities.; Peptides with angiotensin I converting enzyme (ACE) inhibitory activity generated from porcine skeletal muscle proteins by the action of meat-borne Lactobacillus.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.; Glycinyl-histidinyl-serine (GHS), a novel rapeseed protein-derived peptide has blood pressure-lowering effect in spontaneously hypertensive rats.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1021\/jf051263l; 10.1021\/jf900857w; 10.1016\/j.talanta.2012.12.041; 10.1016\/j.jprot.2013.06.023; 10.1016\/j.foodchem.2013.05.140; 10.1021\/jf400865m; 10.1080\/10408398.2012.664829", "pubmedid": "16448176 19572648 23598136 23806758 23871047 23919612 24915368", "mw": "266.29", "pi": "5.18", "charge_ph7": "-0.6", "gravy": "1.05", "instability": "66.7", "hydrophobic": "0.5", "boman": "-1.36", "helix": "0.0", "turn_pct": "0.0", "sheet": "1.0" }, { "id": "aceip0942", "seq": "TFPHGP", "length": "6", "detail": "Milk", "source": "Milk", "ic50": "0.068 mg\/ml", "reference": "Review on the angiotensin-I-converting enzyme (ACE) inhibitor peptides from marine proteins.", "doi": "10.1007\/s12010-012-0024-y", "pubmedid": "23271625", "mw": "654.71", "pi": "6.4", "charge_ph7": "-0.51", "gravy": "-0.7833", "instability": "43.72", "hydrophobic": "0.5", "boman": "-0.445", "helix": "0.0", "turn_pct": "0.5", "sheet": "0.3333" }, { "id": "aceip0943", "seq": "TG", "length": "2", "detail": "Prince-of-Wales feather", "source": "Plants", "ic50": "<20 mM", "reference": "Binding of peptide substrates and inhibitors of angiotensin-converting enzyme. Importance of the COOH-terminal dipeptide sequence.; Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Three-dimensional holograph vector of atomic interaction field (3D-HoVAIF): a novel rotation-translation invariant 3D structure descriptor and its applications to peptides.; QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.; Peptides with angiotensin I converting enzyme (ACE) inhibitory activity generated from porcine skeletal muscle proteins by the action of meat-borne Lactobacillus.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1021\/jf051263l; 10.1002\/psc.892; 10.1007\/s00894-010-0862-x; 10.1016\/j.jprot.2013.06.023; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "6243277 16448176 17654623 20941517 23806758 23871047", "mw": "176.17", "pi": "5.18", "charge_ph7": "-0.6", "gravy": "-0.55", "instability": "-37.45", "hydrophobic": "0.0", "boman": "-0.34", "helix": "0.0", "turn_pct": "0.5", "sheet": "0.5" }, { "id": "aceip0944", "seq": "TGGGNV", "length": "6", "detail": "Milk-Cheese (Goat milk protein and cheeses) | Milk-Cheese (Sheep milk and cheeses proteins)", "source": "Milk", "ic50": "68.00 %", "reference": "Free radical scavenging and angiotensin-I converting enzyme inhibitory peptides from Pacific cod (Gadus macrocephalus) skin gelatin.", "doi": "10.1016\/j.ijbiomac.2011.09.009", "pubmedid": "21945677", "mw": "503.51", "pi": "5.18", "charge_ph7": "-0.6", "gravy": "-0.2", "instability": "21.17", "hydrophobic": "0.1667", "boman": "-0.83", "helix": "0.0", "turn_pct": "0.6667", "sheet": "0.3333" }, { "id": "aceip0945", "seq": "TGPIPN", "length": "6", "detail": "Milk (bovine) | Casein | Milk-Cheese (Sheep milk and cheeses proteins)", "source": "Milk", "ic50": "316 μM", "reference": "Identification and characterization of novel angiotensin-converting enzyme inhibitors obtained from goat milk.", "doi": "10.3168\/jds.S0022-0302(06)72369-4", "pubmedid": "16899665", "mw": "597.66", "pi": "5.18", "charge_ph7": "-0.6", "gravy": "-0.55", "instability": "-10.62", "hydrophobic": "0.5", "boman": "-0.6633", "helix": "0.0", "turn_pct": "0.6667", "sheet": "0.3333" }, { "id": "aceip0946", "seq": "TGPIPNSLPQ", "length": "10", "detail": "Milk | Cheese", "source": "Milk", "ic50": ">1000 μM", "reference": "Angiotensin-converting enzyme inhibitory activity of peptides derived from caprine kefir.", "doi": "10.3168\/jds.S0022-0302(05)73032-0", "pubmedid": "16162521", "mw": "1023.14", "pi": "5.18", "charge_ph7": "-0.6", "gravy": "-0.54", "instability": "36.15", "hydrophobic": "0.5", "boman": "-0.67", "helix": "0.1", "turn_pct": "0.6", "sheet": "0.3" }, { "id": "aceip0947", "seq": "TGVY", "length": "4", "detail": "Fish (Cuttlefish)", "source": "Fish", "ic50": "18.2 μM", "reference": "Antihypertensive peptides from food proteins: a review.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1039\/c2fo10192k; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "22249830 23871047", "mw": "438.47", "pi": "5.18", "charge_ph7": "-0.6", "gravy": "0.45", "instability": "-32.58", "hydrophobic": "0.25", "boman": "-1.145", "helix": "0.0", "turn_pct": "0.25", "sheet": "0.75" }, { "id": "aceip0948", "seq": "THIKWGD", "length": "7", "detail": "Sweet-potato", "source": "Potato", "ic50": "50 μM", "reference": "Potent synthetic analogues of angiotensin-converting enzyme inhibitor derived from Tuna muscle.", "doi": "", "pubmedid": "1368734", "mw": "855.94", "pi": "6.42", "charge_ph7": "-0.51", "gravy": "-1.1571", "instability": "44.4", "hydrophobic": "0.2857", "boman": "-0.5257", "helix": "0.1429", "turn_pct": "0.2857", "sheet": "0.4286" }, { "id": "aceip0949", "seq": "TK", "length": "2", "detail": "Chickpea", "source": "Legume", "ic50": "<20 mM", "reference": "Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.", "doi": "10.1021\/jf051263l", "pubmedid": "16448176", "mw": "247.29", "pi": "8.41", "charge_ph7": "0.4", "gravy": "-2.3", "instability": "5.0", "hydrophobic": "0.0", "boman": "0.92", "helix": "0.5", "turn_pct": "0.0", "sheet": "0.5" }, { "id": "aceip0950", "seq": "TKIVP", "length": "5", "detail": "ND", "source": "ND", "ic50": "400 μM", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "23194537", "mw": "556.7", "pi": "8.41", "charge_ph7": "0.4", "gravy": "0.5", "instability": "12.56", "hydrophobic": "0.6", "boman": "-1.424", "helix": "0.2", "turn_pct": "0.2", "sheet": "0.6" }, { "id": "aceip0951", "seq": "TKVIP", "length": "5", "detail": "Milk | Cereals | Chicken", "source": "Milk | Cereal | Chicken", "ic50": "400 μM", "reference": "Identification of two distinct antibacterial domains within the sequence of bovine alpha(s2)-casein.; Antihypertensive peptides: production, bioavailability and incorporation into foods.; Antihypertensive peptides from food proteins: a review.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/s0304-4165(99)00079-3; 10.1016\/j.cis.2010.11.001; 10.1039\/c2fo10192k; 10.1016\/j.foodchem.2012.09.092", "pubmedid": "10434050 21185549 22249830 23194537", "mw": "556.7", "pi": "8.41", "charge_ph7": "0.4", "gravy": "0.5", "instability": "-14.74", "hydrophobic": "0.6", "boman": "-1.424", "helix": "0.2", "turn_pct": "0.2", "sheet": "0.6" }, { "id": "aceip0952", "seq": "TKY", "length": "3", "detail": "Meat", "source": "Meat", "ic50": "<20 mM", "reference": "Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Inhibition strength of short peptides derived from an ACE inhibitory peptide.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1021\/jf051263l; 10.1021\/jf202902r; 10.1080\/10408398.2012.664829", "pubmedid": "16448176 21923188 24915368", "mw": "410.46", "pi": "8.26", "charge_ph7": "0.4", "gravy": "-1.9667", "instability": "6.67", "hydrophobic": "0.0", "boman": "0.66", "helix": "0.3333", "turn_pct": "0.0", "sheet": "0.6667" }, { "id": "aceip0953", "seq": "TNP", "length": "3", "detail": "sea cucumber", "source": "Animal", "ic50": "<20 mM", "reference": "Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Peptide inhibitors for angiotensin I-converting enzyme from enzymatic hydrolysates of porcine skeletal muscle proteins.", "doi": "10.1021\/jf051263l; 10.1016\/s0309-1740(00)00108-x", "pubmedid": "16448176 22061507", "mw": "330.34", "pi": "5.18", "charge_ph7": "-0.6", "gravy": "-1.9333", "instability": "-53.03", "hydrophobic": "0.3333", "boman": "0.6267", "helix": "0.0", "turn_pct": "0.6667", "sheet": "0.3333" }, { "id": "aceip0954", "seq": "TP", "length": "2", "detail": "Milk (bovine) | Amaranth | Sardine | Fish (Shark) | Cereals | pea | Pork", "source": "Milk | Plants | Fish | Cereal | Legume | Porcine", "ic50": "<20 mM", "reference": "Angiotensin I-converting enzyme inhibitory activity and insulin secretion stimulative activity of fermented fish sauce.; Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1016\/S1389-1723(03)70138-8; 10.1021\/jf051263l; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "16233562 16448176 23871047", "mw": "216.23", "pi": "5.18", "charge_ph7": "-0.6", "gravy": "-1.15", "instability": "5.0", "hydrophobic": "0.5", "boman": "0.13", "helix": "0.0", "turn_pct": "0.5", "sheet": "0.5" }, { "id": "aceip0955", "seq": "TPPAGPDGGPP", "length": "11", "detail": "ND", "source": "ND", "ic50": null, "reference": "A novel peptide from the ACEI\/BPP-CNP precursor in the venom of Crotalus durissus collilineatus.", "doi": "10.1016\/j.cbpc.2006.04.006", "pubmedid": "16979945", "mw": "962.01", "pi": "4.05", "charge_ph7": "-1.6", "gravy": "-1.0545", "instability": "65.98", "hydrophobic": "0.5455", "boman": "-0.2445", "helix": "0.0909", "turn_pct": "0.8182", "sheet": "0.0909" }, { "id": "aceip0956", "seq": "TPVVVPPFLQP", "length": "11", "detail": "Milk (bovine) | Cereals | Chicken", "source": "Milk | Cereal | Chicken", "ic50": "749 μM", "reference": "Structural analysis of new antihypertensive peptides derived from cheese whey protein by proteinase K digestion.; Antihypertensive peptides: production, bioavailability and incorporation into foods.; Antihypertensive peptides from food proteins: a review.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.3168\/jds.S0022-0302(98)75878-3; 10.1016\/j.cis.2010.11.001; 10.1039\/c2fo10192k; 10.1080\/10408398.2012.664829", "pubmedid": "9891260 21185549 22249830 24915368", "mw": "1193.43", "pi": "5.18", "charge_ph7": "-0.6", "gravy": "0.7818", "instability": "126.27", "hydrophobic": "0.8182", "boman": "-1.6727", "helix": "0.0909", "turn_pct": "0.3636", "sheet": "0.5455" }, { "id": "aceip0957", "seq": "TPWVPPFLQP", "length": "10", "detail": "Meat", "source": "Meat", "ic50": "749 μM", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "23194537", "mw": "1181.38", "pi": "5.18", "charge_ph7": "-0.6", "gravy": "-0.07", "instability": "107.27", "hydrophobic": "0.8", "boman": "-1.265", "helix": "0.1", "turn_pct": "0.4", "sheet": "0.5" }, { "id": "aceip0958", "seq": "TQ", "length": "2", "detail": "Fish | Yellowfin sole", "source": "Fish", "ic50": "0 0", "reference": "Application of at-line two-dimensional liquid chromatography-mass spectrometry for identification of small hydrophilic angiotensin I-inhibiting peptides in milk hydrolysates.", "doi": "10.1007\/s00216-008-1990-3", "pubmedid": "18392815", "mw": "247.25", "pi": "5.18", "charge_ph7": "-0.6", "gravy": "-2.1", "instability": "-32.7", "hydrophobic": "0.0", "boman": "0.81", "helix": "0.0", "turn_pct": "0.0", "sheet": "0.5" }, { "id": "aceip0959", "seq": "TQSLVYP", "length": "7", "detail": "ND", "source": "ND", "ic50": "64 μM", "reference": "Inhibition of angiotensin-converting enzyme by synthetic peptide fragments of various beta-caseins.; Evaluation of the allergenicity of goat milk, cow milk, and their lactosera in a guinea pig model.", "doi": "10.3168\/jds.2008-1125", "pubmedid": "1368548 19233776", "mw": "806.9", "pi": "5.18", "charge_ph7": "-0.6", "gravy": "0.0143", "instability": "67.43", "hydrophobic": "0.4286", "boman": "-0.9086", "helix": "0.1429", "turn_pct": "0.2857", "sheet": "0.5714" }, { "id": "aceip0960", "seq": "TQTPVVVPPFIQPE", "length": "14", "detail": "ND", "source": "ND", "ic50": null, "reference": "Casein fermentate of Lactobacillus animalis DPC6134 contains a range of novel propeptide angiotensin-converting enzyme inhibitors.", "doi": "10.1128\/AEM.00096-07", "pubmedid": "17483275", "mw": "1551.78", "pi": "4.59", "charge_ph7": "-1.59", "gravy": "0.1143", "instability": "85.1", "hydrophobic": "0.6429", "boman": "-1.0814", "helix": "0.0714", "turn_pct": "0.2857", "sheet": "0.5" }, { "id": "aceip0961", "seq": "TQVY", "length": "4", "detail": "Milk", "source": "Milk", "ic50": "18.2 μM", "reference": "Depressor effect of wheat germ hydrolysate and its novel angiotensin I-converting enzyme inhibitory peptide, Ile-Val-Tyr, and the metabolism in rat and human plasma.; Antihypertensive effect of rice protein hydrolysate with in vitro angiotensin I-converting enzyme inhibitory activity in spontaneously hypertensive rats.; Vegetable foods: a cheap source of proteins and peptides with antihypertensive, antioxidant, and other less occurrence bioactivities.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1248\/bpb.23.427; 10.1016\/j.talanta.2012.12.041; 10.1080\/10408398.2012.664829", "pubmedid": "10784421 17392118 23598136 24915368", "mw": "509.55", "pi": "5.18", "charge_ph7": "-0.6", "gravy": "-0.325", "instability": "-49.05", "hydrophobic": "0.25", "boman": "-0.57", "helix": "0.0", "turn_pct": "0.0", "sheet": "0.75" }, { "id": "aceip0962", "seq": "TTI", "length": "3", "detail": "Milk | Casein | Milk (whey)", "source": "Milk", "ic50": "6.59-27.38 μM", "reference": "Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1080\/10408398.2012.664829", "pubmedid": "24915368", "mw": "333.38", "pi": "5.18", "charge_ph7": "-0.6", "gravy": "1.0333", "instability": "6.67", "hydrophobic": "0.3333", "boman": "-1.4667", "helix": "0.0", "turn_pct": "0.0", "sheet": "1.0" }, { "id": "aceip0963", "seq": "TTMLIQDEDDLEMA", "length": "14", "detail": "Milk", "source": "Milk", "ic50": null, "reference": "Casein fermentate of Lactobacillus animalis DPC6134 contains a range of novel propeptide angiotensin-converting enzyme inhibitors.", "doi": "10.1128\/AEM.00096-07", "pubmedid": "17483275", "mw": "1624.79", "pi": "4.05", "charge_ph7": "-5.59", "gravy": "-0.3357", "instability": "45.61", "hydrophobic": "0.4286", "boman": "-0.7907", "helix": "0.5", "turn_pct": "0.2143", "sheet": "0.3571" }, { "id": "aceip0964", "seq": "TTMPLW", "length": "6", "detail": "Casein | Milk (Casein) | Lactobacillus helveticus", "source": "Milk | Bacteria", "ic50": "12 μM", "reference": "Antihypertensive peptides: production, bioavailability and incorporation into foods.; Bioactive peptides derived from milk proteins and their health beneficial potentials: an update.; Antihypertensive peptides from food proteins: a review.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.cis.2010.11.001; 10.1039\/c0fo00016g; 10.1039\/c2fo10192k; 10.1016\/j.foodchem.2012.09.092", "pubmedid": "21185549 21773582 22249830 23194537", "mw": "747.9", "pi": "5.18", "charge_ph7": "-0.6", "gravy": "0.3", "instability": "121.03", "hydrophobic": "0.6667", "boman": "-1.5133", "helix": "0.3333", "turn_pct": "0.1667", "sheet": "0.6667" }, { "id": "aceip0965", "seq": "TTN", "length": "3", "detail": "Egg (Ovalbumin)", "source": "Egg", "ic50": "<20 mM", "reference": "Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Peptide inhibitors for angiotensin I-converting enzyme from enzymatic hydrolysates of porcine skeletal muscle proteins.", "doi": "10.1021\/jf051263l; 10.1016\/s0309-1740(00)00108-x", "pubmedid": "16448176 22061507", "mw": "334.33", "pi": "5.18", "charge_ph7": "-0.6", "gravy": "-1.6333", "instability": "-43.43", "hydrophobic": "0.0", "boman": "0.7133", "helix": "0.0", "turn_pct": "0.3333", "sheet": "0.6667" }, { "id": "aceip0966", "seq": "TVDQ", "length": "4", "detail": "ND", "source": "ND", "ic50": null, "reference": "Angiotensin I-converting-enzyme-inhibitory and antibacterial peptides from Lactobacillus helveticus PR4 proteinase-hydrolyzed caseins of milk from six species.", "doi": "10.1128\/AEM.69.9.5297-5305.2003", "pubmedid": "12957917", "mw": "461.47", "pi": "4.05", "charge_ph7": "-1.6", "gravy": "-0.875", "instability": "-30.07", "hydrophobic": "0.25", "boman": "-0.185", "helix": "0.0", "turn_pct": "0.25", "sheet": "0.5" }, { "id": "aceip0967", "seq": "TVDQHQ", "length": "6", "detail": "Pork", "source": "Porcine", "ic50": "183.5 μM", "reference": "Angiotensin I-converting-enzyme-inhibitory and antibacterial peptides from Lactobacillus helveticus PR4 proteinase-hydrolyzed caseins of milk from six species.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1128\/AEM.69.9.5297-5305.2003; 10.1016\/j.foodchem.2012.09.092", "pubmedid": "12957917 23194537", "mw": "726.74", "pi": "5.05", "charge_ph7": "-1.51", "gravy": "-1.7", "instability": "-16.72", "hydrophobic": "0.1667", "boman": "0.2683", "helix": "0.0", "turn_pct": "0.1667", "sheet": "0.3333" }, { "id": "aceip0968", "seq": "TVPY", "length": "4", "detail": "Pork", "source": "Porcine", "ic50": "2.0 μM", "reference": "Preparation and characterization of novel bioactive peptides responsible for angiotensin I-converting enzyme inhibition from wheat germ.", "doi": "10.1002\/(SICI)1099-1387(199907)5:7<289::AID-PSC196>3.0.CO;2-6", "pubmedid": "10442764", "mw": "478.54", "pi": "5.18", "charge_ph7": "-0.6", "gravy": "0.15", "instability": "55.65", "hydrophobic": "0.5", "boman": "-0.91", "helix": "0.0", "turn_pct": "0.25", "sheet": "0.75" }, { "id": "aceip0969", "seq": "TVVPG", "length": "5", "detail": "Sea squirt | Ascidian", "source": "Animal", "ic50": "6.5 μM", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "23194537", "mw": "471.55", "pi": "5.18", "charge_ph7": "-0.6", "gravy": "1.14", "instability": "46.52", "hydrophobic": "0.6", "boman": "-1.752", "helix": "0.0", "turn_pct": "0.4", "sheet": "0.6" }, { "id": "aceip0970", "seq": "TVY", "length": "3", "detail": "Sesame", "source": "Plants", "ic50": "<20 mM", "reference": "Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1021\/jf051263l; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "16448176 23871047", "mw": "381.42", "pi": "5.18", "charge_ph7": "-0.6", "gravy": "0.7333", "instability": "-18.47", "hydrophobic": "0.3333", "boman": "-1.2133", "helix": "0.0", "turn_pct": "0.0", "sheet": "1.0" }, { "id": "aceip0971", "seq": "TVYTKGRVMP", "length": "10", "detail": "Sweet-potato", "source": "Potato", "ic50": "38 μM", "reference": "Inhibition of angiotensin-converting enzyme by synthetic peptide fragments of various beta-caseins.", "doi": "", "pubmedid": "1368548", "mw": "1151.38", "pi": "9.99", "charge_ph7": "1.4", "gravy": "-0.28", "instability": "28.42", "hydrophobic": "0.4", "boman": "-0.641", "helix": "0.2", "turn_pct": "0.2", "sheet": "0.5" }, { "id": "aceip0972", "seq": "TYLGS", "length": "5", "detail": "Pork", "source": "Porcine", "ic50": "0.86 μM", "reference": "Inhibition strength of short peptides derived from an ACE inhibitory peptide.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1021\/jf202902r; 10.1016\/j.foodchem.2012.09.092", "pubmedid": "21923188 23194537", "mw": "539.58", "pi": "5.18", "charge_ph7": "-0.6", "gravy": "0.12", "instability": "8.0", "hydrophobic": "0.2", "boman": "-0.924", "helix": "0.2", "turn_pct": "0.4", "sheet": "0.6" }, { "id": "aceip0973", "seq": "VA", "length": "2", "detail": "Pork", "source": "Porcine", "ic50": null, "reference": "Three-dimensional holograph vector of atomic interaction field (3D-HoVAIF): a novel rotation-translation invariant 3D structure descriptor and its applications to peptides.", "doi": "10.1002\/psc.892", "pubmedid": "17654623", "mw": "188.22", "pi": "5.49", "charge_ph7": "-0.27", "gravy": "3.0", "instability": "5.0", "hydrophobic": "1.0", "boman": "-2.925", "helix": "0.5", "turn_pct": "0.0", "sheet": "0.5" }, { "id": "aceip0974", "seq": "VAA", "length": "3", "detail": "Pork", "source": "Porcine", "ic50": "13 μM", "reference": "Structures and activity of angiotensin-converting enzyme inhibitors in an alpha-zein hydrolysate.; Bioactive peptides in amaranth (Amaranthus hypochondriacus) seed.; Cellular membrane disruption by amyloid fibrils involved intermolecular disulfide cross-linking.