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Peptide record

TPDB47709

ACE inhibitor ACE inhibitors Antihypertensive standard
5 amino acids
Basic Information
3D PDB MODEL
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TPDB47709
ACE inhibitor
ACE inhibitors Antihypertensive
Cardiometabolic peptides
Peptipedia AHTPDB AHTpin
standard
No
A 5-aa standard natural multi-activity (ACE inhibitors and Antihypertensive) peptide sequence curated from Peptipedia, AHTPDB, and AHTpin, with an available 3D structural model.
Sequence
VLIVP
Physicochemical Analysis
C27H49N5O6
ARNDCEQGHKMFSTWY
V
539.72
6.02
0
0
4
-0
-0.28
3.020
272.00
Mammalian: 100 hour Yeast: >20 hour 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
0
H
1
I
1
L
0
K
0
M
0
F
1
P
0
S
0
T
0
W
0
Y
2
V
Amino Acid Distribution
A: 0 R: 0 N: 0 D: 0 C: 0 E: 0 Q: 0 G: 0 H: 0 I: 1 L: 1 K: 0 M: 0 F: 0 P: 1 S: 0 T: 0 W: 0 Y: 0 V: 2
Chemical Descriptors
5
C27H49N5O6
539.72
6.02
-0
-0.28
3.020
539.7059
539.3671
Evidence Records 2 records
Evidence 1 Activity

Activity

IC50
ACE inhibitors
1.69 µM
This peptide was synthesized using solid-phase FMOC chemistry. The IC50 for ACE inhibition was 1.69 ± 0.17 micromole. The synthetic peptide was a potent competitive inhibitor of ACE with a Ki of 4.5 ± 0.25 × 10-6 M. This peptide was resistant to digestion by proteases of the gastrointestinal tract. The antihypertensive property of this peptide derived from glycinin might find importance in the development of therapeutic functional foods.
ACE inhibitor
ah

Source & Reference

NA
Gouda K. G. M., Gowda L. R. A., Rao G. A., Prakash V.
Angiotensin I-Converting Enzyme Inhibitory Peptide Derived from Glycinin, the 11S Globulin of Soybean (Glycine max) . J. Agric. Food Chem., 54 (13), 4568 -4573, 2006.
2006
Journal

Other

5
Protease P was applied to hydrolyse the glycynin, the major storage protein of soybean.
Evidence 2 Activity

Activity

IC50
Antihypertensive
1.69 µM
This peptide was synthesized using solid-phase FMOC chemistry. The IC50 for ACE inhibition was 1.69 ± 0.17 micromole. The synthetic peptide was a potent competitive inhibitor of ACE with a Ki of 4.5 ± 0.25 × 10-6 M. This peptide was resistant to digestion by proteases of the gastrointestinal tract. The antihypertensive property of this peptide derived from glycinin might find importance in the development of therapeutic functional foods.
ACE inhibitor
ah

Source & Reference

AHTPDB
Gouda K. G. M., Gowda L. R. A., Rao G. A., Prakash V.
Angiotensin I-Converting Enzyme Inhibitory Peptide Derived from Glycinin, the 11S Globulin of Soybean (Glycine max) . J. Agric. Food Chem., 54 (13), 4568 -4573, 2006.
2006
Journal

Other

Source Activity Label Source Definition
Antihypertensive
AHTPDB manually curated experimentally validated antihypertensive peptide annotation.
5
Protease P was applied to hydrolyse the glycynin, the major storage protein of soybean.
Additional Detail Fields 1 fields
5