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Peptide record

TPDB66658

ACE inhibitor from cuttlefish (Sepia officinalis) ACE inhibitors standard
5 amino acids
Basic Information
3D PDB MODEL
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TPDB66658
ACE inhibitor from cuttlefish (Sepia officinalis)
ACE inhibitors
Cardiometabolic peptides
Peptipedia
standard
No
A 5-aa standard natural ace inhibitors peptide sequence curated from Peptipedia, with an available 3D structural model.
Sequence
VELYP
Physicochemical Analysis
C30H45N5O9
ARNDCQGHIKMFSTW
ELPYV
619.72
3.29
0
1
3
-1
1.04
0.320
136.00
Mammalian: 100 hour Yeast: >20 hour E.coli: >10 hour
1490
240.43
1
Residue Composition
number
0
A
0
R
0
N
0
D
0
C
1
E
0
Q
0
G
0
H
0
I
1
L
0
K
0
M
0
F
1
P
0
S
0
T
0
W
1
Y
1
V
Amino Acid Distribution
A: 0 R: 0 N: 0 D: 0 C: 0 E: 1 Q: 0 G: 0 H: 0 I: 0 L: 1 K: 0 M: 0 F: 0 P: 1 S: 0 T: 0 W: 0 Y: 1 V: 1
Chemical Descriptors
5
C30H45N5O9
619.72
3.29
-1
1.04
0.320
619.7046
619.3206
Evidence Records 1 records
Evidence 1 Activity

Activity

IC50
ACE inhibitors
5.22 µM
ACE inhibitor
ah

Source & Reference

NA
Balti R., Bougatef A., Sila A., Guillochon D., Dhulster P., Nedjar-Arroume N.
Nine novel angiotensin I-converting enzyme (ACE) inhibitory peptides from cuttlefish (Sepia officinalis) muscle protein hydrolysates and antihypertensive effect of the potent active peptide in spontaneously hypertensive rats. Food Chem., 170, 519-525
2015
Journal

Other

5
BIOPEP-UWM database of bioactive peptides SMILES: N[C@@H](C(C)C)C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC1=CC=C(C=C1)O)C(=O)N2[C@@H](CCC2)C(=O)O InChI=1S/C30H45N5O9/c1-16(2)14-21(33-26(39)20(11-12-24(37)38)32-28(41)25(31)17(3)4)27(40)34-22(15-18-7-9-19(36)10-8-18)29(42)35-13-5-6-23(35)30(43)44/h7-10,16-17,20-23,25,36H,5-6,11-15,31H2,1-4H3,(H,32,41)(H,33,39)(H,34,40)(H,37,38)(H,43,44)/t20-,21-,22-,23-,25-/m0/s1 InChIKey=IJQMCDFGQCCCGV-AQBORDMYSA-N
Additional Detail Fields 1 fields
5