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1021\/jf072911z; 10.1021\/bi900219c; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "1368684 18211015 19449893 23871047", "mw": "259.3", "pi": "5.49", "charge_ph7": "-0.27", "gravy": "2.6", "instability": "6.67", "hydrophobic": "1.0", "boman": "-2.5533", "helix": "0.6667", "turn_pct": "0.0", "sheet": "0.3333" }, { "id": "aceip0975", "seq": "VADVYVGK", "length": "8", "detail": "ND", "source": "ND", "ic50": "2.82 μM", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "23194537", "mw": "849.97", "pi": "5.81", "charge_ph7": "-0.27", "gravy": "0.6625", "instability": "-32.51", "hydrophobic": "0.5", "boman": "-1.4337", "helix": "0.25", "turn_pct": "0.25", "sheet": "0.5" }, { "id": "aceip0976", "seq": "VAF", "length": "3", "detail": "Egg (Ovalbumin)", "source": "Egg", "ic50": "35.8 μM", "reference": "Review on the angiotensin-I-converting enzyme (ACE) inhibitor peptides from marine proteins.; Vegetable foods: a cheap source of proteins and peptides with antihypertensive, antioxidant, and other less occurrence bioactivities.", "doi": "10.1007\/s12010-012-0024-y; 10.1016\/j.talanta.2012.12.041", "pubmedid": "23271625 23598136", "mw": "335.4", "pi": "5.49", "charge_ph7": "-0.27", "gravy": "2.9333", "instability": "6.67", "hydrophobic": "1.0", "boman": "-2.9433", "helix": "0.3333", "turn_pct": "0.0", "sheet": "0.6667" }, { "id": "aceip0977", "seq": "VAGTW", "length": "5", "detail": "Milk (bovine) | Casein", "source": "Milk", "ic50": "534 μM", "reference": "Angiotensin I-converting enzyme inhibitory properties of whey protein digests: concentration and characterization of active peptides.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1017\/s0022029999003982; 10.1016\/j.foodchem.2012.09.092", "pubmedid": "10717843 23194537", "mw": "532.59", "pi": "5.49", "charge_ph7": "-0.27", "gravy": "0.8", "instability": "-39.04", "hydrophobic": "0.6", "boman": "-1.772", "helix": "0.2", "turn_pct": "0.2", "sheet": "0.6" }, { "id": "aceip0978", "seq": "VAGTWY", "length": "6", "detail": "Cheese (Gouda cheese)", "source": "Milk", "ic50": "1682 μM", "reference": "Quality and acceptability of a set-type yogurt made from camel milk.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.3168\/jds.2008-1408; 10.1016\/j.foodchem.2012.09.092", "pubmedid": "19233778 23194537", "mw": "695.76", "pi": "5.49", "charge_ph7": "-0.27", "gravy": "0.45", "instability": "-30.87", "hydrophobic": "0.5", "boman": "-1.4533", "helix": "0.1667", "turn_pct": "0.1667", "sheet": "0.6667" }, { "id": "aceip0979", "seq": "VAHINVGK", "length": "8", "detail": "ND", "source": "ND", "ic50": "6.76 μM", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "23194537", "mw": "836.98", "pi": "8.73", "charge_ph7": "0.82", "gravy": "0.4625", "instability": "31.84", "hydrophobic": "0.5", "boman": "-1.445", "helix": "0.25", "turn_pct": "0.25", "sheet": "0.375" }, { "id": "aceip0980", "seq": "VAHINVWK", "length": "8", "detail": "Spinach", "source": "Plants", "ic50": "3.47 μM", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "23194537", "mw": "966.14", "pi": "8.73", "charge_ph7": "0.82", "gravy": "0.4", "instability": "53.06", "hydrophobic": "0.625", "boman": "-1.6187", "helix": "0.25", "turn_pct": "0.125", "sheet": "0.5" }, { "id": "aceip0981", "seq": "VAND", "length": "4", "detail": "Spinach", "source": "Plants", "ic50": "411 μM", "reference": "Vegetable foods: a cheap source of proteins and peptides with antihypertensive, antioxidant, and other less occurrence bioactivities.", "doi": "10.1016\/j.talanta.2012.12.041", "pubmedid": "23598136", "mw": "417.41", "pi": "4.3", "charge_ph7": "-1.26", "gravy": "-0.25", "instability": "7.5", "hydrophobic": "0.5", "boman": "-0.6375", "helix": "0.25", "turn_pct": "0.5", "sheet": "0.25" }, { "id": "aceip0982", "seq": "VAP", "length": "3", "detail": "Fish (Skate)", "source": "Fish", "ic50": "0.00534 mg\/ml", "reference": "Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Bioactive peptides in amaranth (Amaranthus hypochondriacus) seed.; Vegetable foods: a cheap source of proteins and peptides with antihypertensive, antioxidant, and other less occurrence bioactivities.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.; Glycinyl-histidinyl-serine (GHS), a novel rapeseed protein-derived peptide has blood pressure-lowering effect in spontaneously hypertensive rats.", "doi": "10.1021\/jf051263l; 10.1021\/jf072911z; 10.1016\/j.talanta.2012.12.041; 10.1016\/j.foodchem.2013.05.140; 10.1021\/jf400865m", "pubmedid": "16448176 18211015 23598136 23871047 23919612", "mw": "285.34", "pi": "5.49", "charge_ph7": "-0.27", "gravy": "1.4667", "instability": "70.87", "hydrophobic": "1.0", "boman": "-1.95", "helix": "0.3333", "turn_pct": "0.3333", "sheet": "0.3333" }, { "id": "aceip0983", "seq": "VAPEEHPT", "length": "8", "detail": "Milk | Sardine | Salmon", "source": "Milk | Fish", "ic50": null, "reference": "Angiotensin I-converting enzyme inhibitory peptides generated from in vitro gastrointestinal digestion of pork meat.", "doi": "10.1021\/jf904204n", "pubmedid": "20151679", "mw": "878.93", "pi": "4.51", "charge_ph7": "-2.17", "gravy": "-1.0125", "instability": "82.28", "hydrophobic": "0.5", "boman": "-0.165", "helix": "0.375", "turn_pct": "0.25", "sheet": "0.25" }, { "id": "aceip0984", "seq": "VAPFPEVF", "length": "8", "detail": "Amaranth | Sardine | Cereals", "source": "Plants | Fish | Cereal", "ic50": "362.5 ± 23.56 μM", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "23194537", "mw": "905.05", "pi": "4.05", "charge_ph7": "-1.26", "gravy": "1.1375", "instability": "102.7", "hydrophobic": "0.875", "boman": "-1.7763", "helix": "0.25", "turn_pct": "0.25", "sheet": "0.5" }, { "id": "aceip0985", "seq": "VAV", "length": "3", "detail": "Pork", "source": "Porcine", "ic50": "260 μM", "reference": "Inhibition of angiotensin-converting enzyme by synthetic peptide fragments of human kappa-casein.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1016\/j.foodchem.2013.05.140", "pubmedid": "1368540 23871047", "mw": "287.36", "pi": "5.49", "charge_ph7": "-0.27", "gravy": "3.4", "instability": "6.67", "hydrophobic": "1.0", "boman": "-3.2967", "helix": "0.3333", "turn_pct": "0.0", "sheet": "0.6667" }, { "id": "aceip0986", "seq": "VAW", "length": "3", "detail": "Casein | Milk (human)", "source": "Milk", "ic50": "2.86 μM", "reference": "ACE inhibitory peptides and antioxidant peptides derived from in vitro digestion hydrolysate of hen egg white lysozyme.", "doi": "10.1016\/j.foodchem.2012.05.059", "pubmedid": "22953850", "mw": "374.43", "pi": "5.49", "charge_ph7": "-0.27", "gravy": "1.7", "instability": "6.67", "hydrophobic": "1.0", "boman": "-2.7267", "helix": "0.3333", "turn_pct": "0.0", "sheet": "0.6667" }, { "id": "aceip0987", "seq": "VAWKL", "length": "5", "detail": "Milk (Sheep raw milk cheese (synthesised))", "source": "Milk", "ic50": "31.62 μM", "reference": "Effects of angiotensin I-converting enzyme inhibitory substances derived from Indonesian dried-salted fish on blood pressure of rats.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1271\/bbb.59.425; 10.1016\/j.foodchem.2012.09.092", "pubmedid": "7766180 23194537", "mw": "615.76", "pi": "8.72", "charge_ph7": "0.73", "gravy": "1.0", "instability": "-8.98", "hydrophobic": "0.8", "boman": "-2.304", "helix": "0.6", "turn_pct": "0.0", "sheet": "0.6" }, { "id": "aceip0988", "seq": "VAY", "length": "3", "detail": "Arachin", "source": "Legume", "ic50": "16 μM", "reference": "Structures and activity of angiotensin-converting enzyme inhibitors in an alpha-zein hydrolysate.; Bioactive peptides in amaranth (Amaranthus hypochondriacus) seed.; Cellular membrane disruption by amyloid fibrils involved intermolecular disulfide cross-linking.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1021\/jf072911z; 10.1021\/bi900219c; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "1368684 18211015 19449893 23871047", "mw": "351.4", "pi": "5.49", "charge_ph7": "-0.27", "gravy": "1.5667", "instability": "6.67", "hydrophobic": "0.6667", "boman": "-1.9033", "helix": "0.3333", "turn_pct": "0.0", "sheet": "0.6667" }, { "id": "aceip0989", "seq": "VD", "length": "2", "detail": "Milk", "source": "Milk", "ic50": null, "reference": "Quantitative structure-activity relationship study of bitter di- and tri-peptides including relationship with angiotensin I-converting enzyme inhibitory activity.", "doi": "10.1002\/psc.800", "pubmedid": "17117396", "mw": "232.23", "pi": "4.3", "charge_ph7": "-1.26", "gravy": "0.35", "instability": "-70.15", "hydrophobic": "0.5", "boman": "-1.18", "helix": "0.0", "turn_pct": "0.5", "sheet": "0.5" }, { "id": "aceip0990", "seq": "VDF", "length": "3", "detail": "Milk (Casein)", "source": "Milk", "ic50": "<10 μM", "reference": "Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1080\/10408398.2012.664829", "pubmedid": "24915368", "mw": "379.41", "pi": "4.05", "charge_ph7": "-1.26", "gravy": "1.1667", "instability": "-68.57", "hydrophobic": "0.6667", "boman": "-1.78", "helix": "0.0", "turn_pct": "0.3333", "sheet": "0.6667" }, { "id": "aceip0991", "seq": "VE", "length": "2", "detail": "Milk (bovine)", "source": "Milk", "ic50": "0 0", "reference": "Quantitative structure-activity relationship study of bitter di- and tri-peptides including relationship with angiotensin I-converting enzyme inhibitory activity.; Application of at-line two-dimensional liquid chromatography-mass spectrometry for identification of small hydrophilic angiotensin I-inhibiting peptides in milk hydrolysates.; Peptides with angiotensin I converting enzyme (ACE) inhibitory activity generated from porcine skeletal muscle proteins by the action of meat-borne Lactobacillus.", "doi": "10.1002\/psc.800; 10.1007\/s00216-008-1990-3; 10.1016\/j.jprot.2013.06.023", "pubmedid": "17117396 18392815 23806758", "mw": "246.26", "pi": "4.6", "charge_ph7": "-1.26", "gravy": "0.35", "instability": "5.0", "hydrophobic": "0.5", "boman": "-1.2", "helix": "0.5", "turn_pct": "0.0", "sheet": "0.5" }, { "id": "aceip0992", "seq": "VECYGPNRPQF", "length": "11", "detail": "Milk (bovine) | Garlic | Carp | Cereals | Pork", "source": "Milk | Plants | Fish | Cereal | Porcine", "ic50": "29.6 μM", "reference": "Review on the angiotensin-I-converting enzyme (ACE) inhibitor peptides from marine proteins.; Glycinyl-histidinyl-serine (GHS), a novel rapeseed protein-derived peptide has blood pressure-lowering effect in spontaneously hypertensive rats.", "doi": "10.1007\/s12010-012-0024-y; 10.1021\/jf400865m", "pubmedid": "23271625 23919612", "mw": "1309.45", "pi": "5.97", "charge_ph7": "-0.27", "gravy": "-0.9455", "instability": "69.48", "hydrophobic": "0.3636", "boman": "-0.16", "helix": "0.0909", "turn_pct": "0.3636", "sheet": "0.2727" }, { "id": "aceip0993", "seq": "VENLHLPLPL", "length": "10", "detail": "Milk (bovine) | Cereals | Chicken", "source": "Milk | Cereal | Chicken", "ic50": null, "reference": "Identification of angiotensin-I-converting enzyme inhibitory peptides derived from sodium caseinate hydrolysates produced by Lactobacillus helveticus NCC 2765.", "doi": "10.1021\/jf049510t", "pubmedid": "15537298", "mw": "1144.36", "pi": "5.24", "charge_ph7": "-1.18", "gravy": "0.6", "instability": "47.52", "hydrophobic": "0.7", "boman": "-1.947", "helix": "0.5", "turn_pct": "0.3", "sheet": "0.5" }, { "id": "aceip0994", "seq": "VENLHLPLPLL", "length": "11", "detail": "ND", "source": "ND", "ic50": "175 μM", "reference": "Identification of angiotensin-I-converting enzyme inhibitory peptides derived from sodium caseinate hydrolysates produced by Lactobacillus helveticus NCC 2765.", "doi": "10.1021\/jf049510t", "pubmedid": "15537298", "mw": "1257.52", "pi": "5.24", "charge_ph7": "-1.18", "gravy": "0.8909", "instability": "44.11", "hydrophobic": "0.7273", "boman": "-2.2173", "helix": "0.5455", "turn_pct": "0.2727", "sheet": "0.5455" }, { "id": "aceip0995", "seq": "VF", "length": "2", "detail": "Flaxseed", "source": "Plants", "ic50": "<20 mM", "reference": "Angiotensin I-converting enzyme inhibitory peptides in an alkaline protease hydrolyzate derived from sardine muscle.; Antihypertensive effects of Undaria pinnatifida (wakame) peptide on blood pressure in spontaneously hypertensive rats.; Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Quantitative structure-activity relationship study of bitter di- and tri-peptides including relationship with angiotensin I-converting enzyme inhibitory activity.; Three-dimensional holograph vector of atomic interaction field (3D-HoVAIF): a novel rotation-translation invariant 3D structure descriptor and its applications to peptides.; Bioactive peptides in amaranth (Amaranthus hypochondriacus) seed.; Ala-Val-Phe and Val-Phe: ACE inhibitory peptides derived from insect protein with antihypertensive activity in spontaneously hypertensive rats.; QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.; Antihypertensive peptides from food proteins: a review.; Review on the angiotensin-I-converting enzyme (ACE) inhibitor peptides from marine proteins.; Vegetable foods: a cheap source of proteins and peptides with antihypertensive, antioxidant, and other less occurrence bioactivities.; Peptides with angiotensin I converting enzyme (ACE) inhibitory activity generated from porcine skeletal muscle proteins by the action of meat-borne Lactobacillus.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1271\/bbb.58.2244; 10.1016\/j.jnutbio.2003.11.004; 10.1021\/jf051263l; 10.1002\/psc.800; 10.1002\/psc.892; 10.1021\/jf072911z; 10.1016\/j.peptides.2009.05.029; 10.1007\/s00894-010-0862-x; 10.1039\/c2fo10192k; 10.1007\/s12010-012-0024-y; 10.1016\/j.talanta.2012.12.041; 10.1016\/j.jprot.2013.06.023; 10.1016\/j.foodchem.2013.05.140; 10.1080\/10408398.2012.664829", "pubmedid": "7765718 15135150 16448176 17117396 17654623 18211015 19524628 20941517 22249830 23271625 23598136 23806758 23871047 24915368", "mw": "264.32", "pi": "5.49", "charge_ph7": "-0.27", "gravy": "3.5", "instability": "5.0", "hydrophobic": "1.0", "boman": "-3.51", "helix": "0.0", "turn_pct": "0.0", "sheet": "1.0" }, { "id": "aceip0996", "seq": "VFER", "length": "4", "detail": "Flaxseed", "source": "Plants", "ic50": "152.8 μM", "reference": "Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1080\/10408398.2012.664829", "pubmedid": "24915368", "mw": "549.62", "pi": "5.97", "charge_ph7": "-0.26", "gravy": "-0.25", "instability": "7.5", "hydrophobic": "0.5", "boman": "-0.665", "helix": "0.25", "turn_pct": "0.0", "sheet": "0.5" }, { "id": "aceip0997", "seq": "VFGKEK", "length": "6", "detail": "Egg (Ovalbumin)", "source": "Egg", "ic50": null, "reference": "Enterococcus faecalis strains from food, environmental, and clinical origin produce ACE-inhibitory peptides and other bioactive peptides during growth in bovine skim milk.", "doi": "10.1016\/j.ijfoodmicro.2013.06.019", "pubmedid": "23845432", "mw": "706.83", "pi": "8.56", "charge_ph7": "0.73", "gravy": "-0.7833", "instability": "-5.82", "hydrophobic": "0.3333", "boman": "-0.5267", "helix": "0.5", "turn_pct": "0.1667", "sheet": "0.3333" }, { "id": "aceip0998", "seq": "VFGR", "length": "4", "detail": "Pork", "source": "Porcine", "ic50": null, "reference": "What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1016\/j.foodchem.2013.05.140", "pubmedid": "23871047", "mw": "477.56", "pi": "9.72", "charge_ph7": "0.73", "gravy": "0.525", "instability": "7.5", "hydrophobic": "0.5", "boman": "-1.31", "helix": "0.0", "turn_pct": "0.25", "sheet": "0.5" }, { "id": "aceip0999", "seq": "VFK", "length": "3", "detail": "Milk (human)", "source": "Milk", "ic50": "<20 mM", "reference": "Angiotensin I-converting enzyme inhibitory properties of whey protein digests: concentration and characterization of active peptides.; Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.", "doi": "10.1017\/s0022029999003982; 10.1021\/jf051263l", "pubmedid": "10717843 16448176", "mw": "392.49", "pi": "8.72", "charge_ph7": "0.73", "gravy": "1.0333", "instability": "-43.43", "hydrophobic": "0.6667", "boman": "-1.8133", "helix": "0.3333", "turn_pct": "0.0", "sheet": "0.6667" }, { "id": "aceip1000", "seq": "VFPS", "length": "4", "detail": "Milk (bovine) | Milk (whey) | Milk (Fermented Milk)", "source": "Milk", "ic50": "0.46 μM", "reference": "Inhibition strength of short peptides derived from an ACE inhibitory peptide.", "doi": "10.1021\/jf202902r", "pubmedid": "21923188", "mw": "448.51", "pi": "5.49", "charge_ph7": "-0.27", "gravy": "1.15", "instability": "103.8", "hydrophobic": "0.75", "boman": "-1.545", "helix": "0.0", "turn_pct": "0.5", "sheet": "0.5" }, { "id": "aceip1001", "seq": "VG", "length": "2", "detail": "Milk (bovine)", "source": "Milk", "ic50": "<20 mM", "reference": "Binding of peptide substrates and inhibitors of angiotensin-converting enzyme. Importance of the COOH-terminal dipeptide sequence.; Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Three-dimensional holograph vector of atomic interaction field (3D-HoVAIF): a novel rotation-translation invariant 3D structure descriptor and its applications to peptides.; Antihypertensive effect of peptide-enriched soy sauce-like seasoning and identification of its angiotensin I-converting enzyme inhibitory substances.; QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.; Vegetable foods: a cheap source of proteins and peptides with antihypertensive, antioxidant, and other less occurrence bioactivities.; Peptides with angiotensin I converting enzyme (ACE) inhibitory activity generated from porcine skeletal muscle proteins by the action of meat-borne Lactobacillus.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1021\/jf051263l; 10.1002\/psc.892; 10.1021\/jf903261h; 10.1007\/s00894-010-0862-x; 10.1016\/j.talanta.2012.12.041; 10.1016\/j.jprot.2013.06.023; 10.1016\/j.foodchem.2013.05.140; 10.1080\/10408398.2012.664829", "pubmedid": "6243277 16448176 17654623 19994857 20941517 23598136 23806758 23871047 24915368", "mw": "174.2", "pi": "5.49", "charge_ph7": "-0.27", "gravy": "1.9", "instability": "-37.45", "hydrophobic": "0.5", "boman": "-2.49", "helix": "0.0", "turn_pct": "0.5", "sheet": "0.5" }, { "id": "aceip1002", "seq": "VGINYWLAHK", "length": "10", "detail": "Milk (bovine)", "source": "Milk", "ic50": "327 μM", "reference": "Angiotensin I-converting enzyme inhibitory properties of whey protein digests: concentration and characterization of active peptides.", "doi": "10.1017\/s0022029999003982", "pubmedid": "10717843", "mw": "1200.39", "pi": "8.57", "charge_ph7": "0.82", "gravy": "0.11", "instability": "9.18", "hydrophobic": "0.5", "boman": "-1.463", "helix": "0.3", "turn_pct": "0.2", "sheet": "0.5" }, { "id": "aceip1003", "seq": "VGLPIF", "length": "6", "detail": "Milk (bovine) | Pork | Chicken", "source": "Milk | Porcine | Chicken", "ic50": "25.26 mg\/ml", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "23194537", "mw": "644.8", "pi": "5.49", "charge_ph7": "-0.27", "gravy": "2.2167", "instability": "26.28", "hydrophobic": "0.8333", "boman": "-2.9667", "helix": "0.1667", "turn_pct": "0.3333", "sheet": "0.6667" }, { "id": "aceip1004", "seq": "VGP", "length": "3", "detail": "Milk (bovine)", "source": "Milk", "ic50": "<20 mM", "reference": "Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.", "doi": "10.1021\/jf051263l", "pubmedid": "16448176", "mw": "271.31", "pi": "5.49", "charge_ph7": "-0.27", "gravy": "0.7333", "instability": "-21.63", "hydrophobic": "0.6667", "boman": "-1.66", "helix": "0.0", "turn_pct": "0.6667", "sheet": "0.3333" }, { "id": "aceip1005", "seq": "VGPR", "length": "4", "detail": "Chicken", "source": "Chicken", "ic50": "382->1000 μM", "reference": "Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1080\/10408398.2012.664829", "pubmedid": "24915368", "mw": "427.5", "pi": "9.72", "charge_ph7": "0.73", "gravy": "-0.575", "instability": "-32.58", "hydrophobic": "0.5", "boman": "-0.565", "helix": "0.0", "turn_pct": "0.5", "sheet": "0.25" }, { "id": "aceip1006", "seq": "VHLAP", "length": "5", "detail": "Flaxseed", "source": "Plants", "ic50": "4.5 μM", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "23194537", "mw": "535.64", "pi": "6.71", "charge_ph7": "-0.18", "gravy": "1.0", "instability": "46.52", "hydrophobic": "0.8", "boman": "-1.956", "helix": "0.4", "turn_pct": "0.2", "sheet": "0.4" }, { "id": "aceip1007", "seq": "VHLPP", "length": "5", "detail": "Flaxseed", "source": "Plants", "ic50": "18 μM", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "23194537", "mw": "561.67", "pi": "6.71", "charge_ph7": "-0.18", "gravy": "0.32", "instability": "85.04", "hydrophobic": "0.8", "boman": "-1.594", "helix": "0.2", "turn_pct": "0.4", "sheet": "0.4" }, { "id": "aceip1008", "seq": "VHLPPP", "length": "6", "detail": "Milk (bovine) | Milk (human)", "source": "Milk", "ic50": "200 μM", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "23194537", "mw": "658.79", "pi": "6.71", "charge_ph7": "-0.18", "gravy": "0.0", "instability": "104.63", "hydrophobic": "0.8333", "boman": "-1.3283", "helix": "0.1667", "turn_pct": "0.5", "sheet": "0.3333" }, { "id": "aceip1009", "seq": "VI", "length": "2", "detail": "Milk (bovine) | Milk (human)", "source": "Milk", "ic50": null, "reference": "Quantitative structure-activity relationship study of bitter di- and tri-peptides including relationship with angiotensin I-converting enzyme inhibitory activity.", "doi": "10.1002\/psc.800", "pubmedid": "17117396", "mw": "230.3", "pi": "5.49", "charge_ph7": "-0.27", "gravy": "4.35", "instability": "5.0", "hydrophobic": "1.0", "boman": "-4.48", "helix": "0.0", "turn_pct": "0.0", "sheet": "1.0" }, { "id": "aceip1010", "seq": "VIEKYP", "length": "6", "detail": "Casein | Milk (Casein)", "source": "Milk", "ic50": "0.1 μM", "reference": "Angiotensin converting enzyme inhibitory peptides derived from food proteins: biochemistry, bioactivity and production.; Langmuir monolayers of a hydrogenated\/fluorinated catanionic surfactant: from the macroscopic to the nanoscopic size scale.