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Peptide record

TPDB26087

ACE inhibitor dipeptidyl peptidase IV inhibitor (DPP IV inhibitor) NH2-Val-Phe-COOH ACE inhibitors Antibacterial Anticancer Antifungal Antihypertensive Antiparasitic Antiviral Bitter Neuropeptide iDPPIV Selfassembly standard
2 amino acids
Basic Information
3D PDB MODEL
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TPDB26087
ACE inhibitor dipeptidyl peptidase IV inhibitor (DPP IV inhibitor) NH2-Val-Phe-COOH
ACE inhibitors Antibacterial Anticancer Antifungal Antihypertensive Antiparasitic Antiviral Bitter Neuropeptide iDPPIV Selfassembly
Anti-infective peptides Cardiometabolic peptides Cancer-related peptides Neuroactive peptides Food sensory peptides Self-assembling and biomaterial peptides
FermFooDB Peptipedia SATPdb CAFPdb AHTPDB AHTpin Tastepeptides-Meta iDPPIV SAPdb
standard
No
A 2-aa standard natural multi-activity (ACE inhibitors, Antibacterial, Anticancer, and other sources) peptide sequence curated from FermFooDB, Peptipedia, SATPdb, and other sources, with an available 3D structural model.
Sequence
VF
Physicochemical Analysis
C14H20N2O3
ARNDCEQGHILKMPSTWY
FV
264.32
6.02
0
0
2
-0
-1.06
3.500
145.00
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
0
I
0
L
0
K
0
M
1
F
0
P
0
S
0
T
0
W
0
Y
1
V
Amino Acid Distribution
A: 0 R: 0 N: 0 D: 0 C: 0 E: 0 Q: 0 G: 0 H: 0 I: 0 L: 0 K: 0 M: 0 F: 1 P: 0 S: 0 T: 0 W: 0 Y: 0 V: 1
Chemical Descriptors
2
C14H20N2O3
264.32
6.02
-0
-1.06
3.500
264.3194
264.1469
Self-Assembly Information 1 records
Record 1 Selfassembly

Source

17172307
10.1016/j.compbiomed.2021.104391
SAPdb: A database of short peptides and the corresponding nanostructures formed by self-assembly

Self-Assembly

Nanostructure formation
Nanofiber Nanofibrils
pH: 5.8 temperature: Room temperature solvent: Aqueous dispersion concentration: 2% (w/v)
Selfassembly; Nanostructure=Nanofiber; Nanofibrils; Trigger=pH: 5.8; temperature: Room temperature; solvent: Aqueous dispersion; concentration: 2% (w/v)
Transmission Electron Microscopy (TEM), Scanning Electron Microscopy (SEM)
Selfassembly
Evidence Records 4 records
Evidence 1 Activity

Activity

IC50
ACE inhibitors
9.20 µM
Inhibitor of Angiotensin-Converting Enzyme (ACE) (EC 3.4.15.1) (MEROPS ID: M02-001)
ACE inhibitor
ah

Source & Reference

FermFooDB
Matsufuji H., Matsui T., Seki E., Osajima K., Nakashima M., Osajima Y.
Angiotensin I-converting enzyme inhibitory peptides in an alkaline proteinase hydrolysate derived from sardine muscle. Biosci. Biotech. Biochem., 58, 2244-2245, 1994
1994
Journal

