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Peptide record

TPDB47594

ACE inhibitor cyclic dipeptides (CDPs) ACE inhibitors Antihypertensive Selfassembly standard
2 amino acids
Basic Information
3D PDB MODEL
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TPDB47594
ACE inhibitor cyclic dipeptides (CDPs)
ACE inhibitors Antihypertensive Selfassembly
Cardiometabolic peptides Self-assembling and biomaterial peptides
Peptipedia AHTPDB AHTpin SAPdb
standard
No
A 2-aa standard natural multi-activity (ACE inhibitors, Antihypertensive, and Selfassembly) peptide sequence curated from Peptipedia, AHTPDB, AHTpin, and other sources, with an available 3D structural model.
Sequence
GS
Physicochemical Analysis
C5H10N2O4
ARNDCEQHILKMFPTWYV
GS
162.15
6.02
0
0
0
-0
0.14
-0.600
0.00
Mammalian: 30 hour Yeast: >20 hour E.coli: >10 hour
0
0.00
1
Residue Composition
number
0
A
0
R
0
N
0
D
0
C
0
E
0
Q
1
G
0
H
0
I
0
L
0
K
0
M
0
F
0
P
1
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: 1 H: 0 I: 0 L: 0 K: 0 M: 0 F: 0 P: 0 S: 1 T: 0 W: 0 Y: 0 V: 0
Chemical Descriptors
2
C5H10N2O4
162.15
6.02
-0
0.14
-0.600
162.1435
162.0638
Self-Assembly Information 1 records
Record 1 Selfassembly

Source

29933690
10.1016/j.compbiomed.2021.104391
SAPdb: A database of short peptides and the corresponding nanostructures formed by self-assembly

Self-Assembly

Nanostructure formation
Nanotube nanotubes
temperature: Room temperature solvent: chloroform and methanol
Selfassembly; Nanostructure=Nanotube; nanotubes; Trigger=temperature: Room temperature; solvent: chloroform and methanol
SEM and TEM
Selfassembly
Evidence Records 3 records
Evidence 1 Activity

Activity

IC50
ACE inhibitors
3800.00 µM
ACE inhibitor
ah

Source & Reference

NA
Cheung H.-S., Wang F.-L., Ondetti M. A., Sabo E. F., Cushman D. W.
Binding of peptide substrates and inhibitors of angiotensin-converting enzyme. J. Biol. Chem., 255, 401-407
1980
Journal

Other

2
This peptide was also identified in cuttlefish (Sepia officinalis) hydrolysate IC50=1156.30 uM Balti R., Bougatef A., Sila A., Guillochon D., Dhulster P., Nedjar-Arroume N. 2015. 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 Chemistry, 170, 519-525.
Evidence 2 Activity

Activity

IC50
Antihypertensive
3800.00 µM
ACE inhibitor
ah

Source & Reference

AHTPDB
Cheung H.-S., Wang F.-L., Ondetti M. A., Sabo E. F., Cushman D. W.
Binding of peptide substrates and inhibitors of angiotensin-converting enzyme. J. Biol. Chem., 255, 401-407
1980
Journal

Other

Source Activity Label Source Definition
Antihypertensive
AHTPDB manually curated experimentally validated antihypertensive peptide annotation.
2
This peptide was also identified in cuttlefish (Sepia officinalis) hydrolysate IC50=1156.30 uM Balti R., Bougatef A., Sila A., Guillochon D., Dhulster P., Nedjar-Arroume N. 2015. 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 Chemistry, 170, 519-525.
Evidence 3 Selfassembly

Activity

Nanostructure formation
Selfassembly Nanostructure=Nanotube nanotubes Trigger=temperature: Room temperature solvent: chloroform and methanol
Nanotube nanotubes

Source & Reference

SAPdb
10.1016/j.compbiomed.2021.104391

Other

None specified
temperature: Room temperature solvent: chloroform and methanol
SEM and TEM
29933690
SAPdb: A database of short peptides and the corresponding nanostructures formed by self-assembly
SAPdb ID NA low-detail seed row from experimentally curated self-assembly database.
Additional Detail Fields 6 fields
temperature: Room temperature solvent: chloroform and methanol
None specified
SAPdb ID NA low-detail seed row from experimentally curated self-assembly database.
2
29933690
SAPdb: A database of short peptides and the corresponding nanostructures formed by self-assembly