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.2174\/138161207780363068; 10.1021\/la900593c; 10.1016\/j.foodchem.2012.09.092", "pubmedid": "17430180 19449890 23194537", "mw": "747.88", "pi": "5.97", "charge_ph7": "-0.27", "gravy": "-0.2667", "instability": "102.13", "hydrophobic": "0.5", "boman": "-0.9333", "helix": "0.3333", "turn_pct": "0.1667", "sheet": "0.5" }, { "id": "aceip1011", "seq": "VIF", "length": "3", "detail": "ND", "source": "Milk", "ic50": "7.5 μM", "reference": "Quantitative structure-activity relationship study of bitter di- and tri-peptides including relationship with angiotensin I-converting enzyme inhibitory activity.; QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.; Review on the angiotensin-I-converting enzyme (ACE) inhibitor peptides from marine proteins.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1002\/psc.800; 10.1007\/s00894-010-0862-x; 10.1007\/s12010-012-0024-y; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "17117396 20941517 23271625 23871047", "mw": "377.48", "pi": "5.49", "charge_ph7": "-0.27", "gravy": "3.8333", "instability": "6.67", "hydrophobic": "1.0", "boman": "-3.98", "helix": "0.0", "turn_pct": "0.0", "sheet": "1.0" }, { "id": "aceip1012", "seq": "VIGSPPQIN", "length": "9", "detail": "ND", "source": "ND", "ic50": "1000 μM", "reference": "QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1007\/s00894-010-0862-x; 10.1016\/j.foodchem.2012.09.092", "pubmedid": "20941517 23194537", "mw": "924.05", "pi": "5.49", "charge_ph7": "-0.27", "gravy": "0.2", "instability": "100.51", "hydrophobic": "0.5556", "boman": "-1.2222", "helix": "0.0", "turn_pct": "0.5556", "sheet": "0.3333" }, { "id": "aceip1013", "seq": "VIIF", "length": "4", "detail": "Fish (Sardine fermented sauce)", "source": "Fish", "ic50": "0.0027 mg\/ml", "reference": "Review on the angiotensin-I-converting enzyme (ACE) inhibitor peptides from marine proteins.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1007\/s12010-012-0024-y; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "23271625 23871047", "mw": "490.64", "pi": "5.49", "charge_ph7": "-0.27", "gravy": "4.0", "instability": "7.5", "hydrophobic": "1.0", "boman": "-4.215", "helix": "0.0", "turn_pct": "0.0", "sheet": "1.0" }, { "id": "aceip1014", "seq": "VIKP", "length": "4", "detail": "Milk (human)", "source": "Milk", "ic50": null, "reference": "What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1016\/j.foodchem.2013.05.140", "pubmedid": "23871047", "mw": "455.59", "pi": "8.72", "charge_ph7": "0.73", "gravy": "0.8", "instability": "-32.58", "hydrophobic": "0.75", "boman": "-1.845", "helix": "0.25", "turn_pct": "0.25", "sheet": "0.5" }, { "id": "aceip1015", "seq": "VIPEL", "length": "5", "detail": "Pork", "source": "Porcine", "ic50": "799.24 μM", "reference": "Angiotensin I-converting enzyme inhibitory peptides generated from in vitro gastrointestinal digestion of pork meat.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1021\/jf904204n; 10.1016\/j.foodchem.2012.09.092; 10.1080\/10408398.2012.664829", "pubmedid": "20151679 23194537 24915368", "mw": "569.69", "pi": "4.05", "charge_ph7": "-1.26", "gravy": "1.48", "instability": "37.0", "hydrophobic": "0.8", "boman": "-2.448", "helix": "0.4", "turn_pct": "0.2", "sheet": "0.6" }, { "id": "aceip1016", "seq": "VIY", "length": "3", "detail": "Milk (human)", "source": "Milk", "ic50": "<20 mM", "reference": "Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Antihypertensive effect of angiotensin I-converting enzyme inhibitory peptides from a sesame protein hydrolysate in spontaneously hypertensive rats.; Antihypertensive peptides from food proteins: a review.; Vegetable foods: a cheap source of proteins and peptides with antihypertensive, antioxidant, and other less occurrence bioactivities.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1021\/jf051263l; 10.1271\/bbb.70.1118; 10.1039\/c2fo10192k; 10.1016\/j.talanta.2012.12.041; 10.1016\/j.foodchem.2013.05.140; 10.1080\/10408398.2012.664829", "pubmedid": "16448176 16717411 22249830 23598136 23871047 24915368", "mw": "393.48", "pi": "5.49", "charge_ph7": "-0.27", "gravy": "2.4667", "instability": "6.67", "hydrophobic": "0.6667", "boman": "-2.94", "helix": "0.0", "turn_pct": "0.0", "sheet": "1.0" }, { "id": "aceip1017", "seq": "VK", "length": "2", "detail": "Casein", "source": "Milk", "ic50": "<20 mM", "reference": "Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Model of the exofacial substrate-binding site and helical folding of the human Glut1 glucose transporter based on scanning mutagenesis.; Peptides with angiotensin I converting enzyme (ACE) inhibitory activity generated from porcine skeletal muscle proteins by the action of meat-borne Lactobacillus.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1021\/jf051263l; 10.1021\/bi900521n; 10.1016\/j.jprot.2013.06.023; 10.1080\/10408398.2012.664829", "pubmedid": "16448176 19449892 23806758 24915368", "mw": "245.32", "pi": "8.72", "charge_ph7": "0.73", "gravy": "0.15", "instability": "-9.4", "hydrophobic": "0.5", "boman": "-1.23", "helix": "0.5", "turn_pct": "0.0", "sheet": "0.5" }, { "id": "aceip1018", "seq": "VKAGF", "length": "5", "detail": "Rabbit", "source": "Mammal", "ic50": "20.3 μM", "reference": "Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1080\/10408398.2012.664829", "pubmedid": "24915368", "mw": "520.62", "pi": "8.72", "charge_ph7": "0.73", "gravy": "0.9", "instability": "2.24", "hydrophobic": "0.6", "boman": "-1.638", "helix": "0.4", "turn_pct": "0.2", "sheet": "0.4" }, { "id": "aceip1019", "seq": "VKK", "length": "3", "detail": "Milk", "source": "Milk", "ic50": "0.036 mg\/ml", "reference": "What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1016\/j.foodchem.2013.05.140", "pubmedid": "23871047", "mw": "373.49", "pi": "10.0", "charge_ph7": "1.73", "gravy": "-1.2", "instability": "-2.93", "hydrophobic": "0.3333", "boman": "-0.2933", "helix": "0.6667", "turn_pct": "0.0", "sheet": "0.3333" }, { "id": "aceip1020", "seq": "VKKVLGNP", "length": "8", "detail": "Milk (Fermented Milk)", "source": "Milk", "ic50": "28.5 μM", "reference": "Angiotensin-I converting enzyme inhibitory peptide derived from porcine skeletal muscle myosin and its antihypertensive activity in spontaneously hypertensive rats.; Antihypertensive peptides from food proteins: a review.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1111\/j.1750-3841.2007.00571.x; 10.1039\/c2fo10192k; 10.1016\/j.foodchem.2012.09.092; 10.1080\/10408398.2012.664829", "pubmedid": "18034756 22249830 23194537 24915368", "mw": "854.05", "pi": "10.0", "charge_ph7": "1.73", "gravy": "-0.1375", "instability": "-19.68", "hydrophobic": "0.5", "boman": "-1.145", "helix": "0.375", "turn_pct": "0.375", "sheet": "0.375" }, { "id": "aceip1021", "seq": "VKP", "length": "3", "detail": "Milk (bovine)", "source": "Milk", "ic50": "0.036 mg\/ml", "reference": "Vegetable foods: a cheap source of proteins and peptides with antihypertensive, antioxidant, and other less occurrence bioactivities.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1016\/j.talanta.2012.12.041; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "23598136 23871047", "mw": "342.43", "pi": "8.72", "charge_ph7": "0.73", "gravy": "-0.4333", "instability": "-28.07", "hydrophobic": "0.6667", "boman": "-0.82", "helix": "0.3333", "turn_pct": "0.3333", "sheet": "0.3333" }, { "id": "aceip1022", "seq": "VL", "length": "2", "detail": "Pork", "source": "Porcine", "ic50": "13 μM", "reference": "Quantitative structure-activity relationship study of bitter di- and tri-peptides including relationship with angiotensin I-converting enzyme inhibitory activity.; Three-dimensional holograph vector of atomic interaction field (3D-HoVAIF): a novel rotation-translation invariant 3D structure descriptor and its applications to peptides.; Vegetable foods: a cheap source of proteins and peptides with antihypertensive, antioxidant, and other less occurrence bioactivities.", "doi": "10.1002\/psc.800; 10.1002\/psc.892; 10.1016\/j.talanta.2012.12.041", "pubmedid": "17117396 17654623 23598136", "mw": "230.3", "pi": "5.49", "charge_ph7": "-0.27", "gravy": "4.0", "instability": "5.0", "hydrophobic": "1.0", "boman": "-4.48", "helix": "0.5", "turn_pct": "0.0", "sheet": "1.0" }, { "id": "aceip1023", "seq": "VLAQYK", "length": "6", "detail": "Soybean", "source": "Legume", "ic50": "0 μM", "reference": "Strategies for designing novel functional meat products.; Purification and identification of angiotensin converting enzyme inhibitory peptides from beef hydrolysates.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1016\/j.meatsci.2006.04.028; 10.1016\/j.meatsci.2004.10.014; 10.1080\/10408398.2012.664829", "pubmedid": "22062731 22063143 24915368", "mw": "720.86", "pi": "8.56", "charge_ph7": "0.73", "gravy": "0.1833", "instability": "-4.23", "hydrophobic": "0.5", "boman": "-1.2817", "helix": "0.5", "turn_pct": "0.0", "sheet": "0.5" }, { "id": "aceip1024", "seq": "VLDTDYK", "length": "7", "detail": "Milk (bovine) | Garlic | Pork | Chicken", "source": "Milk | Plants | Porcine | Chicken", "ic50": "946 μM", "reference": "Angiotensin I-converting enzyme inhibitory properties of whey protein digests: concentration and characterization of active peptides.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1017\/s0022029999003982; 10.1016\/j.foodchem.2012.09.092", "pubmedid": "10717843 23194537", "mw": "852.93", "pi": "4.21", "charge_ph7": "-1.27", "gravy": "-0.7", "instability": "-12.9", "hydrophobic": "0.2857", "boman": "-0.5171", "helix": "0.2857", "turn_pct": "0.2857", "sheet": "0.5714" }, { "id": "aceip1025", "seq": "VLGP", "length": "4", "detail": "ND", "source": "ND", "ic50": null, "reference": "Enterococcus faecalis strains from food, environmental, and clinical origin produce ACE-inhibitory peptides and other bioactive peptides during growth in bovine skim milk.", "doi": "10.1016\/j.ijfoodmicro.2013.06.019", "pubmedid": "23845432", "mw": "384.47", "pi": "5.49", "charge_ph7": "-0.27", "gravy": "1.5", "instability": "7.5", "hydrophobic": "0.75", "boman": "-2.475", "helix": "0.25", "turn_pct": "0.5", "sheet": "0.5" }, { "id": "aceip1026", "seq": "VLGPVRGPFP", "length": "10", "detail": "Pork", "source": "Porcine", "ic50": "137 μM", "reference": "Antihypertensive peptides: production, bioavailability and incorporation into foods.; Antihypertensive peptides from food proteins: a review.; Enterococcus faecalis strains from food, environmental, and clinical origin produce ACE-inhibitory peptides and other bioactive peptides during growth in bovine skim milk.", "doi": "10.1016\/j.cis.2010.11.001; 10.1039\/c2fo10192k; 10.1016\/j.ijfoodmicro.2013.06.019", "pubmedid": "21185549 22249830 23845432", "mw": "1038.24", "pi": "9.72", "charge_ph7": "0.73", "gravy": "0.49", "instability": "58.29", "hydrophobic": "0.7", "boman": "-1.514", "helix": "0.1", "turn_pct": "0.5", "sheet": "0.4" }, { "id": "aceip1027", "seq": "VLIVP", "length": "5", "detail": "Tuna", "source": "Fish", "ic50": "1.69 μM", "reference": "Angiotensin I-converting enzyme inhibitory peptide derived from glycinin, the 11S globulin of soybean (Glycine max).; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.; Vegetable foods: a cheap source of proteins and peptides with antihypertensive, antioxidant, and other less occurrence bioactivities.; Rational design of angiotensin-I-converting enzyme inhibitory peptides by integrating in silico modeling and an in vitro assay.", "doi": "10.1021\/jf060264q; 10.1016\/j.foodchem.2012.09.092; 10.1016\/j.talanta.2012.12.041; 10.1002\/cmdc.201300132", "pubmedid": "16786999 23194537 23598136 23740817", "mw": "539.71", "pi": "5.49", "charge_ph7": "-0.27", "gravy": "3.02", "instability": "29.54", "hydrophobic": "1.0", "boman": "-3.584", "helix": "0.2", "turn_pct": "0.2", "sheet": "0.8" }, { "id": "aceip1028", "seq": "VLNENL", "length": "6", "detail": "Casein | Pork", "source": "Milk | Porcine", "ic50": null, "reference": "Enterococcus faecalis strains from food, environmental, and clinical origin produce ACE-inhibitory peptides and other bioactive peptides during growth in bovine skim milk.", "doi": "10.1016\/j.ijfoodmicro.2013.06.019", "pubmedid": "23845432", "mw": "700.78", "pi": "4.05", "charge_ph7": "-1.26", "gravy": "0.2167", "instability": "8.33", "hydrophobic": "0.5", "boman": "-1.5", "helix": "0.5", "turn_pct": "0.3333", "sheet": "0.5" }, { "id": "aceip1029", "seq": "VLP", "length": "3", "detail": "Yeast", "source": "Fungi", "ic50": "<10 μM", "reference": "Inhibition of angiotensin-converting enzyme by synthetic peptide fragments of various beta-caseins.; Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Bioactive peptides in amaranth (Amaranthus hypochondriacus) seed.; Peptides with angiotensin I converting enzyme (ACE) inhibitory activity generated from porcine skeletal muscle proteins by the action of meat-borne Lactobacillus.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1021\/jf051263l; 10.1021\/jf072911z; 10.1016\/j.jprot.2013.06.023; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "1368548 16448176 18211015 23806758 23871047", "mw": "327.42", "pi": "5.49", "charge_ph7": "-0.27", "gravy": "2.1333", "instability": "70.87", "hydrophobic": "1.0", "boman": "-2.9867", "helix": "0.3333", "turn_pct": "0.3333", "sheet": "0.6667" }, { "id": "aceip1030", "seq": "VLPEI", "length": "5", "detail": "Milk (human) | Chicken", "source": "Milk | Chicken", "ic50": "46.56>1000 μM", "reference": "Angiotensin I-converting enzyme inhibitory peptides generated from in vitro gastrointestinal digestion of pork meat.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1021\/jf904204n; 10.1080\/10408398.2012.664829", "pubmedid": "20151679 24915368", "mw": "569.69", "pi": "4.05", "charge_ph7": "-1.26", "gravy": "1.48", "instability": "119.8", "hydrophobic": "0.8", "boman": "-2.448", "helix": "0.4", "turn_pct": "0.2", "sheet": "0.6" }, { "id": "aceip1031", "seq": "VLPIP", "length": "5", "detail": "Milk (human)", "source": "Milk", "ic50": "31 μM", "reference": "Inhibition of angiotensin-converting enzyme by synthetic peptide fragments of various beta-caseins.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "1368548 23194537", "mw": "537.69", "pi": "5.49", "charge_ph7": "-0.27", "gravy": "1.86", "instability": "40.76", "hydrophobic": "1.0", "boman": "-2.776", "helix": "0.2", "turn_pct": "0.4", "sheet": "0.6" }, { "id": "aceip1032", "seq": "VLPIPQ", "length": "6", "detail": "Milk (human)", "source": "Milk", "ic50": "5300 μM", "reference": "Inhibition of angiotensin-converting enzyme by synthetic peptide fragments of various beta-caseins.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "1368548 23194537", "mw": "665.82", "pi": "5.49", "charge_ph7": "-0.27", "gravy": "0.9667", "instability": "67.73", "hydrophobic": "0.8333", "boman": "-2.0867", "helix": "0.1667", "turn_pct": "0.3333", "sheet": "0.5" }, { "id": "aceip1033", "seq": "VLPVPQK", "length": "7", "detail": "Tuna", "source": "Fish", "ic50": null, "reference": "Enterococcus faecalis strains from food, environmental, and clinical origin produce ACE-inhibitory peptides and other bioactive peptides during growth in bovine skim milk.", "doi": "10.1016\/j.ijfoodmicro.2013.06.019", "pubmedid": "23845432", "mw": "779.97", "pi": "8.72", "charge_ph7": "0.73", "gravy": "0.2286", "instability": "118.63", "hydrophobic": "0.7143", "boman": "-1.4371", "helix": "0.2857", "turn_pct": "0.2857", "sheet": "0.4286" }, { "id": "aceip1034", "seq": "VLPYP", "length": "5", "detail": "Tuna", "source": "Fish", "ic50": "36 μM", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "23194537", "mw": "587.71", "pi": "5.49", "charge_ph7": "-0.27", "gravy": "0.7", "instability": "71.2", "hydrophobic": "0.8", "boman": "-1.764", "helix": "0.2", "turn_pct": "0.4", "sheet": "0.6" }, { "id": "aceip1035", "seq": "VLPYPV", "length": "6", "detail": "Tuna", "source": "Fish", "ic50": "420 μM", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "23194537", "mw": "686.84", "pi": "5.49", "charge_ph7": "-0.27", "gravy": "1.2833", "instability": "93.1", "hydrophobic": "0.8333", "boman": "-2.1433", "helix": "0.1667", "turn_pct": "0.3333", "sheet": "0.6667" }, { "id": "aceip1036", "seq": "VLY", "length": "3", "detail": "Pork", "source": "Porcine", "ic50": "<20 mM", "reference": "Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.", "doi": "10.1021\/jf051263l", "pubmedid": "16448176", "mw": "393.48", "pi": "5.49", "charge_ph7": "-0.27", "gravy": "2.2333", "instability": "6.67", "hydrophobic": "0.6667", "boman": "-2.94", "helix": "0.3333", "turn_pct": "0.0", "sheet": "1.0" }, { "id": "aceip1037", "seq": "VMDKPQG", "length": "7", "detail": "Milk", "source": "Milk", "ic50": "38.9 μM", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.; Vegetable foods: a cheap source of proteins and peptides with antihypertensive, antioxidant, and other less occurrence bioactivities.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1016\/j.foodchem.2012.09.092; 10.1016\/j.talanta.2012.12.041; 10.1080\/10408398.2012.664829", "pubmedid": "23194537 23598136 24915368", "mw": "773.9", "pi": "5.81", "charge_ph7": "-0.27", "gravy": "-0.9714", "instability": "13.19", "hydrophobic": "0.4286", "boman": "-0.3871", "helix": "0.2857", "turn_pct": "0.4286", "sheet": "0.1429" }, { "id": "aceip1038", "seq": "VMP", "length": "3", "detail": "Milk (bovine)", "source": "Milk", "ic50": "29 μM", "reference": "Inhibition of angiotensin-converting enzyme by synthetic peptide fragments of various beta-caseins.