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Peptide record

TPDB00752

ACE inhibitor ACE inhibitors Antihypertensive Antioxidant Neuropeptide standard
5 amino acids
Basic Information
3D PDB MODEL
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TPDB00752
ACE inhibitor
ACE inhibitors Antihypertensive Antioxidant Neuropeptide
Cardiometabolic peptides Neuroactive peptides Functional / health-promoting peptides
FermFooDB Peptipedia AHTPDB AHTpin AnOxPePred - 1.0 AODB Multi-AOP
standard
No
A 5-aa standard natural multi-activity (ACE inhibitors, Antihypertensive, Antioxidant, and other sources) peptide sequence curated from FermFooDB, Peptipedia, AHTPDB, and other sources, with an available 3D structural model.
Sequence
HLPLP
Physicochemical Analysis
C28H45N7O6
ARNDCEQGIKMFSTWYV
LP
575.71
7.85
1
0
2
+0
0.74
0.240
156.00
Mammalian: 3.5 hour Yeast: 10 min E.coli: >10 hour
0
0.00
0
Residue Composition
number
0
A
0
R
0
N
0
D
0
C
0
E
0
Q
0
G
1
H
0
I
2
L
0
K
0
M
0
F
2
P
0
S
0
T
0
W
0
Y
0
V
Amino Acid Distribution
A: 0 R: 0 N: 0 D: 0 C: 0 E: 0 Q: 0 G: 0 H: 1 I: 0 L: 2 K: 0 M: 0 F: 0 P: 2 S: 0 T: 0 W: 0 Y: 0 V: 0
Chemical Descriptors
5
C28H45N7O6
575.71
7.85
+0
0.74
0.240
575.6984
575.3421
Evidence Records 3 records
Evidence 1 Activity

Activity

IC50
ACE inhibitors
41.00 µM
Inhibitor of Angiotensin-Converting Enzyme (ACE) (EC 3.4.15.1) (MEROPS ID: M02-001) antihypertensive peptide in vivo in rats.
ACE inhibitor
ah

Source & Reference

FermFooDB
Kohmura M., Nio N., Kubo K., Minoshima Y., Munekata E., Ariyoshi Y.
Inhibition of angiotensin-converting enzyme by synthetic peptides of human beta-casein. Agric. Biol. Chem., 53(8), 2107-2114 (1989)
1989
Journal

Other

5
BIOPEP-UWM database of bioactive peptides SMILES: [H][C@](N)(Cc1cnc[nH]1)C(=O)N[C@@]([H])(CC(C)C)C(=O)N1CCC[C@@]1([H])C(=O)N[C@@]([H])(CC(C)C)C(=O)N1CCC[C@@]1([H])C(O)=O InChI=1S/C28H45N7O6/c1-16(2)11-20(32-24(36)19(29)13-18-14-30-15-31-18)26(38)34-9-5-7-22(34)25(37)33-21(12-17(3)4)27(39)35-10-6-8-23(35)28(40)41/h14-17,19-23H,5-13,29H2,1-4H3,(H,30,31)(H,32,36)(H,33,37)(H,40,41)/t19-,20-,21-,22-,23-/m0/s1 InChIKey: FGQVFEKPNYGHEX-VUBDRERZSA-N Information concerning Angiotensin-Converting Enzyme (ACE) is available in MEROPS database of proteolytic enzymes (http://merops.sanger.ac.uk/) ID: M02-001 Another value of peptide IC50 (EC50) = 21 uM. Hernández-Ledesma B., Quirós A., Amigo L., Recio I., 2007, Identification of bioactive peptides after digestion of human milk and infant formula with pepsin and pancreatin. Int. Dairy J., 17, 42-49 Antihypertensive activity in vivo in rats: Sanchez-Rivera L., Ferreira Santos P., Miralles B., Carron R., Montero J., Recio I., 2016, Peptide fragments from beta-casein f(134–138), HLPLP, generated by the action of rat blood plasma peptidases show potent antihypertensive activity. Food Res. Int., 88, 348-353
Evidence 2 Activity

Activity

IC50
Antihypertensive
41.00 µM
Inhibitor of Angiotensin-Converting Enzyme (ACE) (EC 3.4.15.1) (MEROPS ID: M02-001) antihypertensive peptide in vivo in rats.
ACE inhibitor
ah

Source & Reference

AHTPDB FermFooDB
Kohmura M., Nio N., Kubo K., Minoshima Y., Munekata E., Ariyoshi Y.
Inhibition of angiotensin-converting enzyme by synthetic peptides of human beta-casein. Agric. Biol. Chem., 53(8), 2107-2114 (1989)
1989
Journal

Other

Source Activity Label Source Definition
Antihypertensive
AHTPDB manually curated experimentally validated antihypertensive peptide annotation.
5
BIOPEP-UWM database of bioactive peptides SMILES: [H][C@](N)(Cc1cnc[nH]1)C(=O)N[C@@]([H])(CC(C)C)C(=O)N1CCC[C@@]1([H])C(=O)N[C@@]([H])(CC(C)C)C(=O)N1CCC[C@@]1([H])C(O)=O InChI=1S/C28H45N7O6/c1-16(2)11-20(32-24(36)19(29)13-18-14-30-15-31-18)26(38)34-9-5-7-22(34)25(37)33-21(12-17(3)4)27(39)35-10-6-8-23(35)28(40)41/h14-17,19-23H,5-13,29H2,1-4H3,(H,30,31)(H,32,36)(H,33,37)(H,40,41)/t19-,20-,21-,22-,23-/m0/s1 InChIKey: FGQVFEKPNYGHEX-VUBDRERZSA-N Information concerning Angiotensin-Converting Enzyme (ACE) is available in MEROPS database of proteolytic enzymes (http://merops.sanger.ac.uk/) ID: M02-001 Another value of peptide IC50 (EC50) = 21 uM. Hernández-Ledesma B., Quirós A., Amigo L., Recio I., 2007, Identification of bioactive peptides after digestion of human milk and infant formula with pepsin and pancreatin. Int. Dairy J., 17, 42-49 Antihypertensive activity in vivo in rats: Sanchez-Rivera L., Ferreira Santos P., Miralles B., Carron R., Montero J., Recio I., 2016, Peptide fragments from beta-casein f(134–138), HLPLP, generated by the action of rat blood plasma peptidases show potent antihypertensive activity. Food Res. Int., 88, 348-353
Evidence 3 Activity

Activity

Antioxidative activity
Antioxidant

Source & Reference

AODB FermFooDB
DFBP
Additional Detail Fields 1 fields
5