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1016\/j.foodchem.2013.05.140", "pubmedid": "1368548 23871047", "mw": "345.46", "pi": "5.49", "charge_ph7": "-0.27", "gravy": "1.5", "instability": "153.13", "hydrophobic": "1.0", "boman": "-2.13", "helix": "0.3333", "turn_pct": "0.3333", "sheet": "0.3333" }, { "id": "aceip1039", "seq": "VNEL", "length": "4", "detail": "Milk (human)", "source": "Milk", "ic50": null, "reference": "Hot topic: Changes in angiotensin-converting enzyme inhibition and concentrations of the tripeptides Val-Pro-Pro and Ile-Pro-Pro during ripening of different Swiss cheese varieties.", "doi": "10.3168\/jds.2008-1531", "pubmedid": "19233775", "mw": "473.52", "pi": "4.05", "charge_ph7": "-1.26", "gravy": "0.25", "instability": "7.5", "hydrophobic": "0.5", "boman": "-1.425", "helix": "0.5", "turn_pct": "0.25", "sheet": "0.5" }, { "id": "aceip1040", "seq": "VP", "length": "2", "detail": "Milk-Cheese (Sheep milk and cheeses proteins)", "source": "Milk", "ic50": "<20 mM", "reference": "Binding of peptide substrates and inhibitors of angiotensin-converting enzyme. Importance of the COOH-terminal dipeptide sequence.; Angiotensin I-converting enzyme inhibitory activity and insulin secretion stimulative activity of fermented fish sauce.; Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Three-dimensional holograph vector of atomic interaction field (3D-HoVAIF): a novel rotation-translation invariant 3D structure descriptor and its applications to peptides.; Antihypertensive effect of peptide-enriched soy sauce-like seasoning and identification of its angiotensin I-converting enzyme inhibitory substances.; QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.; Vegetable foods: a cheap source of proteins and peptides with antihypertensive, antioxidant, and other less occurrence bioactivities.; Peptides with angiotensin I converting enzyme (ACE) inhibitory activity generated from porcine skeletal muscle proteins by the action of meat-borne Lactobacillus.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1016\/S1389-1723(03)70138-8; 10.1021\/jf051263l; 10.1002\/psc.892; 10.1021\/jf903261h; 10.1007\/s00894-010-0862-x; 10.1016\/j.talanta.2012.12.041; 10.1016\/j.jprot.2013.06.023; 10.1016\/j.foodchem.2013.05.140; 10.1080\/10408398.2012.664829", "pubmedid": "6243277 16233562 16448176 17654623 19994857 20941517 23598136 23806758 23871047 24915368", "mw": "214.26", "pi": "5.49", "charge_ph7": "-0.27", "gravy": "1.3", "instability": "101.3", "hydrophobic": "1.0", "boman": "-2.02", "helix": "0.0", "turn_pct": "0.5", "sheet": "0.5" }, { "id": "aceip1041", "seq": "VPFGVG", "length": "6", "detail": "Milk (bovine) | Casein", "source": "Milk", "ic50": "336 μM", "reference": "Isolation and characterization of a low molecular weight peptide contained in sourdough.", "doi": "10.1021\/jf070069r", "pubmedid": "17516655", "mw": "574.67", "pi": "5.49", "charge_ph7": "-0.27", "gravy": "1.4667", "instability": "58.38", "hydrophobic": "0.6667", "boman": "-2.1567", "helix": "0.0", "turn_pct": "0.5", "sheet": "0.5" }, { "id": "aceip1042", "seq": "VPK", "length": "3", "detail": "Milk (bovine) | Cereals | Pork | Chicken", "source": "Milk | Cereal | Porcine | Chicken", "ic50": "0 μM", "reference": "Angiotensin I-converting enzyme inhibitory properties of whey protein digests: concentration and characterization of active peptides.", "doi": "10.1017\/s0022029999003982", "pubmedid": "10717843", "mw": "342.43", "pi": "8.72", "charge_ph7": "0.73", "gravy": "-0.4333", "instability": "70.87", "hydrophobic": "0.6667", "boman": "-0.82", "helix": "0.3333", "turn_pct": "0.3333", "sheet": "0.3333" }, { "id": "aceip1043", "seq": "VPLGTQYT", "length": "8", "detail": "ND", "source": "ND", "ic50": null, "reference": "Hot topic: Changes in angiotensin-converting enzyme inhibition and concentrations of the tripeptides Val-Pro-Pro and Ile-Pro-Pro during ripening of different Swiss cheese varieties.", "doi": "10.3168\/jds.2008-1531", "pubmedid": "19233775", "mw": "877.98", "pi": "5.49", "charge_ph7": "-0.27", "gravy": "-0.025", "instability": "-7.25", "hydrophobic": "0.375", "boman": "-0.985", "helix": "0.125", "turn_pct": "0.25", "sheet": "0.625" }, { "id": "aceip1044", "seq": "VPP", "length": "3", "detail": "ND", "source": "ND", "ic50": "<20 mM", "reference": "Antihypertensive effect of sour milk and peptides isolated from it that are inhibitors to angiotensin I-converting enzyme.; Purification and characterization of angiotensin I-converting enzyme inhibitors from sour milk.; Randomized controlled trial of sour milk on blood pressure in borderline hypertensive men.; Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Bioactive peptides in amaranth (Amaranthus hypochondriacus) seed.; Evaluation of the allergenicity of goat milk, cow milk, and their lactosera in a guinea pig model.; Antihypertensive peptides: production, bioavailability and incorporation into foods.; LC-MS\/MS quantification of bioactive angiotensin I-converting enzyme inhibitory peptides in rye malt sourdoughs.; Antihypertensive peptides from food proteins: a review.; VPPIPP and IPPVPP: two hexapeptides innovated to exert antihypertensive activity.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.; Comparison of analytical methods to assay inhibitors of angiotensin I-converting enzyme.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.3168\/jds.S0022-0302(95)76745-5; 10.3168\/jds.S0022-0302(95)76689-9; 10.1016\/j.amjhyper.2004.03.674; 10.1021\/jf051263l; 10.1021\/jf072911z; 10.3168\/jds.2008-1125; 10.1016\/j.cis.2010.11.001; 10.1021\/jf2033329; 10.1039\/c2fo10192k; 10.1371\/journal.pone.0062384; 10.1016\/j.foodchem.2013.05.140; 10.1016\/j.foodchem.2013.06.048; 10.1080\/10408398.2012.664829", "pubmedid": "7673515 7790570 15288885 16448176 18211015 19233776 21185549 21985248 22249830 23638059 23871047 23993489 24915368", "mw": "311.38", "pi": "5.49", "charge_ph7": "-0.27", "gravy": "0.3333", "instability": "135.07", "hydrophobic": "1.0", "boman": "-1.3467", "helix": "0.0", "turn_pct": "0.6667", "sheet": "0.3333" }, { "id": "aceip1045", "seq": "VPPFLQPEV", "length": "9", "detail": "Synthesized | Fish (Alaska pollack) | Cereals", "source": "Synthesized | Fish | Cereal", "ic50": null, "reference": "Casein fermentate of Lactobacillus animalis DPC6134 contains a range of novel propeptide angiotensin-converting enzyme inhibitors.", "doi": "10.1128\/AEM.00096-07", "pubmedid": "17483275", "mw": "1025.2", "pi": "4.05", "charge_ph7": "-1.26", "gravy": "0.3556", "instability": "150.02", "hydrophobic": "0.7778", "boman": "-1.4422", "helix": "0.2222", "turn_pct": "0.3333", "sheet": "0.4444" }, { "id": "aceip1046", "seq": "VPPIPP", "length": "6", "detail": "ND", "source": "ND", "ic50": "34.71 %", "reference": "The potential role of milk-derived peptides in cardiovascular disease.; VPPIPP and IPPVPP: two hexapeptides innovated to exert antihypertensive activity.", "doi": "10.1039\/c1fo10017c; 10.1371\/journal.pone.0062384", "pubmedid": "21779574 23638059", "mw": "618.76", "pi": "5.49", "charge_ph7": "-0.27", "gravy": "0.3833", "instability": "99.83", "hydrophobic": "1.0", "boman": "-1.4933", "helix": "0.0", "turn_pct": "0.6667", "sheet": "0.3333" }, { "id": "aceip1047", "seq": "VPQ", "length": "3", "detail": "Milk (bovine)", "source": "Milk", "ic50": null, "reference": "Angiotensin I-converting-enzyme-inhibitory and antibacterial peptides from Lactobacillus helveticus PR4 proteinase-hydrolyzed caseins of milk from six species.", "doi": "10.1128\/AEM.69.9.5297-5305.2003", "pubmedid": "12957917", "mw": "342.39", "pi": "5.49", "charge_ph7": "-0.27", "gravy": "-0.3", "instability": "135.07", "hydrophobic": "0.6667", "boman": "-0.8933", "helix": "0.0", "turn_pct": "0.3333", "sheet": "0.3333" }, { "id": "aceip1048", "seq": "VPQP", "length": "4", "detail": "ND", "source": "ND", "ic50": ">1000 μM", "reference": "Inhibition of angiotensin-converting enzyme by synthetic peptide fragments of various beta-caseins.", "doi": "", "pubmedid": "1368548", "mw": "439.51", "pi": "5.49", "charge_ph7": "-0.27", "gravy": "-0.625", "instability": "151.95", "hydrophobic": "0.75", "boman": "-0.67", "helix": "0.0", "turn_pct": "0.5", "sheet": "0.25" }, { "id": "aceip1049", "seq": "VPQPIP", "length": "6", "detail": "Skate", "source": "Fish", "ic50": "290 μM", "reference": "Inhibition of angiotensin-converting enzyme by synthetic peptide fragments of various beta-caseins.", "doi": "", "pubmedid": "1368548", "mw": "649.78", "pi": "5.49", "charge_ph7": "-0.27", "gravy": "0.0667", "instability": "99.83", "hydrophobic": "0.8333", "boman": "-1.2667", "helix": "0.0", "turn_pct": "0.5", "sheet": "0.3333" }, { "id": "aceip1050", "seq": "VPYPQRDMPIQA", "length": "12", "detail": "Pork", "source": "Porcine", "ic50": null, "reference": "Casein fermentate of Lactobacillus animalis DPC6134 contains a range of novel propeptide angiotensin-converting enzyme inhibitors.", "doi": "10.1128\/AEM.00096-07", "pubmedid": "17483275", "mw": "1414.63", "pi": "5.81", "charge_ph7": "-0.27", "gravy": "-0.725", "instability": "88.17", "hydrophobic": "0.5833", "boman": "-0.4883", "helix": "0.1667", "turn_pct": "0.3333", "sheet": "0.25" }, { "id": "aceip1051", "seq": "VQV", "length": "3", "detail": "Soybean", "source": "Legume", "ic50": "<20 mM", "reference": "Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.", "doi": "10.1021\/jf051263l", "pubmedid": "16448176", "mw": "344.41", "pi": "5.49", "charge_ph7": "-0.27", "gravy": "1.6333", "instability": "-18.47", "hydrophobic": "0.6667", "boman": "-2.24", "helix": "0.0", "turn_pct": "0.0", "sheet": "0.6667" }, { "id": "aceip1052", "seq": "VR", "length": "2", "detail": "Milk (bovine) | Cereals (Wheat) | Pork", "source": "Milk | Cereal | Porcine", "ic50": "0.332 mg\/ml", "reference": "Identification of novel angiotensin-converting enzyme-inhibitory peptides from ovine milk proteins by CE-MS and chromatographic techniques.; Review on the angiotensin-I-converting enzyme (ACE) inhibitor peptides from marine proteins.; Peptides with angiotensin I converting enzyme (ACE) inhibitory activity generated from porcine skeletal muscle proteins by the action of meat-borne Lactobacillus.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1002\/elps.200700324; 10.1007\/s12010-012-0024-y; 10.1016\/j.jprot.2013.06.023; 10.1080\/10408398.2012.664829", "pubmedid": "17948260 23271625 23806758 24915368", "mw": "273.33", "pi": "9.72", "charge_ph7": "0.73", "gravy": "-0.15", "instability": "5.0", "hydrophobic": "0.5", "boman": "-0.66", "helix": "0.0", "turn_pct": "0.0", "sheet": "0.5" }, { "id": "aceip1053", "seq": "VRGPFP", "length": "6", "detail": "Milk (human)", "source": "Milk", "ic50": "505.28 μM", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.; Enterococcus faecalis strains from food, environmental, and clinical origin produce ACE-inhibitory peptides and other bioactive peptides during growth in bovine skim milk.", "doi": "10.1016\/j.foodchem.2012.09.092; 10.1016\/j.ijfoodmicro.2013.06.019", "pubmedid": "23194537 23845432", "mw": "671.79", "pi": "9.72", "charge_ph7": "0.73", "gravy": "-0.1833", "instability": "58.38", "hydrophobic": "0.6667", "boman": "-0.8733", "helix": "0.0", "turn_pct": "0.5", "sheet": "0.3333" }, { "id": "aceip1054", "seq": "VRGPFPIIV", "length": "9", "detail": "ND", "source": "ND", "ic50": "395 μM", "reference": "Antihypertensive peptides: production, bioavailability and incorporation into foods.; Antihypertensive peptides from food proteins: a review.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.; Enterococcus faecalis strains from food, environmental, and clinical origin produce ACE-inhibitory peptides and other bioactive peptides during growth in bovine skim milk.", "doi": "10.1016\/j.cis.2010.11.001; 10.1039\/c2fo10192k; 10.1016\/j.foodchem.2012.09.092; 10.1016\/j.ijfoodmicro.2013.06.019", "pubmedid": "21185549 22249830 23194537 23845432", "mw": "997.23", "pi": "9.72", "charge_ph7": "0.73", "gravy": "1.3444", "instability": "32.82", "hydrophobic": "0.7778", "boman": "-2.1244", "helix": "0.0", "turn_pct": "0.3333", "sheet": "0.5556" }, { "id": "aceip1055", "seq": "VRK", "length": "3", "detail": "ND", "source": "ND", "ic50": "700 μM", "reference": "What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1016\/j.foodchem.2013.05.140", "pubmedid": "23871047", "mw": "401.5", "pi": "11.0", "charge_ph7": "1.73", "gravy": "-1.4", "instability": "6.67", "hydrophobic": "0.3333", "boman": "0.0867", "helix": "0.3333", "turn_pct": "0.0", "sheet": "0.3333" }, { "id": "aceip1056", "seq": "VRP", "length": "3", "detail": "ND", "source": "ND", "ic50": "<20 mM", "reference": "Inhibition of angiotensin-converting enzyme by synthetic peptide fragments of human kappa-casein.; Angiotensin I-converting enzyme inhibitory peptides derived from bonito bowels autolysate.; Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Bioactive peptides in amaranth (Amaranthus hypochondriacus) seed.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1271\/bbb.57.695; 10.1021\/jf051263l; 10.1021\/jf072911z; 10.1016\/j.foodchem.2013.05.140; 10.1080\/10408398.2012.664829", "pubmedid": "1368540 7763772 16448176 18211015 23871047 24915368", "mw": "370.45", "pi": "9.72", "charge_ph7": "0.73", "gravy": "-0.6333", "instability": "70.87", "hydrophobic": "0.6667", "boman": "-0.44", "helix": "0.0", "turn_pct": "0.3333", "sheet": "0.3333" }, { "id": "aceip1057", "seq": "VRYL", "length": "4", "detail": "ND", "source": "ND", "ic50": "24.1 μM", "reference": "Angiotensin converting enzyme inhibitory peptides derived from food proteins: biochemistry, bioactivity and production.", "doi": "10.2174\/138161207780363068", "pubmedid": "17430180", "mw": "549.66", "pi": "8.72", "charge_ph7": "0.73", "gravy": "0.55", "instability": "-11.35", "hydrophobic": "0.5", "boman": "-1.525", "helix": "0.25", "turn_pct": "0.0", "sheet": "0.75" }, { "id": "aceip1058", "seq": "VSKVKET", "length": "7", "detail": "ND", "source": "ND", "ic50": null, "reference": "Enterococcus faecalis strains from food, environmental, and clinical origin produce ACE-inhibitory peptides and other bioactive peptides during growth in bovine skim milk.", "doi": "10.1016\/j.ijfoodmicro.2013.06.019", "pubmedid": "23845432", "mw": "789.92", "pi": "8.56", "charge_ph7": "0.73", "gravy": "-0.6286", "instability": "-7.67", "hydrophobic": "0.2857", "boman": "-0.3114", "helix": "0.4286", "turn_pct": "0.1429", "sheet": "0.4286" }, { "id": "aceip1059", "seq": "VSP", "length": "3", "detail": "Casein", "source": "Milk", "ic50": "<10 μM", "reference": "Structures and activity of angiotensin-converting enzyme inhibitors in an alpha-zein hydrolysate.; Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Bioactive peptides in amaranth (Amaranthus hypochondriacus) seed.; Cellular membrane disruption by amyloid fibrils involved intermolecular disulfide cross-linking.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1021\/jf051263l; 10.1021\/jf072911z; 10.1021\/bi900219c; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "1368684 16448176 18211015 19449893 23871047", "mw": "301.34", "pi": "5.49", "charge_ph7": "-0.27", "gravy": "0.6", "instability": "153.13", "hydrophobic": "0.6667", "boman": "-1.0667", "helix": "0.0", "turn_pct": "0.6667", "sheet": "0.3333" }, { "id": "aceip1060", "seq": "VSW", "length": "3", "detail": "Milk-Cheese (Sheep milk and cheeses proteins)", "source": "Milk", "ic50": "<20 mM", "reference": "Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.", "doi": "10.1021\/jf051263l", "pubmedid": "16448176", "mw": "390.43", "pi": "5.49", "charge_ph7": "-0.27", "gravy": "0.8333", "instability": "6.67", "hydrophobic": "0.6667", "boman": "-1.8433", "helix": "0.0", "turn_pct": "0.3333", "sheet": "0.6667" }, { "id": "aceip1061", "seq": "VTP", "length": "3", "detail": "Milk (Sheep raw milk cheese (synthesised))", "source": "Milk", "ic50": null, "reference": "Vegetable foods: a cheap source of proteins and peptides with antihypertensive, antioxidant, and other less occurrence bioactivities.", "doi": "10.1016\/j.talanta.2012.12.041", "pubmedid": "23598136", "mw": "315.37", "pi": "5.49", "charge_ph7": "-0.27", "gravy": "0.6333", "instability": "-21.63", "hydrophobic": "0.6667", "boman": "-1.26", "helix": "0.0", "turn_pct": "0.3333", "sheet": "0.6667" }, { "id": "aceip1062", "seq": "VTPALR", "length": "6", "detail": "Milk (bovine) | Fish (Alaska pollack) | Cereals (Wheat) | Pork | Chicken", "source": "Milk | Fish | Cereal | Porcine | Chicken", "ic50": "82.4 μM", "reference": "Novel angiotensin I-converting enzyme inhibitory peptides isolated from Alcalase hydrolysate of mung bean protein.; Vegetable foods: a cheap source of proteins and peptides with antihypertensive, antioxidant, and other less occurrence bioactivities.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1002\/psc.758; 10.1016\/j.talanta.2012.12.041; 10.1080\/10408398.2012.664829", "pubmedid": "16680798 23598136 24915368", "mw": "655.79", "pi": "9.72", "charge_ph7": "0.73", "gravy": "0.5", "instability": "58.38", "hydrophobic": "0.6667", "boman": "-1.2983", "helix": "0.3333", "turn_pct": "0.1667", "sheet": "0.5" }, { "id": "aceip1063", "seq": "VTR", "length": "3", "detail": "Synthesized | Fish (Alaska pollack) | Cereals", "source": "Synthesized | Fish | Cereal", "ic50": "<20 mM", "reference": "Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.", "doi": "10.1021\/jf051263l", "pubmedid": "16448176", "mw": "374.44", "pi": "9.72", "charge_ph7": "0.73", "gravy": "-0.3333", "instability": "-21.63", "hydrophobic": "0.3333", "boman": "-0.3533", "helix": "0.0", "turn_pct": "0.0", "sheet": "0.6667" }, { "id": "aceip1064", "seq": "VTSTAV", "length": "6", "detail": "Milk (human)", "source": "Milk", "ic50": "52 μM", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "23194537", "mw": "576.64", "pi": "5.49", "charge_ph7": "-0.27", "gravy": "1.3333", "instability": "-5.82", "hydrophobic": "0.5", "boman": "-1.4217", "helix": "0.1667", "turn_pct": "0.1667", "sheet": "0.6667" }, { "id": "aceip1065", "seq": "VTVNPYKWLP", "length": "10", "detail": "Milk (bovine) | Milk (human) | Amaranth | Cereals | Pork | Chicken connectin", "source": "Milk | Plants | Cereal | Porcine | Chicken", "ic50": "5.5 μM", "reference": "Novel angiotensin-converting enzyme (ACE) inhibitory peptides derived from boneless chicken leg meat.; Inhibition strength of short peptides derived from an ACE inhibitory peptide.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1021\/jf100977z; 10.1021\/jf202902r; 10.1016\/j.foodchem.2012.09.092", "pubmedid": "20509692 21923188 23194537", "mw": "1216.43", "pi": "8.56", "charge_ph7": "0.73", "gravy": "-0.13", "instability": "29.23", "hydrophobic": "0.6", "boman": "-1.173", "helix": "0.2", "turn_pct": "0.3", "sheet": "0.6" }, { "id": "aceip1066", "seq": "VTY", "length": "3", "detail": "Milk (Casein) | Yak", "source": "Milk | Mammal", "ic50": null, "reference": "Vegetable foods: a cheap source of proteins and peptides with antihypertensive, antioxidant, and other less occurrence bioactivities.", "doi": "10.1016\/j.talanta.2012.12.041", "pubmedid": "23598136", "mw": "381.42", "pi": "5.49", "charge_ph7": "-0.27", "gravy": "0.7333", "instability": "-21.63", "hydrophobic": "0.3333", "boman": "-1.2133", "helix": "0.0", "turn_pct": "0.0", "sheet": "1.0" }, { "id": "aceip1067", "seq": "VV", "length": "2", "detail": "Milk-Cheese (Goat milk protein and cheeses)", "source": "Milk", "ic50": null, "reference": "Three-dimensional holograph vector of atomic interaction field (3D-HoVAIF): a novel rotation-translation invariant 3D structure descriptor and its applications to peptides.", "doi": "10.1002\/psc.892", "pubmedid": "17654623", "mw": "216.28", "pi": "5.49", "charge_ph7": "-0.27", "gravy": "4.2", "instability": "5.0", "hydrophobic": "1.0", "boman": "-4.04", "helix": "0.0", "turn_pct": "0.0", "sheet": "1.0" }, { "id": "aceip1068", "seq": "VVF", "length": "3", "detail": "Casein | Milk (Digested milk products)", "source": "Milk", "ic50": "<20 mM", "reference": "Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.", "doi": "10.1021\/jf051263l", "pubmedid": "16448176", "mw": "363.45", "pi": "5.49", "charge_ph7": "-0.27", "gravy": "3.7333", "instability": "6.67", "hydrophobic": "1.0", "boman": "-3.6867", "helix": "0.0", "turn_pct": "0.0", "sheet": "1.0" }, { "id": "aceip1069", "seq": "VVPPA", "length": "5", "detail": "Pork", "source": "Porcine", "ic50": "79.43 μM", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.; Review on the angiotensin-I-converting enzyme (ACE) inhibitor peptides from marine proteins.; Vegetable foods: a cheap source of proteins and peptides with antihypertensive, antioxidant, and other less occurrence bioactivities.", "doi": "10.1016\/j.foodchem.2012.09.092; 10.1007\/s12010-012-0024-y; 10.1016\/j.talanta.2012.12.041", "pubmedid": "23194537 23271625 23598136", "mw": "481.59", "pi": "5.49", "charge_ph7": "-0.27", "gravy": "1.4", "instability": "123.56", "hydrophobic": "1.0", "boman": "-1.978", "helix": "0.2", "turn_pct": "0.4", "sheet": "0.4" }, { "id": "aceip1070", "seq": "VVPPFIQPE", "length": "9", "detail": "Soybean", "source": "Legume", "ic50": null, "reference": "Casein fermentate of Lactobacillus animalis DPC6134 contains a range of novel propeptide angiotensin-converting enzyme inhibitors.", "doi": "10.1128\/AEM.00096-07", "pubmedid": "17483275", "mw": "1025.2", "pi": "4.6", "charge_ph7": "-1.26", "gravy": "0.4333", "instability": "113.8", "hydrophobic": "0.7778", "boman": "-1.4422", "helix": "0.1111", "turn_pct": "0.3333", "sheet": "0.4444" }, { "id": "aceip1071", "seq": "VVRP", "length": "4", "detail": "Bonito", "source": "Fish", "ic50": "81 μM", "reference": "Inhibition of angiotensin-converting enzyme by synthetic peptide fragments of human kappa-casein.; Angiotensin converting enzyme inhibitory peptides derived from food proteins: biochemistry, bioactivity and production.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.2174\/138161207780363068; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "1368540 17430180 23871047", "mw": "469.58", "pi": "9.72", "charge_ph7": "0.73", "gravy": "0.575", "instability": "55.65", "hydrophobic": "0.75", "boman": "-1.34", "helix": "0.0", "turn_pct": "0.25", "sheet": "0.5" }, { "id": "aceip1072", "seq": "VVV", "length": "3", "detail": "Milk (human)", "source": "Milk", "ic50": null, "reference": "Quantitative structure-activity relationship study of bitter di- and tri-peptides including relationship with angiotensin I-converting enzyme inhibitory activity.; QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1002\/psc.800; 10.1007\/s00894-010-0862-x; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "17117396 20941517 23871047", "mw": "315.41", "pi": "5.49", "charge_ph7": "-0.27", "gravy": "4.2", "instability": "6.67", "hydrophobic": "1.0", "boman": "-4.04", "helix": "0.0", "turn_pct": "0.0", "sheet": "1.0" }, { "id": "aceip1073", "seq": "VVVPP", "length": "5", "detail": "Milk (bovine) | Milk | Cereals (Wheat) | Pork | Chicken", "source": "Milk | Cereal | Porcine | Chicken", "ic50": "284.4 μM", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "23194537", "mw": "509.64", "pi": "5.49", "charge_ph7": "-0.27", "gravy": "1.88", "instability": "85.04", "hydrophobic": "1.0", "boman": "-2.424", "helix": "0.0", "turn_pct": "0.4", "sheet": "0.6" }, { "id": "aceip1074", "seq": "VVVPPF", "length": "6", "detail": "Yak", "source": "Mammal", "ic50": ">1500 μM", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.; Enterococcus faecalis strains from food, environmental, and clinical origin produce ACE-inhibitory peptides and other bioactive peptides during growth in bovine skim milk.", "doi": "10.1016\/j.foodchem.2012.09.092; 10.1016\/j.ijfoodmicro.2013.06.019", "pubmedid": "23194537 23845432", "mw": "656.81", "pi": "5.49", "charge_ph7": "-0.27", "gravy": "2.0333", "instability": "104.63", "hydrophobic": "1.0", "boman": "-2.5167", "helix": "0.0", "turn_pct": "0.3333", "sheet": "0.6667" }, { "id": "aceip1075", "seq": "VVW", "length": "3", "detail": "Milk", "source": "Milk", "ic50": "22 μM", "reference": "Vegetable foods: a cheap source of proteins and peptides with antihypertensive, antioxidant, and other less occurrence bioactivities.", "doi": "10.1016\/j.talanta.2012.12.041", "pubmedid": "23598136", "mw": "402.49", "pi": "5.49", "charge_ph7": "-0.27", "gravy": "2.5", "instability": "6.67", "hydrophobic": "1.0", "boman": "-3.47", "helix": "0.0", "turn_pct": "0.0", "sheet": "1.0" }, { "id": "aceip1076", "seq": "VVY", "length": "3", "detail": "ND", "source": "ND", "ic50": "22 μM", "reference": "What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1016\/j.foodchem.2013.05.140; 10.1080\/10408398.2012.664829", "pubmedid": "23871047 24915368", "mw": "379.45", "pi": "5.49", "charge_ph7": "-0.27", "gravy": "2.3667", "instability": "-18.47", "hydrophobic": "0.6667", "boman": "-2.6467", "helix": "0.0", "turn_pct": "0.0", "sheet": "1.0" }, { "id": "aceip1077", "seq": "VVYPW", "length": "5", "detail": "Casein | Milk (human)", "source": "Milk", "ic50": "0.254 mg\/ml", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "23194537", "mw": "662.78", "pi": "5.49", "charge_ph7": "-0.27", "gravy": "0.92", "instability": "11.84", "hydrophobic": "0.8", "boman": "-2.054", "helix": "0.0", "turn_pct": "0.2", "sheet": "0.8" }, { "id": "aceip1078", "seq": "VVYPWT", "length": "6", "detail": "Cereals | Pork | Chicken", "source": "Cereal | Porcine | Chicken", "ic50": "6.02 μM", "reference": "Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1080\/10408398.2012.664829", "pubmedid": "24915368", "mw": "763.88", "pi": "5.49", "charge_ph7": "-0.27", "gravy": "0.65", "instability": "-13.52", "hydrophobic": "0.6667", "boman": "-1.6683", "helix": "0.0", "turn_pct": "0.1667", "sheet": "0.8333" }, { "id": "aceip1079", "seq": "VVYPWTQRF", "length": "9", "detail": "Milk", "source": "Milk", "ic50": "0.066 μM\/ml", "reference": "Antihypertensive peptides from food proteins: a review.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.; Review on the angiotensin-I-converting enzyme (ACE) inhibitor peptides from marine proteins.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1039\/c2fo10192k; 10.1016\/j.foodchem.2012.09.092; 10.1007\/s12010-012-0024-y; 10.1080\/10408398.2012.664829", "pubmedid": "22249830 23194537 23271625 24915368", "mw": "1195.37", "pi": "8.72", "charge_ph7": "0.73", "gravy": "-0.1444", "instability": "-14.06", "hydrophobic": "0.5556", "boman": "-0.99", "helix": "0.0", "turn_pct": "0.1111", "sheet": "0.6667" }, { "id": "aceip1080", "seq": "VW", "length": "2", "detail": "Milk (Fermented Milk)", "source": "Milk", "ic50": "0.0016 mM", "reference": "Structure and activity of angiotensin I converting enzyme inhibitory peptides from sake and sake lees.; Angiotensin I-converting enzyme inhibitory peptides derived from wakame (Undaria pinnatifida) and their antihypertensive effect in spontaneously hypertensive rats.; New antihypertensive peptides isolated from rapeseed.; Antihypertensive effects of Undaria pinnatifida (wakame) peptide on blood pressure in spontaneously hypertensive rats.; Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Three-dimensional holograph vector of atomic interaction field (3D-HoVAIF): a novel rotation-translation invariant 3D structure descriptor and its applications to peptides.; Bioactive peptides in amaranth (Amaranthus hypochondriacus) seed.; Isolation and identification of antihypertensive peptides from antarctic krill tail meat hydrolysate.; QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.; Inhibition strength of short peptides derived from an ACE inhibitory peptide.; Antihypertensive peptides from food proteins: a review.; Review on the angiotensin-I-converting enzyme (ACE) inhibitor peptides from marine proteins.; Vegetable foods: a cheap source of proteins and peptides with antihypertensive, antioxidant, and other less occurrence bioactivities.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.; Glycinyl-histidinyl-serine (GHS), a novel rapeseed protein-derived peptide has blood pressure-lowering effect in spontaneously hypertensive rats.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1271\/bbb.58.1767; 10.1021\/jf020482t; 10.1016\/s0196-9781(03)00174-8; 10.1016\/j.jnutbio.2003.11.004; 10.1021\/jf051263l; 10.1002\/psc.892; 10.1021\/jf072911z; 10.1111\/j.1750-3841.2009.01138.x; 10.1007\/s00894-010-0862-x; 10.1021\/jf202902r; 10.1039\/c2fo10192k; 10.1007\/s12010-012-0024-y; 10.1016\/j.talanta.2012.12.041; 10.1016\/j.foodchem.2013.05.140; 10.1021\/jf400865m; 10.1080\/10408398.2012.664829", "pubmedid": "7765503 12358510 12948830 15135150 16448176 17654623 18211015 19490329 20941517 21923188 22249830 23271625 23598136 23871047 23919612 24915368", "mw": "303.36", "pi": "5.49", "charge_ph7": "-0.27", "gravy": "1.65", "instability": "5.0", "hydrophobic": "1.0", "boman": "-3.185", "helix": "0.0", "turn_pct": "0.0", "sheet": "1.0" }, { "id": "aceip1081", "seq": "VWIG", "length": "4", "detail": "ND", "source": "ND", "ic50": "110 μM", "reference": "Angiotensin converting enzyme inhibitory peptides derived from food proteins: biochemistry, bioactivity and production.", "doi": "10.2174\/138161207780363068", "pubmedid": "17430180", "mw": "473.57", "pi": "5.49", "charge_ph7": "-0.27", "gravy": "1.85", "instability": "7.5", "hydrophobic": "0.75", "boman": "-3.0575", "helix": "0.0", "turn_pct": "0.25", "sheet": "0.75" }, { "id": "aceip1082", "seq": "VWIS", "length": "4", "detail": "Cereals (Maize)", "source": "Cereal", "ic50": "0.030 mM", "reference": "New antihypertensive peptides isolated from rapeseed.; Antihypertensive peptides from food proteins: a review.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.; Glycinyl-histidinyl-serine (GHS), a novel rapeseed protein-derived peptide has blood pressure-lowering effect in spontaneously hypertensive rats.", "doi": "10.1016\/s0196-9781(03)00174-8; 10.1039\/c2fo10192k; 10.1016\/j.foodchem.2013.05.140; 10.1021\/jf400865m", "pubmedid": "12948830 22249830 23871047 23919612", "mw": "503.59", "pi": "5.49", "charge_ph7": "-0.27", "gravy": "1.75", "instability": "7.5", "hydrophobic": "0.75", "boman": "-2.6125", "helix": "0.0", "turn_pct": "0.25", "sheet": "0.75" }, { "id": "aceip1083", "seq": "VWY", "length": "3", "detail": "Milk (bovine)", "source": "Milk", "ic50": "<20 mM", "reference": "Structure and activity of angiotensin I converting enzyme inhibitory peptides from sake and sake lees.; Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Vegetable foods: a cheap source of proteins and peptides with antihypertensive, antioxidant, and other less occurrence bioactivities.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1271\/bbb.58.1767; 10.1021\/jf051263l; 10.1016\/j.talanta.2012.12.041; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "7765503 16448176 23598136 23871047", "mw": "466.53", "pi": "5.49", "charge_ph7": "-0.27", "gravy": "0.6667", "instability": "6.67", "hydrophobic": "0.6667", "boman": "-2.0767", "helix": "0.0", "turn_pct": "0.0", "sheet": "1.0" }, { "id": "aceip1084", "seq": "VY", "length": "2", "detail": "Milk (bovine) | Cereals (Wheat) | Pork", "source": "Milk | Cereal | Porcine", "ic50": "<20 mM", "reference": "Structure and activity of angiotensin I converting enzyme inhibitory peptides from sake and sake lees.; Antihypertensive effect of valyl-tyrosine, a short chain peptide derived from sardine muscle hydrolyzate, on mild hypertensive subjects.; Angiotensin I-converting enzyme inhibitory peptides derived from wakame (Undaria pinnatifida) and their antihypertensive effect in spontaneously hypertensive rats.; Antihypertensive effects of Undaria pinnatifida (wakame) peptide on blood pressure in spontaneously hypertensive rats.; Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Quantitative structure-activity relationship study of bitter di- and tri-peptides including relationship with angiotensin I-converting enzyme inhibitory activity.; Three-dimensional holograph vector of atomic interaction field (3D-HoVAIF): a novel rotation-translation invariant 3D structure descriptor and its applications to peptides.; Bioactive peptides in amaranth (Amaranthus hypochondriacus) seed.; Assessing the dependence of (51)V A(z) value on the aromatic ring orientation of V(IV)O(2+) pyridine complexes.; Angiotensin I converting enzyme inhibitory peptides produced by autolysis reactions from wheat bran.; QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.; Antihypertensive peptides from food proteins: a review.; Review on the angiotensin-I-converting enzyme (ACE) inhibitor peptides from marine proteins.; Vegetable foods: a cheap source of proteins and peptides with antihypertensive, antioxidant, and other less occurrence bioactivities.; Peptides with angiotensin I converting enzyme (ACE) inhibitory activity generated from porcine skeletal muscle proteins by the action of meat-borne Lactobacillus.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.; Novel probiotic-fermented milk with angiotensin I-converting enzyme inhibitory peptides produced by Bifidobacterium bifidum MF 20\/5.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1271\/bbb.58.1767; 10.1038\/sj.jhh.1001065; 10.1021\/jf020482t; 10.1016\/j.jnutbio.2003.11.004; 10.1021\/jf051263l; 10.1002\/psc.800; 10.1002\/psc.892; 10.1021\/jf072911z; 10.1021\/ic9001779; 10.1021\/jf900857w; 10.1007\/s00894-010-0862-x; 10.1039\/c2fo10192k; 10.1007\/s12010-012-0024-y; 10.1016\/j.talanta.2012.12.041; 10.1016\/j.jprot.2013.06.023; 10.1016\/j.foodchem.2013.05.140; 10.1016\/j.ijfoodmicro.2013.09.002; 10.1080\/10408398.2012.664829", "pubmedid": "7765503 10962520 12358510 15135150 16448176 17117396 17654623 18211015 19449891 19572648 20941517 22249830 23271625 23598136 23806758 23871047 24135669 24915368", "mw": "280.32", "pi": "5.49", "charge_ph7": "-0.27", "gravy": "1.45", "instability": "-32.7", "hydrophobic": "0.5", "boman": "-1.95", "helix": "0.0", "turn_pct": "0.0", "sheet": "1.0" }, { "id": "aceip1085", "seq": "VYAP", "length": "4", "detail": "ND", "source": "ND", "ic50": "1.19 mg\/ml", "reference": "Review on the angiotensin-I-converting enzyme (ACE) inhibitor peptides from marine proteins.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1007\/s12010-012-0024-y; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "23271625 23871047", "mw": "448.51", "pi": "5.49", "charge_ph7": "-0.27", "gravy": "0.775", "instability": "96.0", "hydrophobic": "0.75", "boman": "-1.4275", "helix": "0.25", "turn_pct": "0.25", "sheet": "0.5" }, { "id": "aceip1086", "seq": "VYIHPF", "length": "6", "detail": "Milk (human)", "source": "Milk", "ic50": null, "reference": "Angiotensin II and its heptapeptide (2-8), hexapeptide (3-8), and pentapeptide (4-8) metabolites in arterial and venous blood of man.", "doi": "10.1161\/01.res.39.5.671", "pubmedid": "975455", "mw": "774.91", "pi": "6.71", "charge_ph7": "-0.18", "gravy": "0.9", "instability": "43.63", "hydrophobic": "0.6667", "boman": "-1.8017", "helix": "0.0", "turn_pct": "0.1667", "sheet": "0.6667" }, { "id": "aceip1087", "seq": "VYNEGLPAP", "length": "9", "detail": "Milk (human)", "source": "Milk", "ic50": "3.1 μM", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "23194537", "mw": "959.05", "pi": "4.05", "charge_ph7": "-1.26", "gravy": "-0.2333", "instability": "64.71", "hydrophobic": "0.5556", "boman": "-0.9233", "helix": "0.3333", "turn_pct": "0.4444", "sheet": "0.3333" }, { "id": "aceip1088", "seq": "VYP", "length": "3", "detail": "Milk (human)", "source": "Milk", "ic50": "<20 mM", "reference": "Inhibition of angiotensin-converting enzyme by synthetic peptide fragments of various beta-caseins.; Structural analysis of new antihypertensive peptides derived from cheese whey protein by proteinase K digestion.; Quantitative structure-activity relationship study of bitter di- and tri-peptides including relationship with angiotensin I-converting enzyme inhibitory activity.; Bioactive peptides in amaranth (Amaranthus hypochondriacus) seed.; Evaluation of the allergenicity of goat milk, cow milk, and their lactosera in a guinea pig model.; QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.; Antihypertensive peptides: production, bioavailability and incorporation into foods.; Antihypertensive peptides from food proteins: a review.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.3168\/jds.S0022-0302(98)75878-3; 10.1002\/psc.800; 10.1021\/jf072911z; 10.3168\/jds.2008-1125; 10.1007\/s00894-010-0862-x; 10.1016\/j.cis.2010.11.001; 10.1039\/c2fo10192k; 10.1016\/j.foodchem.2013.05.140; 10.1080\/10408398.2012.664829", "pubmedid": "1368548 9891260 17117396 18211015 19233776 20941517 21185549 22249830 23871047 24915368", "mw": "377.43", "pi": "5.49", "charge_ph7": "-0.27", "gravy": "0.4333", "instability": "22.67", "hydrophobic": "0.6667", "boman": "-1.3", "helix": "0.0", "turn_pct": "0.3333", "sheet": "0.6667" }, { "id": "aceip1089", "seq": "VYPFPG", "length": "6", "detail": "Milk (human)", "source": "Milk", "ic50": "221 μM", "reference": "Structural analysis of new antihypertensive peptides derived from cheese whey protein by proteinase K digestion.; Evaluation of the allergenicity of goat milk, cow milk, and their lactosera in a guinea pig model.; Antihypertensive peptides: production, bioavailability and incorporation into foods.; Antihypertensive peptides from food proteins: a review.; Characterisation of a new antihypertensive angiotensin I-converting enzyme inhibitory peptide from Pleurotus cornucopiae.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.3168\/jds.S0022-0302(98)75878-3; 10.3168\/jds.2008-1125; 10.1016\/j.cis.2010.11.001; 10.1039\/c2fo10192k; 10.1016\/j.foodchem.2011.01.010; 10.1016\/j.foodchem.2012.09.092; 10.1080\/10408398.2012.664829", "pubmedid": "9891260 19233776 21185549 22249830 23140680 23194537 24915368", "mw": "678.77", "pi": "5.49", "charge_ph7": "-0.27", "gravy": "0.35", "instability": "80.53", "hydrophobic": "0.6667", "boman": "-1.3033", "helix": "0.0", "turn_pct": "0.5", "sheet": "0.5" }, { "id": "aceip1090", "seq": "VYPHK", "length": "5", "detail": "Milk (bovine) | Casein | Amaranth | Cereals", "source": "Milk | Plants | Cereal", "ic50": "4.59 μM", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "23194537", "mw": "642.75", "pi": "8.57", "charge_ph7": "0.82", "gravy": "-1.16", "instability": "64.96", "hydrophobic": "0.4", "boman": "-0.266", "helix": "0.2", "turn_pct": "0.2", "sheet": "0.4" }, { "id": "aceip1091", "seq": "WA", "length": "2", "detail": "Milk (bovine)", "source": "Milk", "ic50": "<20 mM", "reference": "Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Review on the angiotensin-I-converting enzyme (ACE) inhibitor peptides from marine proteins.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1021\/jf051263l; 10.1007\/s12010-012-0024-y; 10.1016\/j.foodchem.2013.05.140; 10.1080\/10408398.2012.664829", "pubmedid": "16448176 23271625 23871047 24915368", "mw": "275.3", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "0.45", "instability": "-70.15", "hydrophobic": "1.0", "boman": "-2.07", "helix": "0.5", "turn_pct": "0.0", "sheet": "0.5" }, { "id": "aceip1092", "seq": "WE", "length": "2", "detail": "Milk (human)", "source": "Milk", "ic50": null, "reference": "Three-dimensional holograph vector of atomic interaction field (3D-HoVAIF): a novel rotation-translation invariant 3D structure descriptor and its applications to peptides.", "doi": "10.1002\/psc.892", "pubmedid": "17654623", "mw": "333.34", "pi": "4.6", "charge_ph7": "-1.23", "gravy": "-2.2", "instability": "5.0", "hydrophobic": "0.5", "boman": "-0.345", "helix": "0.5", "turn_pct": "0.0", "sheet": "0.5" }, { "id": "aceip1093", "seq": "WG", "length": "2", "detail": "Milk (bovine) | Amaranth | Cereals | Sake | Chicken connectin", "source": "Milk | Plants | Cereal | Chicken", "ic50": "<20 mM", "reference": "Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Three-dimensional holograph vector of atomic interaction field (3D-HoVAIF): a novel rotation-translation invariant 3D structure descriptor and its applications to peptides.; QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.; Peptides with angiotensin I converting enzyme (ACE) inhibitory activity generated from porcine skeletal muscle proteins by the action of meat-borne Lactobacillus.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1021\/jf051263l; 10.1002\/psc.892; 10.1007\/s00894-010-0862-x; 10.1016\/j.jprot.2013.06.023; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "16448176 17654623 20941517 23806758 23871047", "mw": "261.28", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "-0.65", "instability": "-46.85", "hydrophobic": "0.5", "boman": "-1.635", "helix": "0.0", "turn_pct": "0.5", "sheet": "0.5" }, { "id": "aceip1094", "seq": "WH", "length": "2", "detail": "ND", "source": "ND", "ic50": "5.1 μM", "reference": "Antihypertensive effects of Undaria pinnatifida (wakame) peptide on blood pressure in spontaneously hypertensive rats.", "doi": "10.1016\/j.jnutbio.2003.11.004", "pubmedid": "15135150", "mw": "341.36", "pi": "6.74", "charge_ph7": "-0.15", "gravy": "-2.05", "instability": "123.4", "hydrophobic": "0.5", "boman": "-0.67", "helix": "0.0", "turn_pct": "0.0", "sheet": "0.5" }, { "id": "aceip1095", "seq": "WHHTF", "length": "5", "detail": "Milk (Sheep raw milk cheese (synthesised))", "source": "Milk", "ic50": "24.1 μM", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "23194537", "mw": "726.78", "pi": "6.92", "charge_ph7": "-0.07", "gravy": "-1.04", "instability": "64.96", "hydrophobic": "0.4", "boman": "-0.614", "helix": "0.0", "turn_pct": "0.0", "sheet": "0.6" }, { "id": "aceip1096", "seq": "WL", "length": "2", "detail": "Soybean", "source": "Legume", "ic50": "<20 mM", "reference": "Angiotensin I-converting enzyme inhibitory peptides isolated from tofuyo fermented soybean food.; Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Vegetable foods: a cheap source of proteins and peptides with antihypertensive, antioxidant, and other less occurrence bioactivities.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.; Glycinyl-histidinyl-serine (GHS), a novel rapeseed protein-derived peptide has blood pressure-lowering effect in spontaneously hypertensive rats.", "doi": "10.1271\/bbb.67.1278; 10.1021\/jf051263l; 10.1016\/j.talanta.2012.12.041; 10.1016\/j.foodchem.2013.05.140; 10.1021\/jf400865m", "pubmedid": "12843654 16448176 23598136 23871047 23919612", "mw": "317.38", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "1.45", "instability": "66.7", "hydrophobic": "1.0", "boman": "-3.625", "helix": "0.5", "turn_pct": "0.0", "sheet": "1.0" }, { "id": "aceip1097", "seq": "WLAHK", "length": "5", "detail": "Amaranth | Sake", "source": "Plants | Cereal", "ic50": "77 μM", "reference": "Angiotensin I-converting enzyme inhibitory properties of whey protein digests: concentration and characterization of active peptides.; Angiotensin converting enzyme inhibitory peptides derived from food proteins: biochemistry, bioactivity and production.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1017\/s0022029999003982; 10.2174\/138161207780363068; 10.1016\/j.foodchem.2012.09.092", "pubmedid": "10717843 17430180 23194537", "mw": "653.77", "pi": "8.76", "charge_ph7": "0.85", "gravy": "-0.48", "instability": "63.06", "hydrophobic": "0.6", "boman": "-1.298", "helix": "0.6", "turn_pct": "0.0", "sheet": "0.4" }, { "id": "aceip1098", "seq": "WLP", "length": "3", "detail": "Milk (human)", "source": "Milk", "ic50": "400 μM", "reference": "Inhibition strength of short peptides derived from an ACE inhibitory peptide.", "doi": "10.1021\/jf202902r", "pubmedid": "21923188", "mw": "414.5", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "0.4333", "instability": "112.0", "hydrophobic": "1.0", "boman": "-2.4167", "helix": "0.3333", "turn_pct": "0.3333", "sheet": "0.6667" }, { "id": "aceip1099", "seq": "WM", "length": "2", "detail": "Milk (human)", "source": "Milk", "ic50": "<20 mM", "reference": "Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Antihypertensive peptides from food proteins: a review.; Review on the angiotensin-I-converting enzyme (ACE) inhibitor peptides from marine proteins.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1021\/jf051263l; 10.1039\/c2fo10192k; 10.1007\/s12010-012-0024-y; 10.1016\/j.foodchem.2013.05.140; 10.1080\/10408398.2012.664829", "pubmedid": "16448176 22249830 23271625 23871047 24915368", "mw": "335.42", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "0.5", "instability": "123.4", "hydrophobic": "1.0", "boman": "-2.34", "helix": "0.5", "turn_pct": "0.0", "sheet": "0.5" }, { "id": "aceip1100", "seq": "WNINA", "length": "5", "detail": "ND", "source": "ND", "ic50": null, "reference": "Release of angiotensin I-converting enzyme inhibitory peptides from flaxseed (Linum usitatissimum L.) protein under simulated gastrointestinal digestion.", "doi": "10.1021\/jf202000e", "pubmedid": "21776963", "mw": "616.67", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "-0.32", "instability": "120.56", "hydrophobic": "0.6", "boman": "-1.164", "helix": "0.2", "turn_pct": "0.4", "sheet": "0.4" }, { "id": "aceip1101", "seq": "WNLNA", "length": "5", "detail": "Casein", "source": "Milk", "ic50": null, "reference": "Release of angiotensin I-converting enzyme inhibitory peptides from flaxseed (Linum usitatissimum L.) protein under simulated gastrointestinal digestion.", "doi": "10.1021\/jf202000e", "pubmedid": "21776963", "mw": "616.67", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "-0.46", "instability": "32.68", "hydrophobic": "0.6", "boman": "-1.164", "helix": "0.4", "turn_pct": "0.4", "sheet": "0.4" }, { "id": "aceip1102", "seq": "WPEAAELMMEVDP", "length": "13", "detail": "Fungi (Agaricus bisporus)", "source": "Fungi", "ic50": "21.6 μM", "reference": "Antihypertensive effect of angiotensin i converting enzyme-inhibitory peptide from hydrolysates of Bigeye tuna dark muscle, Thunnus obesus.; Antihypertensive peptides from food proteins: a review.; Review on the angiotensin-I-converting enzyme (ACE) inhibitor peptides from marine proteins.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1021\/jf0710635; 10.1039\/c2fo10192k; 10.1007\/s12010-012-0024-y; 10.1080\/10408398.2012.664829", "pubmedid": "17894458 22249830 23271625 24915368", "mw": "1517.72", "pi": "4.05", "charge_ph7": "-4.23", "gravy": "-0.2077", "instability": "8.82", "hydrophobic": "0.6923", "boman": "-1.0008", "helix": "0.6154", "turn_pct": "0.2308", "sheet": "0.2308" }, { "id": "aceip1103", "seq": "WPERPPQIP", "length": "9", "detail": "Milk (bovine) | Cereals (Buckwheat) | Soybean", "source": "Milk | Cereal | Legume", "ic50": "25.67 mg\/ml", "reference": "Purification and identification of an ACE inhibitory peptide from walnut protein.", "doi": "10.1021\/jf4001378", "pubmedid": "23566262", "mw": "1119.27", "pi": "6.0", "charge_ph7": "-0.24", "gravy": "-1.5889", "instability": "89.2", "hydrophobic": "0.6667", "boman": "-0.17", "helix": "0.1111", "turn_pct": "0.4444", "sheet": "0.2222" }, { "id": "aceip1104", "seq": "WPPRPQIPP", "length": "9", "detail": "Milk (bovine) | Cereals | Pork | Chicken", "source": "Milk | Cereal | Porcine | Chicken", "ic50": null, "reference": "Identification of novel bradykinin-potentiating peptides and C-type natriuretic peptide from Lachesis muta venom.", "doi": "10.1016\/j.toxicon.2005.03.006", "pubmedid": "15876444", "mw": "1087.27", "pi": "9.75", "charge_ph7": "0.76", "gravy": "-1.3778", "instability": "82.91", "hydrophobic": "0.7778", "boman": "-0.3522", "helix": "0.0", "turn_pct": "0.5556", "sheet": "0.2222" }, { "id": "aceip1105", "seq": "WQVLPNAVPAK", "length": "11", "detail": "Tuna", "source": "Fish", "ic50": "10.1 μM", "reference": "Changes in arterial blood pressure after single oral administration of milk-casein-derived peptides in spontaneously hypertensive rats.; Antihypertensive peptides: production, bioavailability and incorporation into foods.; Antihypertensive peptides from food proteins: a review.", "doi": "10.1002\/mnfr.200900448; 10.1016\/j.cis.2010.11.001; 10.1039\/c2fo10192k", "pubmedid": "20397194 21185549 22249830", "mw": "1222.44", "pi": "8.75", "charge_ph7": "0.76", "gravy": "0.0727", "instability": "54.76", "hydrophobic": "0.7273", "boman": "-1.3082", "helix": "0.3636", "turn_pct": "0.2727", "sheet": "0.3636" }, { "id": "aceip1106", "seq": "WSKVVL", "length": "6", "detail": "Tuna", "source": "Fish", "ic50": "154.88 μM", "reference": "Effects of angiotensin I-converting enzyme inhibitory substances derived from Indonesian dried-salted fish on blood pressure of rats.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1271\/bbb.59.425; 10.1016\/j.foodchem.2012.09.092", "pubmedid": "7766180 23194537", "mw": "730.89", "pi": "8.75", "charge_ph7": "0.76", "gravy": "1.1", "instability": "-5.82", "hydrophobic": "0.6667", "boman": "-2.1517", "helix": "0.3333", "turn_pct": "0.1667", "sheet": "0.6667" }, { "id": "aceip1107", "seq": "WSVPQPK", "length": "7", "detail": "Tuna", "source": "Fish", "ic50": "21 μM", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "23194537", "mw": "840.97", "pi": "8.75", "charge_ph7": "0.76", "gravy": "-1.1571", "instability": "91.11", "hydrophobic": "0.5714", "boman": "-0.37", "helix": "0.1429", "turn_pct": "0.4286", "sheet": "0.2857" }, { "id": "aceip1108", "seq": "WVPSVY", "length": "6", "detail": "Tuna", "source": "Fish", "ic50": "25.7 μM", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.; Vegetable foods: a cheap source of proteins and peptides with antihypertensive, antioxidant, and other less occurrence bioactivities.", "doi": "10.1016\/j.foodchem.2012.09.092; 10.1016\/j.talanta.2012.12.041", "pubmedid": "23194537 23598136", "mw": "749.85", "pi": "5.52", "charge_ph7": "-0.24", "gravy": "0.6333", "instability": "45.82", "hydrophobic": "0.6667", "boman": "-1.5717", "helix": "0.0", "turn_pct": "0.3333", "sheet": "0.6667" }, { "id": "aceip1109", "seq": "WW", "length": "2", "detail": "Tuna", "source": "Fish", "ic50": null, "reference": "Three-dimensional holograph vector of atomic interaction field (3D-HoVAIF): a novel rotation-translation invariant 3D structure descriptor and its applications to peptides.", "doi": "10.1002\/psc.892", "pubmedid": "17654623", "mw": "390.44", "pi": "5.53", "charge_ph7": "-0.24", "gravy": "-0.9", "instability": "5.0", "hydrophobic": "1.0", "boman": "-2.33", "helix": "0.0", "turn_pct": "0.0", "sheet": "1.0" }, { "id": "aceip1110", "seq": "WY", "length": "2", "detail": "Tuna", "source": "Fish", "ic50": "38.3 μM", "reference": "ACE-inhibitory and radical-scavenging activity of peptides derived from beta-lactoglobulin f(19-25). Interactions with ascorbic acid.", "doi": "10.1021\/jf063427j", "pubmedid": "17411066", "mw": "367.4", "pi": "5.52", "charge_ph7": "-0.24", "gravy": "-1.1", "instability": "5.0", "hydrophobic": "0.5", "boman": "-1.095", "helix": "0.0", "turn_pct": "0.0", "sheet": "1.0" }, { "id": "aceip1111", "seq": "WYSL", "length": "4", "detail": "Tuna", "source": "Fish", "ic50": null, "reference": "What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1016\/j.foodchem.2013.05.140", "pubmedid": "23871047", "mw": "567.63", "pi": "5.52", "charge_ph7": "-0.24", "gravy": "0.2", "instability": "7.5", "hydrophobic": "0.5", "boman": "-1.5675", "helix": "0.25", "turn_pct": "0.25", "sheet": "0.75" }, { "id": "aceip1112", "seq": "WYSLA", "length": "5", "detail": "Tuna", "source": "Fish", "ic50": "86.9 μM", "reference": "ACE-inhibitory and radical-scavenging activity of peptides derived from beta-lactoglobulin f(19-25). Interactions with ascorbic acid.", "doi": "10.1021\/jf063427j", "pubmedid": "17411066", "mw": "638.71", "pi": "5.52", "charge_ph7": "-0.24", "gravy": "0.52", "instability": "8.0", "hydrophobic": "0.6", "boman": "-1.616", "helix": "0.4", "turn_pct": "0.2", "sheet": "0.6" }, { "id": "aceip1113", "seq": "WYSLAM", "length": "6", "detail": "Tuna", "source": "Fish", "ic50": "56.3 μM", "reference": "ACE-inhibitory and radical-scavenging activity of peptides derived from beta-lactoglobulin f(19-25). Interactions with ascorbic acid.", "doi": "10.1021\/jf063427j", "pubmedid": "17411066", "mw": "769.91", "pi": "5.52", "charge_ph7": "-0.24", "gravy": "0.75", "instability": "8.33", "hydrophobic": "0.6667", "boman": "-1.7383", "helix": "0.5", "turn_pct": "0.1667", "sheet": "0.5" }, { "id": "aceip1114", "seq": "WYSLAMA", "length": "7", "detail": "Bonito | Tuna", "source": "Fish", "ic50": "59.9 μM", "reference": "ACE-inhibitory and radical-scavenging activity of peptides derived from beta-lactoglobulin f(19-25). Interactions with ascorbic acid.", "doi": "10.1021\/jf063427j", "pubmedid": "17411066", "mw": "840.99", "pi": "5.52", "charge_ph7": "-0.24", "gravy": "0.9", "instability": "26.2", "hydrophobic": "0.7143", "boman": "-1.7486", "helix": "0.5714", "turn_pct": "0.1429", "sheet": "0.4286" }, { "id": "aceip1115", "seq": "YA", "length": "2", "detail": "ND", "source": "ND", "ic50": "460 μM", "reference": "Three-dimensional holograph vector of atomic interaction field (3D-HoVAIF): a novel rotation-translation invariant 3D structure descriptor and its applications to peptides.; QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1002\/psc.892; 10.1007\/s00894-010-0862-x; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "17654623 20941517 23871047", "mw": "252.27", "pi": "5.52", "charge_ph7": "-0.24", "gravy": "0.25", "instability": "123.4", "hydrophobic": "0.5", "boman": "-0.835", "helix": "0.5", "turn_pct": "0.0", "sheet": "0.5" }, { "id": "aceip1116", "seq": "YAEERYPIL", "length": "9", "detail": "Tuna", "source": "Fish", "ic50": "4.7 μM", "reference": "Antioxidant activity of peptides derived from egg white proteins by enzymatic hydrolysis.; Antihypertensive peptides: production, bioavailability and incorporation into foods.; Antihypertensive peptides from food proteins: a review.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.4315\/0362-028x-67.9.1939; 10.1016\/j.cis.2010.11.001; 10.1039\/c2fo10192k; 10.1016\/j.foodchem.2012.09.092", "pubmedid": "15453585 21185549 22249830 23194537", "mw": "1153.28", "pi": "4.53", "charge_ph7": "-1.24", "gravy": "-0.6222", "instability": "98.16", "hydrophobic": "0.4444", "boman": "-0.5967", "helix": "0.4444", "turn_pct": "0.1111", "sheet": "0.4444" }, { "id": "aceip1117", "seq": "YAKPVA", "length": "6", "detail": "Tuna", "source": "Fish", "ic50": "14.3 μM", "reference": "Changes in arterial blood pressure after single oral administration of milk-casein-derived peptides in spontaneously hypertensive rats.; Antihypertensive peptides: production, bioavailability and incorporation into foods.; Antihypertensive peptides from food proteins: a review.", "doi": "10.1002\/mnfr.200900448; 10.1016\/j.cis.2010.11.001; 10.1039\/c2fo10192k", "pubmedid": "20397194 21185549 22249830", "mw": "647.76", "pi": "8.59", "charge_ph7": "0.76", "gravy": "0.1667", "instability": "67.33", "hydrophobic": "0.6667", "boman": "-0.99", "helix": "0.5", "turn_pct": "0.1667", "sheet": "0.3333" }, { "id": "aceip1118", "seq": "YALPHA", "length": "6", "detail": "Tuna", "source": "Fish", "ic50": "9.8 μM", "reference": "Angiotensin I-converting enzyme inhibitors in autolysates of squid liver and mantle muscle.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1271\/bbb.60.1353; 10.1016\/j.foodchem.2012.09.092", "pubmedid": "8987556 23194537", "mw": "670.76", "pi": "6.74", "charge_ph7": "-0.15", "gravy": "0.2167", "instability": "79.9", "hydrophobic": "0.6667", "boman": "-1.235", "helix": "0.5", "turn_pct": "0.1667", "sheet": "0.3333" }, { "id": "aceip1119", "seq": "YANPAVVRP", "length": "9", "detail": "Milk (human)", "source": "Milk", "ic50": "7.8 μM", "reference": "Inhibition of angiotensin-converting enzyme by synthetic peptide fragments of human kappa-casein.; QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.", "doi": "10.1007\/s00894-010-0862-x", "pubmedid": "1368540 20941517", "mw": "986.12", "pi": "8.75", "charge_ph7": "0.76", "gravy": "-0.0556", "instability": "74.8", "hydrophobic": "0.6667", "boman": "-0.8022", "helix": "0.2222", "turn_pct": "0.3333", "sheet": "0.3333" }, { "id": "aceip1120", "seq": "YE", "length": "2", "detail": "Pork", "source": "Porcine", "ic50": "<20 mM", "reference": "Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.", "doi": "10.1021\/jf051263l", "pubmedid": "16448176", "mw": "310.3", "pi": "4.6", "charge_ph7": "-1.23", "gravy": "-2.4", "instability": "-32.7", "hydrophobic": "0.0", "boman": "0.89", "helix": "0.5", "turn_pct": "0.0", "sheet": "0.5" }, { "id": "aceip1121", "seq": "YEAP", "length": "4", "detail": "Milk (Sheep raw milk cheese (synthesised))", "source": "Milk", "ic50": null, "reference": "Vegetable foods: a cheap source of proteins and peptides with antihypertensive, antioxidant, and other less occurrence bioactivities.", "doi": "10.1016\/j.talanta.2012.12.041", "pubmedid": "23598136", "mw": "478.5", "pi": "4.05", "charge_ph7": "-1.24", "gravy": "-1.15", "instability": "36.8", "hydrophobic": "0.5", "boman": "-0.0075", "helix": "0.5", "turn_pct": "0.25", "sheet": "0.25" }, { "id": "aceip1122", "seq": "YEY", "length": "3", "detail": "Milk", "source": "Milk", "ic50": "<20 mM", "reference": "Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.", "doi": "10.1021\/jf051263l", "pubmedid": "16448176", "mw": "473.48", "pi": "4.05", "charge_ph7": "-1.24", "gravy": "-2.0333", "instability": "-18.47", "hydrophobic": "0.0", "boman": "0.64", "helix": "0.3333", "turn_pct": "0.0", "sheet": "0.6667" }, { "id": "aceip1123", "seq": "YF", "length": "2", "detail": "Milk (human)", "source": "Milk", "ic50": null, "reference": "Quantitative structure-activity relationship study of bitter di- and tri-peptides including relationship with angiotensin I-converting enzyme inhibitory activity.", "doi": "10.1002\/psc.800", "pubmedid": "17117396", "mw": "328.36", "pi": "5.52", "charge_ph7": "-0.24", "gravy": "0.75", "instability": "5.0", "hydrophobic": "0.5", "boman": "-1.42", "helix": "0.0", "turn_pct": "0.0", "sheet": "1.0" }, { "id": "aceip1124", "seq": "YG", "length": "2", "detail": "Milk (human)", "source": "Milk", "ic50": "<20 mM", "reference": "Synthetic peptides corresponding to alpha-lactalbumin and beta-lactoglobulin sequences with angiotensin-I-converting enzyme inhibitory activity.; Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Quantitative structure-activity relationship study of bitter di- and tri-peptides including relationship with angiotensin I-converting enzyme inhibitory activity.; Three-dimensional holograph vector of atomic interaction field (3D-HoVAIF): a novel rotation-translation invariant 3D structure descriptor and its applications to peptides.; Bioactive peptides in amaranth (Amaranthus hypochondriacus) seed.; Use of beta-cyclodextrin to decrease the level of cholesterol in milk fat.; Peptides with angiotensin I converting enzyme (ACE) inhibitory activity generated from porcine skeletal muscle proteins by the action of meat-borne Lactobacillus.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1515\/bchm3.1996.377.4.259; 10.1021\/jf051263l; 10.1002\/psc.800; 10.1002\/psc.892; 10.1021\/jf072911z; 10.3168\/jds.2008-1452; 10.1016\/j.jprot.2013.06.023; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "8737991 16448176 17117396 17654623 18211015 19233779 23806758 23871047", "mw": "238.24", "pi": "5.52", "charge_ph7": "-0.24", "gravy": "-0.85", "instability": "-37.45", "hydrophobic": "0.0", "boman": "-0.4", "helix": "0.0", "turn_pct": "0.5", "sheet": "0.5" }, { "id": "aceip1125", "seq": "YGAP", "length": "4", "detail": "Milk (human)", "source": "Milk", "ic50": "17.4 μM", "reference": "Rational design of angiotensin-I-converting enzyme inhibitory peptides by integrating in silico modeling and an in vitro assay.", "doi": "10.1002\/cmdc.201300132", "pubmedid": "23740817", "mw": "406.43", "pi": "5.52", "charge_ph7": "-0.24", "gravy": "-0.375", "instability": "13.2", "hydrophobic": "0.5", "boman": "-0.6525", "helix": "0.25", "turn_pct": "0.5", "sheet": "0.25" }, { "id": "aceip1126", "seq": "YGFLP", "length": "5", "detail": "Casein", "source": "Milk", "ic50": "232.33 μM", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "23194537", "mw": "595.69", "pi": "5.52", "charge_ph7": "-0.24", "gravy": "0.66", "instability": "29.54", "hydrophobic": "0.6", "boman": "-1.74", "helix": "0.2", "turn_pct": "0.4", "sheet": "0.6" }, { "id": "aceip1127", "seq": "YGFLPILP", "length": "8", "detail": "Casein", "source": "Milk", "ic50": "260 μM", "reference": "Inhibition of angiotensin-converting enzyme by synthetic peptide fragments of various beta-caseins.", "doi": "", "pubmedid": "1368548", "mw": "919.12", "pi": "5.52", "charge_ph7": "-0.24", "gravy": "1.25", "instability": "70.36", "hydrophobic": "0.75", "boman": "-2.3175", "helix": "0.25", "turn_pct": "0.375", "sheet": "0.625" }, { "id": "aceip1128", "seq": "YGG", "length": "3", "detail": "ND", "source": "ND", "ic50": "<20 mM", "reference": "Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Quantitative structure-activity relationship study of bitter di- and tri-peptides including relationship with angiotensin I-converting enzyme inhibitory activity.; QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1021\/jf051263l; 10.1002\/psc.800; 10.1007\/s00894-010-0862-x; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "16448176 17117396 20941517 23871047", "mw": "295.29", "pi": "5.52", "charge_ph7": "-0.24", "gravy": "-0.7", "instability": "19.5", "hydrophobic": "0.0", "boman": "-0.58", "helix": "0.0", "turn_pct": "0.6667", "sheet": "0.3333" }, { "id": "aceip1129", "seq": "YGGY", "length": "4", "detail": "Synthesized", "source": "Synthesized", "ic50": "3.4 μM", "reference": "Structure and activity of angiotensin I converting enzyme inhibitory peptides from sake and sake lees.; Bioactive peptides in amaranth (Amaranthus hypochondriacus) seed.; Vegetable foods: a cheap source of proteins and peptides with antihypertensive, antioxidant, and other less occurrence bioactivities.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1271\/bbb.58.1767; 10.1021\/jf072911z; 10.1016\/j.talanta.2012.12.041; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "7765503 18211015 23598136 23871047", "mw": "458.46", "pi": "5.52", "charge_ph7": "-0.24", "gravy": "-0.85", "instability": "-4.1", "hydrophobic": "0.0", "boman": "-0.4", "helix": "0.0", "turn_pct": "0.5", "sheet": "0.5" }, { "id": "aceip1130", "seq": "YGL", "length": "3", "detail": "Synthesized", "source": "Synthesized", "ic50": "<20 mM", "reference": "Angiotensin I-converting enzyme inhibitory properties of whey protein digests: concentration and characterization of active peptides.; Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.", "doi": "10.1017\/s0022029999003982; 10.1021\/jf051263l", "pubmedid": "10717843 16448176", "mw": "351.4", "pi": "5.52", "charge_ph7": "-0.24", "gravy": "0.7", "instability": "-21.63", "hydrophobic": "0.3333", "boman": "-1.9067", "helix": "0.3333", "turn_pct": "0.3333", "sheet": "0.6667" }, { "id": "aceip1131", "seq": "YGLF", "length": "4", "detail": "Synthesized", "source": "Synthesized", "ic50": "733 μM", "reference": "Lactokinins: whey protein-derived ACE inhibitory peptides.; Milk peptides and blood pressure.; Use of beta-cyclodextrin to decrease the level of cholesterol in milk fat.; Antihypertensive peptides: production, bioavailability and incorporation into foods.; Bioactive peptides derived from milk proteins and their health beneficial potentials: an update.; Antihypertensive peptides from food proteins: a review.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1002\/(SICI)1521-3803(19990601)43:3<165::AID-FOOD165>3.0.CO;2-2; 10.1093\/jn\/137.3.825S; 10.3168\/jds.2008-1452; 10.1016\/j.cis.2010.11.001; 10.1039\/c0fo00016g; 10.1039\/c2fo10192k; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "10399349 17311982 19233779 21185549 21773582 22249830 23871047", "mw": "498.57", "pi": "5.52", "charge_ph7": "-0.24", "gravy": "1.225", "instability": "-13.73", "hydrophobic": "0.5", "boman": "-2.175", "helix": "0.25", "turn_pct": "0.25", "sheet": "0.75" }, { "id": "aceip1132", "seq": "YGLVAGTW", "length": "8", "detail": "Milk (bovine) | Cereals (Wheat)", "source": "Milk | Cereal", "ic50": "0 μM", "reference": "Angiotensin I-converting enzyme inhibitory properties of whey protein digests: concentration and characterization of active peptides.", "doi": "10.1017\/s0022029999003982", "pubmedid": "10717843", "mw": "865.97", "pi": "5.52", "charge_ph7": "-0.24", "gravy": "0.7625", "instability": "-31.26", "hydrophobic": "0.5", "boman": "-1.8225", "helix": "0.25", "turn_pct": "0.25", "sheet": "0.625" }, { "id": "aceip1133", "seq": "YGLYP", "length": "5", "detail": "Milk-Cheese (Goat milk protein and cheeses) | Milk-Cheese (Sheep milk and cheeses proteins) | Milk (Caprine Kefir) | Enzymatic-hydrolysis (Hydrolysis with pepsin)", "source": "Milk | Synthesized", "ic50": "159.27 μM", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "23194537", "mw": "611.69", "pi": "5.52", "charge_ph7": "-0.24", "gravy": "-0.16", "instability": "15.7", "hydrophobic": "0.4", "boman": "-1.116", "helix": "0.2", "turn_pct": "0.4", "sheet": "0.6" }, { "id": "aceip1134", "seq": "YGY", "length": "3", "detail": "ND", "source": "ND", "ic50": null, "reference": "Quantitative structure-activity relationship study of bitter di- and tri-peptides including relationship with angiotensin I-converting enzyme inhibitory activity.; QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1002\/psc.800; 10.1007\/s00894-010-0862-x; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "17117396 20941517 23871047", "mw": "401.41", "pi": "5.52", "charge_ph7": "-0.24", "gravy": "-1.0", "instability": "-49.93", "hydrophobic": "0.0", "boman": "-0.22", "helix": "0.0", "turn_pct": "0.3333", "sheet": "0.6667" }, { "id": "aceip1135", "seq": "YH", "length": "2", "detail": "Milk (human)", "source": "Milk", "ic50": "<20 mM", "reference": "Antihypertensive effects of Undaria pinnatifida (wakame) peptide on blood pressure in spontaneously hypertensive rats.; Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Antihypertensive peptides from food proteins: a review.; Vegetable foods: a cheap source of proteins and peptides with antihypertensive, antioxidant, and other less occurrence bioactivities.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1016\/j.jnutbio.2003.11.004; 10.1021\/jf051263l; 10.1039\/c2fo10192k; 10.1016\/j.talanta.2012.12.041; 10.1016\/j.foodchem.2013.05.140; 10.1080\/10408398.2012.664829", "pubmedid": "15135150 16448176 22249830 23598136 23871047 24915368", "mw": "318.33", "pi": "6.74", "charge_ph7": "-0.15", "gravy": "-2.25", "instability": "66.7", "hydrophobic": "0.0", "boman": "0.565", "helix": "0.0", "turn_pct": "0.0", "sheet": "0.5" }, { "id": "aceip1136", "seq": "YIHPF", "length": "5", "detail": "Pork", "source": "Porcine", "ic50": null, "reference": "Angiotensin II and its heptapeptide (2-8), hexapeptide (3-8), and pentapeptide (4-8) metabolites in arterial and venous blood of man.", "doi": "10.1161\/01.res.39.5.671", "pubmedid": "975455", "mw": "675.77", "pi": "6.74", "charge_ph7": "-0.15", "gravy": "0.24", "instability": "65.44", "hydrophobic": "0.6", "boman": "-1.354", "helix": "0.0", "turn_pct": "0.2", "sheet": "0.6" }, { "id": "aceip1137", "seq": "YIPIQY", "length": "6", "detail": "Milk", "source": "Milk", "ic50": "10 μM", "reference": "Identification of novel angiotensin-converting enzyme-inhibitory peptides from ovine milk proteins by CE-MS and chromatographic techniques.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1002\/elps.200700324; 10.1016\/j.foodchem.2012.09.092; 10.1080\/10408398.2012.664829", "pubmedid": "17948260 23194537 24915368", "mw": "795.92", "pi": "5.52", "charge_ph7": "-0.24", "gravy": "0.2167", "instability": "-9.03", "hydrophobic": "0.5", "boman": "-1.3667", "helix": "0.0", "turn_pct": "0.1667", "sheet": "0.6667" }, { "id": "aceip1138", "seq": "YIPIQYVLSR", "length": "10", "detail": "Carp | Cereals (Wheat) | Chicken", "source": "Fish | Cereal | Chicken", "ic50": "132.5 μM", "reference": "Rheological, sensorial, and chemopreventive properties of milk fermented with exopolysaccharide-producing lactic cultures.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.3168\/jds.2008-1256; 10.1016\/j.foodchem.2012.09.092", "pubmedid": "19233777 23194537", "mw": "1251.47", "pi": "8.59", "charge_ph7": "0.76", "gravy": "0.4", "instability": "17.84", "hydrophobic": "0.5", "boman": "-1.36", "helix": "0.1", "turn_pct": "0.2", "sheet": "0.6" }, { "id": "aceip1139", "seq": "YK", "length": "2", "detail": "Flaxseed", "source": "Plants", "ic50": "610 μM", "reference": "Peptides with angiotensin I converting enzyme (ACE) inhibitory activity generated from porcine skeletal muscle proteins by the action of meat-borne Lactobacillus.", "doi": "10.1016\/j.jprot.2013.06.023", "pubmedid": "23806758", "mw": "309.36", "pi": "8.59", "charge_ph7": "0.76", "gravy": "-2.6", "instability": "5.0", "hydrophobic": "0.0", "boman": "0.86", "helix": "0.5", "turn_pct": "0.0", "sheet": "0.5" }, { "id": "aceip1140", "seq": "YKVPQL", "length": "6", "detail": "Meat", "source": "Meat", "ic50": "22 μM", "reference": "Identification of an antihypertensive peptide from casein hydrolysate produced by a proteinase from Lactobacillus helveticus CP790.; Bioactive peptides derived from milk proteins and their health beneficial potentials: an update.; Antihypertensive peptides from food proteins: a review.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.3168\/jds.S0022-0302(96)76487-1; 10.1039\/c0fo00016g; 10.1039\/c2fo10192k; 10.1016\/j.foodchem.2012.09.092", "pubmedid": "8880454 21773582 22249830 23194537", "mw": "746.89", "pi": "8.59", "charge_ph7": "0.76", "gravy": "-0.3833", "instability": "58.38", "hydrophobic": "0.5", "boman": "-0.98", "helix": "0.3333", "turn_pct": "0.1667", "sheet": "0.5" }, { "id": "aceip1141", "seq": "YKW", "length": "3", "detail": "Egg (Ovalbumin)", "source": "Egg", "ic50": "13.3 μM", "reference": "Inhibition strength of short peptides derived from an ACE inhibitory peptide.", "doi": "10.1021\/jf202902r", "pubmedid": "21923188", "mw": "495.57", "pi": "8.59", "charge_ph7": "0.76", "gravy": "-2.0333", "instability": "6.67", "hydrophobic": "0.3333", "boman": "-0.2033", "helix": "0.3333", "turn_pct": "0.0", "sheet": "0.6667" }, { "id": "aceip1142", "seq": "YKWL", "length": "4", "detail": "Milk (bovine) | Cereals | pea | Pork | Chicken", "source": "Milk | Cereal | Legume | Porcine | Chicken", "ic50": "38.7 μM", "reference": "Inhibition strength of short peptides derived from an ACE inhibitory peptide.", "doi": "10.1021\/jf202902r", "pubmedid": "21923188", "mw": "608.73", "pi": "8.59", "charge_ph7": "0.76", "gravy": "-0.575", "instability": "38.35", "hydrophobic": "0.5", "boman": "-1.3825", "helix": "0.5", "turn_pct": "0.0", "sheet": "0.75" }, { "id": "aceip1143", "seq": "YKYY", "length": "4", "detail": "Milk (bovine)", "source": "Milk", "ic50": "64.2 μM", "reference": "Identification of an antihypertensive peptide from peptic digest of wakame (Undaria pinnatifida).; Review on the angiotensin-I-converting enzyme (ACE) inhibitor peptides from marine proteins.; Vegetable foods: a cheap source of proteins and peptides with antihypertensive, antioxidant, and other less occurrence bioactivities.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1016\/s0955-2863(00)00110-8; 10.1007\/s12010-012-0024-y; 10.1016\/j.talanta.2012.12.041; 10.1016\/j.foodchem.2013.05.140; 10.1080\/10408398.2012.664829", "pubmedid": "11091100 23271625 23598136 23871047 24915368", "mw": "635.71", "pi": "8.43", "charge_ph7": "0.76", "gravy": "-1.95", "instability": "38.35", "hydrophobic": "0.0", "boman": "0.5", "helix": "0.25", "turn_pct": "0.0", "sheet": "0.75" }, { "id": "aceip1144", "seq": "YL", "length": "2", "detail": "Milk (Casein)", "source": "Milk", "ic50": "<20 mM", "reference": "Synthetic peptides corresponding to alpha-lactalbumin and beta-lactoglobulin sequences with angiotensin-I-converting enzyme inhibitory activity.; Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Three-dimensional holograph vector of atomic interaction field (3D-HoVAIF): a novel rotation-translation invariant 3D structure descriptor and its applications to peptides.; Bioactive peptides in amaranth (Amaranthus hypochondriacus) seed.; Quality and acceptability of a set-type yogurt made from camel milk.; Review on the angiotensin-I-converting enzyme (ACE) inhibitor peptides from marine proteins.; Peptides with angiotensin I converting enzyme (ACE) inhibitory activity generated from porcine skeletal muscle proteins by the action of meat-borne Lactobacillus.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1515\/bchm3.1996.377.4.259; 10.1021\/jf051263l; 10.1002\/psc.892; 10.1021\/jf072911z; 10.3168\/jds.2008-1408; 10.1007\/s12010-012-0024-y; 10.1016\/j.jprot.2013.06.023; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "8737991 16448176 17654623 18211015 19233778 23271625 23806758 23871047", "mw": "294.35", "pi": "5.52", "charge_ph7": "-0.24", "gravy": "1.25", "instability": "5.0", "hydrophobic": "0.5", "boman": "-2.39", "helix": "0.5", "turn_pct": "0.0", "sheet": "1.0" }, { "id": "aceip1145", "seq": "YLAGNQ", "length": "6", "detail": "Milk", "source": "Milk", "ic50": "14 μM", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.; Vegetable foods: a cheap source of proteins and peptides with antihypertensive, antioxidant, and other less occurrence bioactivities.; Rational design of angiotensin-I-converting enzyme inhibitory peptides by integrating in silico modeling and an in vitro assay.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1016\/j.foodchem.2012.09.092; 10.1016\/j.talanta.2012.12.041; 10.1002\/cmdc.201300132; 10.1080\/10408398.2012.664829", "pubmedid": "23194537 23598136 23740817 24915368", "mw": "664.71", "pi": "5.52", "charge_ph7": "-0.24", "gravy": "-0.5167", "instability": "-18.38", "hydrophobic": "0.3333", "boman": "-0.7583", "helix": "0.3333", "turn_pct": "0.3333", "sheet": "0.3333" }, { "id": "aceip1146", "seq": "YLEPA", "length": "5", "detail": "Meat", "source": "Meat", "ic50": null, "reference": "Isolation from alpha-zein of thermolysin peptides with angiotensin I-converting enzyme inhibitory activity.", "doi": "10.1271\/bbb.60.661", "pubmedid": "8829536", "mw": "591.65", "pi": "4.05", "charge_ph7": "-1.24", "gravy": "-0.16", "instability": "85.04", "hydrophobic": "0.6", "boman": "-0.99", "helix": "0.6", "turn_pct": "0.2", "sheet": "0.4" }, { "id": "aceip1147", "seq": "YLLF", "length": "4", "detail": "Milk (human)", "source": "Milk", "ic50": "172 μM", "reference": "Synthetic peptides corresponding to alpha-lactalbumin and beta-lactoglobulin sequences with angiotensin-I-converting enzyme inhibitory activity.; Analysis of novel angiotensin-I-converting enzyme inhibitory peptides from protease-hydrolyzed marine shrimp Acetes chinensis.; Quality and acceptability of a set-type yogurt made from camel milk.; Bioactive peptides derived from milk proteins and their health beneficial potentials: an update.", "doi": "10.1515\/bchm3.1996.377.4.259; 10.1002\/psc.789; 10.3168\/jds.2008-1408; 10.1039\/c0fo00016g", "pubmedid": "8737991 16981241 19233778 21773582", "mw": "554.68", "pi": "5.52", "charge_ph7": "-0.24", "gravy": "2.275", "instability": "7.5", "hydrophobic": "0.75", "boman": "-3.17", "helix": "0.5", "turn_pct": "0.0", "sheet": "1.0" }, { "id": "aceip1148", "seq": "YLYEIA", "length": "6", "detail": "Milk", "source": "Milk", "ic50": "500 μM", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "23194537", "mw": "770.87", "pi": "4.05", "charge_ph7": "-1.24", "gravy": "0.6667", "instability": "27.87", "hydrophobic": "0.5", "boman": "-1.6217", "helix": "0.5", "turn_pct": "0.0", "sheet": "0.6667" }, { "id": "aceip1149", "seq": "YLYEIAR", "length": "7", "detail": "Salmon | Skate", "source": "Fish", "ic50": "16 μM", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "23194537", "mw": "927.05", "pi": "6.0", "charge_ph7": "-0.24", "gravy": "-0.0714", "instability": "25.31", "hydrophobic": "0.4286", "boman": "-1.0014", "helix": "0.4286", "turn_pct": "0.0", "sheet": "0.5714" }, { "id": "aceip1150", "seq": "YLYEIARR", "length": "8", "detail": "Milk (caprine kefir)", "source": "Milk", "ic50": "86 μM", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "23194537", "mw": "1083.24", "pi": "8.59", "charge_ph7": "0.76", "gravy": "-0.625", "instability": "95.0", "hydrophobic": "0.375", "boman": "-0.5362", "helix": "0.375", "turn_pct": "0.0", "sheet": "0.5" }, { "id": "aceip1151", "seq": "YN", "length": "2", "detail": "Milk (Fermented Milk)", "source": "Milk", "ic50": "51 μM", "reference": "Review on the angiotensin-I-converting enzyme (ACE) inhibitor peptides from marine proteins.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1007\/s12010-012-0024-y; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "23271625 23871047", "mw": "295.29", "pi": "5.52", "charge_ph7": "-0.24", "gravy": "-2.4", "instability": "5.0", "hydrophobic": "0.0", "boman": "0.88", "helix": "0.0", "turn_pct": "0.5", "sheet": "0.5" }, { "id": "aceip1152", "seq": "YNKL", "length": "4", "detail": "Milk (Sheep raw milk cheese (synthesised))", "source": "Milk", "ic50": "21 μM", "reference": "Identification of an antihypertensive peptide from peptic digest of wakame (Undaria pinnatifida).; Review on the angiotensin-I-converting enzyme (ACE) inhibitor peptides from marine proteins.; Vegetable foods: a cheap source of proteins and peptides with antihypertensive, antioxidant, and other less occurrence bioactivities.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1016\/s0955-2863(00)00110-8; 10.1007\/s12010-012-0024-y; 10.1016\/j.talanta.2012.12.041; 10.1016\/j.foodchem.2013.05.140; 10.1080\/10408398.2012.664829", "pubmedid": "11091100 23271625 23598136 23871047 24915368", "mw": "536.62", "pi": "8.59", "charge_ph7": "0.76", "gravy": "-1.225", "instability": "45.47", "hydrophobic": "0.25", "boman": "-0.395", "helix": "0.5", "turn_pct": "0.25", "sheet": "0.5" }, { "id": "aceip1153", "seq": "YP", "length": "2", "detail": "Milk (human)", "source": "Milk", "ic50": "<20 mM", "reference": "Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Bioactive peptides in amaranth (Amaranthus hypochondriacus) seed.; Rheological, sensorial, and chemopreventive properties of milk fermented with exopolysaccharide-producing lactic cultures.; Antihypertensive peptides: production, bioavailability and incorporation into foods.; Antihypertensive peptides from food proteins: a review.; Peptides with angiotensin I converting enzyme (ACE) inhibitory activity generated from porcine skeletal muscle proteins by the action of meat-borne Lactobacillus.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1021\/jf051263l; 10.1021\/jf072911z; 10.3168\/jds.2008-1256; 10.1016\/j.cis.2010.11.001; 10.1039\/c2fo10192k; 10.1016\/j.jprot.2013.06.023; 10.1080\/10408398.2012.664829", "pubmedid": "16448176 18211015 19233777 21185549 22249830 23806758 24915368", "mw": "278.3", "pi": "5.52", "charge_ph7": "-0.24", "gravy": "-1.45", "instability": "66.7", "hydrophobic": "0.5", "boman": "0.07", "helix": "0.0", "turn_pct": "0.5", "sheet": "0.5" }, { "id": "aceip1154", "seq": "YPER", "length": "4", "detail": "Milk (Fermented Milk)", "source": "Milk", "ic50": null, "reference": "What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1016\/j.foodchem.2013.05.140", "pubmedid": "23871047", "mw": "563.6", "pi": "6.0", "charge_ph7": "-0.24", "gravy": "-2.725", "instability": "81.8", "hydrophobic": "0.25", "boman": "1.125", "helix": "0.25", "turn_pct": "0.25", "sheet": "0.25" }, { "id": "aceip1155", "seq": "YPF", "length": "3", "detail": "Milk-Cheese (Goat milk protein and cheeses)", "source": "Milk", "ic50": ">1000 μM", "reference": "Angiotensin-converting enzyme inhibitory activity of peptides derived from caprine kefir.; Quantitative structure-activity relationship study of bitter di- and tri-peptides including relationship with angiotensin I-converting enzyme inhibitory activity.; QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.3168\/jds.S0022-0302(05)73032-0; 10.1002\/psc.800; 10.1007\/s00894-010-0862-x; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "16162521 17117396 20941517 23871047", "mw": "425.48", "pi": "5.52", "charge_ph7": "-0.24", "gravy": "-0.0333", "instability": "112.0", "hydrophobic": "0.6667", "boman": "-0.9467", "helix": "0.0", "turn_pct": "0.3333", "sheet": "0.6667" }, { "id": "aceip1156", "seq": "YPFPGPI", "length": "7", "detail": "Synthesized", "source": "Synthesized", "ic50": "299.25 μM", "reference": "Evaluation of the allergenicity of goat milk, cow milk, and their lactosera in a guinea pig model.; Bioactive peptides derived from milk proteins and their health beneficial potentials: an update.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.3168\/jds.2008-1125; 10.1039\/c0fo00016g; 10.1016\/j.foodchem.2012.09.092", "pubmedid": "19233776 21773582 23194537", "mw": "789.92", "pi": "5.52", "charge_ph7": "-0.24", "gravy": "0.1143", "instability": "81.23", "hydrophobic": "0.7143", "boman": "-1.2429", "helix": "0.0", "turn_pct": "0.5714", "sheet": "0.4286" }, { "id": "aceip1157", "seq": "YPFPGPIP", "length": "8", "detail": "Milk (human) | Cereals", "source": "Milk | Cereal", "ic50": "500 μM", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "23194537", "mw": "887.03", "pi": "5.52", "charge_ph7": "-0.24", "gravy": "-0.1", "instability": "68.72", "hydrophobic": "0.75", "boman": "-1.0875", "helix": "0.0", "turn_pct": "0.625", "sheet": "0.375" }, { "id": "aceip1158", "seq": "YPFPGPIPN", "length": "9", "detail": "Milk (human)", "source": "Milk", "ic50": "14.8 μM", "reference": "Isolation and structural analysis of antihypertensive peptides that exist naturally in Gouda cheese.; Identification of angiotensin-I-converting enzyme inhibitory peptides derived from sodium caseinate hydrolysates produced by Lactobacillus helveticus NCC 2765.; QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.; Antihypertensive peptides: production, bioavailability and incorporation into foods.; Antihypertensive peptides from food proteins: a review.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.3168\/jds.S0022-0302(00)75013-2; 10.1021\/jf049510t; 10.1007\/s00894-010-0862-x; 10.1016\/j.cis.2010.11.001; 10.1039\/c2fo10192k; 10.1016\/j.foodchem.2012.09.092; 10.1080\/10408398.2012.664829", "pubmedid": "10908049 15537298 20941517 21185549 22249830 23194537 24915368", "mw": "1001.13", "pi": "5.52", "charge_ph7": "-0.24", "gravy": "-0.4778", "instability": "62.2", "hydrophobic": "0.6667", "boman": "-0.7867", "helix": "0.0", "turn_pct": "0.6667", "sheet": "0.3333" }, { "id": "aceip1159", "seq": "YPGIA", "length": "5", "detail": "Milk (Casein)", "source": "Milk", "ic50": "46.56>1000 μM", "reference": "Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1080\/10408398.2012.664829", "pubmedid": "24915368", "mw": "519.59", "pi": "5.52", "charge_ph7": "-0.24", "gravy": "0.6", "instability": "15.7", "hydrophobic": "0.6", "boman": "-1.506", "helix": "0.2", "turn_pct": "0.4", "sheet": "0.4" }, { "id": "aceip1160", "seq": "YPK", "length": "3", "detail": "Milk (human)", "source": "Milk", "ic50": "10.5 mg\/ml", "reference": "Plant food-derived Angiotensin I converting enzyme inhibitory peptides.; Vegetable foods: a cheap source of proteins and peptides with antihypertensive, antioxidant, and other less occurrence bioactivities.", "doi": "10.1021\/jf900494d; 10.1016\/j.talanta.2012.12.041", "pubmedid": "19449887 23598136", "mw": "406.48", "pi": "8.59", "charge_ph7": "0.76", "gravy": "-2.2667", "instability": "47.8", "hydrophobic": "0.3333", "boman": "0.5733", "helix": "0.3333", "turn_pct": "0.3333", "sheet": "0.3333" }, { "id": "aceip1161", "seq": "YPLDL", "length": "5", "detail": "Milk-Cheese (Goat milk protein and cheeses)", "source": "Milk", "ic50": "51 μM", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "23194537", "mw": "619.71", "pi": "4.05", "charge_ph7": "-1.24", "gravy": "0.24", "instability": "32.68", "hydrophobic": "0.6", "boman": "-1.604", "helix": "0.4", "turn_pct": "0.4", "sheet": "0.6" }, { "id": "aceip1162", "seq": "YPLDLF", "length": "6", "detail": "Flaxseed", "source": "Plants", "ic50": "24.4 μM", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "23194537", "mw": "766.88", "pi": "4.05", "charge_ph7": "-1.24", "gravy": "0.6667", "instability": "28.9", "hydrophobic": "0.6667", "boman": "-1.8333", "helix": "0.3333", "turn_pct": "0.3333", "sheet": "0.6667" }, { "id": "aceip1163", "seq": "YPQRDMPIQ", "length": "9", "detail": "Milk (bovine, buffalo and ovine)", "source": "Milk", "ic50": "0 0", "reference": "Putting microbes to work: dairy fermentation, cell factories and bioactive peptides. Part I: overview.", "doi": "10.1002\/biot.200600246", "pubmedid": "17407210", "mw": "1147.3", "pi": "5.84", "charge_ph7": "-0.24", "gravy": "-1.4556", "instability": "92.82", "hydrophobic": "0.4444", "boman": "-0.0011", "helix": "0.1111", "turn_pct": "0.3333", "sheet": "0.2222" }, { "id": "aceip1164", "seq": "YPR", "length": "3", "detail": "Casein", "source": "Milk", "ic50": "<20 mM", "reference": "Structure and activity of angiotensin I converting enzyme inhibitory peptides from sake and sake lees.; Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.", "doi": "10.1271\/bbb.58.1767; 10.1021\/jf051263l", "pubmedid": "7765503 16448176", "mw": "434.49", "pi": "8.75", "charge_ph7": "0.76", "gravy": "-2.4667", "instability": "22.67", "hydrophobic": "0.3333", "boman": "0.9533", "helix": "0.0", "turn_pct": "0.3333", "sheet": "0.3333" }, { "id": "aceip1165", "seq": "YPSFQPQPLIYP", "length": "12", "detail": "Milk (bovine, buffalo and ovine)", "source": "Milk", "ic50": "4.8 μM", "reference": "Inhibition of angiotensin-converting enzyme by synthetic peptide fragments of various beta-caseins.", "doi": "", "pubmedid": "1368548", "mw": "1449.65", "pi": "5.52", "charge_ph7": "-0.24", "gravy": "-0.475", "instability": "93.93", "hydrophobic": "0.5833", "boman": "-0.7483", "helix": "0.0833", "turn_pct": "0.4167", "sheet": "0.4167" }, { "id": "aceip1166", "seq": "YPSYGLNY", "length": "8", "detail": "Bovine", "source": "Bovine", "ic50": null, "reference": "Rheological, sensorial, and chemopreventive properties of milk fermented with exopolysaccharide-producing lactic cultures.", "doi": "10.3168\/jds.2008-1256", "pubmedid": "19233777", "mw": "976.04", "pi": "5.52", "charge_ph7": "-0.24", "gravy": "-0.8", "instability": "37.64", "hydrophobic": "0.25", "boman": "-0.3725", "helix": "0.125", "turn_pct": "0.5", "sheet": "0.5" }, { "id": "aceip1167", "seq": "YPYY", "length": "4", "detail": "Milk (human)", "source": "Milk", "ic50": "90.9 μM", "reference": "Antihypertensive peptides from food proteins: a review.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.; Effect of Jatropha curcas peptide fractions on the angiotensin I-converting enzyme inhibitory activity.", "doi": "10.1039\/c2fo10192k; 10.1016\/j.foodchem.2013.05.140; 10.1155\/2013\/541947", "pubmedid": "22249830 23871047 24224169", "mw": "604.65", "pi": "5.52", "charge_ph7": "-0.24", "gravy": "-1.375", "instability": "69.2", "hydrophobic": "0.25", "boman": "0.105", "helix": "0.0", "turn_pct": "0.25", "sheet": "0.75" }, { "id": "aceip1168", "seq": "YQ", "length": "2", "detail": "Milk (Fermented Milk)", "source": "Milk", "ic50": "4-628 μM", "reference": "Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1080\/10408398.2012.664829", "pubmedid": "24915368", "mw": "309.32", "pi": "5.52", "charge_ph7": "-0.24", "gravy": "-2.4", "instability": "5.0", "hydrophobic": "0.0", "boman": "0.75", "helix": "0.0", "turn_pct": "0.0", "sheet": "0.5" }, { "id": "aceip1169", "seq": "YQAP", "length": "4", "detail": "Soybean", "source": "Legume", "ic50": null, "reference": "Vegetable foods: a cheap source of proteins and peptides with antihypertensive, antioxidant, and other less occurrence bioactivities.", "doi": "10.1016\/j.talanta.2012.12.041", "pubmedid": "23598136", "mw": "477.51", "pi": "5.52", "charge_ph7": "-0.24", "gravy": "-1.15", "instability": "55.65", "hydrophobic": "0.5", "boman": "-0.0775", "helix": "0.25", "turn_pct": "0.25", "sheet": "0.25" }, { "id": "aceip1170", "seq": "YQEPVL", "length": "6", "detail": "Milk (bovine) | Carp | Cereals (Wheat) | Pork | Chicken", "source": "Milk | Fish | Cereal | Porcine | Chicken", "ic50": "280 μM", "reference": "Evaluation of the allergenicity of goat milk, cow milk, and their lactosera in a guinea pig model.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.3168\/jds.2008-1125; 10.1016\/j.foodchem.2012.09.092", "pubmedid": "19233776 23194537", "mw": "747.84", "pi": "4.05", "charge_ph7": "-1.24", "gravy": "-0.3167", "instability": "104.63", "hydrophobic": "0.5", "boman": "-0.97", "helix": "0.3333", "turn_pct": "0.1667", "sheet": "0.5" }, { "id": "aceip1171", "seq": "YQEPVLGPVR", "length": "10", "detail": "Egg (Ovalbumin)", "source": "Egg", "ic50": null, "reference": "Evaluation of the allergenicity of goat milk, cow milk, and their lactosera in a guinea pig model.", "doi": "10.3168\/jds.2008-1125", "pubmedid": "19233776", "mw": "1157.32", "pi": "6.0", "charge_ph7": "-0.24", "gravy": "-0.42", "instability": "86.04", "hydrophobic": "0.5", "boman": "-0.808", "helix": "0.2", "turn_pct": "0.3", "sheet": "0.4" }, { "id": "aceip1172", "seq": "YQEPVLGPVRGPFPIIV", "length": "17", "detail": "Cereals (Rice)", "source": "Cereal", "ic50": null, "reference": "Identification of angiotensin-I-converting enzyme inhibitory peptides derived from sodium caseinate hydrolysates produced by Lactobacillus helveticus NCC 2765.", "doi": "10.1021\/jf049510t", "pubmedid": "15537298", "mw": "1881.22", "pi": "6.0", "charge_ph7": "-0.24", "gravy": "0.4824", "instability": "67.4", "hydrophobic": "0.6471", "boman": "-1.5224", "helix": "0.1176", "turn_pct": "0.3529", "sheet": "0.4706" }, { "id": "aceip1173", "seq": "YQEPVLQPVR", "length": "10", "detail": "Egg (Ovalbumin)", "source": "Egg", "ic50": "300 μM", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "23194537", "mw": "1228.4", "pi": "6.0", "charge_ph7": "-0.24", "gravy": "-0.73", "instability": "137.9", "hydrophobic": "0.5", "boman": "-0.578", "helix": "0.2", "turn_pct": "0.2", "sheet": "0.4" }, { "id": "aceip1174", "seq": "YQKFPQY", "length": "7", "detail": "ND", "source": "ND", "ic50": "20.08 μM", "reference": "Bioactive peptides in ovine and caprine cheeselike systems prepared with proteases from Cynara cardunculus.; Antihypertensive peptides: production, bioavailability and incorporation into foods.; Antihypertensive peptides from food proteins: a review.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.3168\/jds.S0022-0302(06)72370-0; 10.1016\/j.cis.2010.11.001; 10.1039\/c2fo10192k; 10.1016\/j.foodchem.2012.09.092; 10.1080\/10408398.2012.664829", "pubmedid": "16899666 21185549 22249830 23194537 24915368", "mw": "973.08", "pi": "8.5", "charge_ph7": "0.76", "gravy": "-1.7571", "instability": "52.83", "hydrophobic": "0.2857", "boman": "0.2286", "helix": "0.1429", "turn_pct": "0.1429", "sheet": "0.4286" }, { "id": "aceip1175", "seq": "YQNPRLGPTGELDPATQPIVAVHNPVIV", "length": "28", "detail": "Rapeseed", "source": "Plants", "ic50": "14.53 μM", "reference": "Identification of angiotensin I-converting enzyme inhibitory peptides from koumiss, a traditional fermented mare's milk.", "doi": "10.3168\/jds.2009-2672", "pubmedid": "20172208", "mw": "2996.38", "pi": "5.32", "charge_ph7": "-1.15", "gravy": "-0.1143", "instability": "19.5", "hydrophobic": "0.5357", "boman": "-0.9889", "helix": "0.1786", "turn_pct": "0.3571", "sheet": "0.3929" }, { "id": "aceip1176", "seq": "YQQP", "length": "4", "detail": "Meat", "source": "Meat", "ic50": null, "reference": "Isolation from alpha-zein of thermolysin peptides with angiotensin I-converting enzyme inhibitory activity.", "doi": "10.1271\/bbb.60.661", "pubmedid": "8829536", "mw": "534.56", "pi": "5.52", "charge_ph7": "-0.24", "gravy": "-2.475", "instability": "103.8", "hydrophobic": "0.25", "boman": "0.715", "helix": "0.0", "turn_pct": "0.25", "sheet": "0.25" }, { "id": "aceip1177", "seq": "YQQPVLGPVR", "length": "10", "detail": "Flaxseed", "source": "Plants", "ic50": "300 μM", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1016\/j.foodchem.2012.09.092", "pubmedid": "23194537", "mw": "1156.33", "pi": "8.75", "charge_ph7": "0.76", "gravy": "-0.42", "instability": "86.04", "hydrophobic": "0.5", "boman": "-0.836", "helix": "0.1", "turn_pct": "0.3", "sheet": "0.4" }, { "id": "aceip1178", "seq": "YQY", "length": "3", "detail": "Milk (bovine) | Milk (Casein)", "source": "Milk", "ic50": "4 μM", "reference": "Vegetable foods: a cheap source of proteins and peptides with antihypertensive, antioxidant, and other less occurrence bioactivities.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1016\/j.talanta.2012.12.041; 10.1080\/10408398.2012.664829", "pubmedid": "23598136 24915368", "mw": "472.49", "pi": "5.52", "charge_ph7": "-0.24", "gravy": "-2.0333", "instability": "-18.47", "hydrophobic": "0.0", "boman": "0.5467", "helix": "0.0", "turn_pct": "0.0", "sheet": "0.6667" }, { "id": "aceip1179", "seq": "YRGGLEPINF", "length": "10", "detail": "Milk (Sheep raw milk cheese (synthesised))", "source": "Milk", "ic50": null, "reference": "Antihypertensive peptides from food proteins: a review.", "doi": "10.1039\/c2fo10192k", "pubmedid": "22249830", "mw": "1165.3", "pi": "6.0", "charge_ph7": "-0.24", "gravy": "-0.41", "instability": "0.17", "hydrophobic": "0.4", "boman": "-0.858", "helix": "0.2", "turn_pct": "0.4", "sheet": "0.4" }, { "id": "aceip1180", "seq": "YRPY", "length": "4", "detail": "Milk (bovine) | Casein", "source": "Milk", "ic50": "320 μM", "reference": "Angiotensin I-converting enzyme inhibitory peptides derived from bonito bowels autolysate.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1271\/bbb.57.695; 10.1016\/j.foodchem.2013.05.140; 10.1080\/10408398.2012.664829", "pubmedid": "7763772 23871047 24915368", "mw": "597.66", "pi": "8.59", "charge_ph7": "0.76", "gravy": "-2.175", "instability": "13.38", "hydrophobic": "0.25", "boman": "0.75", "helix": "0.0", "turn_pct": "0.25", "sheet": "0.5" }, { "id": "aceip1181", "seq": "YSQQQQ", "length": "6", "detail": "ND", "source": "ND", "ic50": "860 μM", "reference": "Isolation from alpha-zein of thermolysin peptides with angiotensin I-converting enzyme inhibitory activity.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.", "doi": "10.1271\/bbb.60.661; 10.1016\/j.foodchem.2012.09.092", "pubmedid": "8829536 23194537", "mw": "780.78", "pi": "5.52", "charge_ph7": "-0.24", "gravy": "-2.6833", "instability": "136.73", "hydrophobic": "0.0", "boman": "1.07", "helix": "0.0", "turn_pct": "0.1667", "sheet": "0.1667" }, { "id": "aceip1182", "seq": "YTAGV", "length": "5", "detail": "Cheese (Manchego cheese)", "source": "Milk", "ic50": "6.59-27.38 μM", "reference": "Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1080\/10408398.2012.664829", "pubmedid": "24915368", "mw": "509.55", "pi": "5.52", "charge_ph7": "-0.24", "gravy": "0.72", "instability": "-8.98", "hydrophobic": "0.4", "boman": "-1.278", "helix": "0.2", "turn_pct": "0.2", "sheet": "0.6" }, { "id": "aceip1183", "seq": "YV", "length": "2", "detail": "Milk (bovine) | Casein | Amaranth | Cereals | Sake | Chicken connectin", "source": "Milk | Plants | Cereal | Chicken", "ic50": "<20 mM", "reference": "Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Isolation and characterization of peptides with antihypertensive activity in foodstuffs.", "doi": "10.1021\/jf051263l; 10.1080\/10408398.2012.664829", "pubmedid": "16448176 24915368", "mw": "280.32", "pi": "5.52", "charge_ph7": "-0.24", "gravy": "1.45", "instability": "5.0", "hydrophobic": "0.5", "boman": "-1.95", "helix": "0.0", "turn_pct": "0.0", "sheet": "1.0" }, { "id": "aceip1184", "seq": "YVA", "length": "3", "detail": "Sardine | Chicken", "source": "Fish | Chicken", "ic50": "<20 mM", "reference": "Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.", "doi": "10.1021\/jf051263l", "pubmedid": "16448176", "mw": "351.4", "pi": "5.52", "charge_ph7": "-0.24", "gravy": "1.5667", "instability": "6.67", "hydrophobic": "0.6667", "boman": "-1.9033", "helix": "0.3333", "turn_pct": "0.0", "sheet": "0.6667" }, { "id": "aceip1185", "seq": "YVP", "length": "3", "detail": "ND", "source": "ND", "ic50": "200 μM", "reference": "Inhibition of angiotensin-converting enzyme by synthetic peptide fragments of human kappa-casein.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1016\/j.foodchem.2013.05.140", "pubmedid": "1368540 23871047", "mw": "377.43", "pi": "5.52", "charge_ph7": "-0.24", "gravy": "0.4333", "instability": "70.87", "hydrophobic": "0.6667", "boman": "-1.3", "helix": "0.0", "turn_pct": "0.3333", "sheet": "0.6667" }, { "id": "aceip1186", "seq": "YW", "length": "2", "detail": "Flaxseed", "source": "Plants", "ic50": "<10 μM", "reference": "Structure and activity of angiotensin I converting enzyme inhibitory peptides from sake and sake lees.; Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.; Assessing the dependence of (51)V A(z) value on the aromatic ring orientation of V(IV)O(2+) pyridine complexes.; Antihypertensive peptides from food proteins: a review.; Vegetable foods: a cheap source of proteins and peptides with antihypertensive, antioxidant, and other less occurrence bioactivities.; What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach.", "doi": "10.1271\/bbb.58.1767; 10.1021\/jf051263l; 10.1021\/ic9001779; 10.1039\/c2fo10192k; 10.1016\/j.talanta.2012.12.041; 10.1016\/j.foodchem.2013.05.140", "pubmedid": "7765503 16448176 19449891 22249830 23598136 23871047", "mw": "367.4", "pi": "5.52", "charge_ph7": "-0.24", "gravy": "-1.1", "instability": "-46.85", "hydrophobic": "0.5", "boman": "-1.095", "helix": "0.0", "turn_pct": "0.0", "sheet": "1.0" }, { "id": "aceip1187", "seq": "YY", "length": "2", "detail": "ND", "source": "ND", "ic50": null, "reference": "Quantitative structure-activity relationship study of bitter di- and tri-peptides including relationship with angiotensin I-converting enzyme inhibitory activity.", "doi": "10.1002\/psc.800", "pubmedid": "17117396", "mw": "344.36", "pi": "5.52", "charge_ph7": "-0.24", "gravy": "-1.3", "instability": "66.7", "hydrophobic": "0.0", "boman": "0.14", "helix": "0.0", "turn_pct": "0.0", "sheet": "1.0" }, { "id": "aceip1188", "seq": "YYAPF", "length": "5", "detail": "ND", "source": "ND", "ic50": "26.3 μM", "reference": "A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.; Vegetable foods: a cheap source of proteins and peptides with antihypertensive, antioxidant, and other less occurrence bioactivities.", "doi": "10.1016\/j.foodchem.2012.09.092; 10.1016\/j.talanta.2012.12.041", "pubmedid": "23194537 23598136", "mw": "659.73", "pi": "5.52", "charge_ph7": "-0.24", "gravy": "0.08", "instability": "157.08", "hydrophobic": "0.6", "boman": "-0.902", "helix": "0.2", "turn_pct": "0.2", "sheet": "0.6" }, { "id": "aceip1189", "seq": "YYAPFDGIL", "length": "9", "detail": "Egg (Ovalbumin)", "source": "Egg", "ic50": "83 μM", "reference": "QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.; A new QSAR model, for angiotensin I-converting enzyme inhibitory oligopeptides.; Vegetable foods: a cheap source of proteins and peptides with antihypertensive, antioxidant, and other less occurrence bioactivities.", "doi": "10.1007\/s00894-010-0862-x; 10.1016\/j.foodchem.2012.09.092; 10.1016\/j.talanta.2012.12.041", "pubmedid": "20941517 23194537 23598136", "mw": "1058.18", "pi": "4.05", "charge_ph7": "-1.24", "gravy": "0.5333", "instability": "117.39", "hydrophobic": "0.5556", "boman": "-1.5122", "helix": "0.2222", "turn_pct": "0.3333", "sheet": "0.5556" }, { "id": "aceip1190", "seq": "YYG", "length": "3", "detail": "Fungi (Agaricus bisporus)", "source": "Fungi", "ic50": null, "reference": "Quantitative structure-activity relationship study of bitter di- and tri-peptides including relationship with angiotensin I-converting enzyme inhibitory activity.; QSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors.; What are the ideal properties for functional food peptides with antihypertensive effect? 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