Other

2
BIOPEP-UWM database of bioactive peptides SMILES: N[C@H](C(=O)N[C@H](C(=O)O)Cc1ccccc1)C(C)C InChI=1S/C14H20N2O3/c1-9(2)12(15)13(17)16-11(14(18)19)8-10-6-4-3-5-7-10/h3-7,9,11-12H,8,15H2,1-2H3,(H,16,17)(H,18,19)/t11-,12-/m0/s1 InChIKey: GJNDXQBALKCYSZ-RYUDHWBXSA-N Information concerning Angiotensin-Converting Enzyme (ACE) is available in MEROPS database of proteolytic enzymes (http://merops.sanger.ac.uk/) ID: XM02-001 Another value of peptide IC50(EC50)=53 uM Cushman D. W., 1981. Angiotensin converting enzyme inhibitors: Evolution of a new class of antihypertensive drugs (page 19). in: Horovitz Z. P. (Ed.)(1981), Mechanisms of action and clinical implications, Urban & Schwarzenberg. Peptide found also in amaranth protein hydrolysate. Barba de la Rosa A. P., Barba Montoya A., Martínez-Cuevas P., Hernández-Ledesma B., León-Galván M. F., De León-Rodríguez A., González C., 2010, Tryptic amaranth glutelin digests induce endothelial nitric oxide production through inhibition of ACE: antihypertensive role of amaranth peptides. Nitric Oxide, 23, 106-111 Inhibitor of Calpain 1 (EC 3.4.22.52) (MEROPS ID: C02.001) according to the BIOPEP-UWM database of bioactive peptides the ChEMBL database the PubChem database Inhibitor of Tripeptidyl peptidase 2 (EC 3.4.14.10) (MEROPS ID S08.090) according to the BIOPEP-UWM database of bioactive peptides the BRENDA database the ChEMBL database the PubChem database Inhibitor of Neprilysin-2 (EC 3.4.24.B14) (MEROPS ID: M13.008) according to the BIOPEP-UWM database of bioactive peptides the BRENDA database Inhibitor of Dipeptidyl Peptidase IV (EC 3.4.14.5) (MEROPS ID: S09.003) according to the BIOPEP-UWM database of bioactive peptides (ID 8917) Antiviral peptide according to the BIOPEP-UWM database of bioactive peptides the ChEMBL database Bitter peptide according to the BIOPEP-UWM database of sensory peptides and amino acids (ID 51)
Evidence 2 Activity

Activity

IC50
Antihypertensive
9.20 µM
Inhibitor of Angiotensin-Converting Enzyme (ACE) (EC 3.4.15.1) (MEROPS ID: M02-001)
ACE inhibitor
ah

Source & Reference

AHTPDB FermFooDB
Matsufuji H., Matsui T., Seki E., Osajima K., Nakashima M., Osajima Y.
Angiotensin I-converting enzyme inhibitory peptides in an alkaline proteinase hydrolysate derived from sardine muscle. Biosci. Biotech. Biochem., 58, 2244-2245, 1994
1994
Journal

Other

Source Activity Label Source Definition
Antihypertensive
AHTPDB manually curated experimentally validated antihypertensive peptide annotation.
2
BIOPEP-UWM database of bioactive peptides SMILES: N[C@H](C(=O)N[C@H](C(=O)O)Cc1ccccc1)C(C)C InChI=1S/C14H20N2O3/c1-9(2)12(15)13(17)16-11(14(18)19)8-10-6-4-3-5-7-10/h3-7,9,11-12H,8,15H2,1-2H3,(H,16,17)(H,18,19)/t11-,12-/m0/s1 InChIKey: GJNDXQBALKCYSZ-RYUDHWBXSA-N Information concerning Angiotensin-Converting Enzyme (ACE) is available in MEROPS database of proteolytic enzymes (http://merops.sanger.ac.uk/) ID: XM02-001 Another value of peptide IC50(EC50)=53 uM Cushman D. W., 1981. Angiotensin converting enzyme inhibitors: Evolution of a new class of antihypertensive drugs (page 19). in: Horovitz Z. P. (Ed.)(1981), Mechanisms of action and clinical implications, Urban & Schwarzenberg. Peptide found also in amaranth protein hydrolysate. Barba de la Rosa A. P., Barba Montoya A., Martínez-Cuevas P., Hernández-Ledesma B., León-Galván M. F., De León-Rodríguez A., González C., 2010, Tryptic amaranth glutelin digests induce endothelial nitric oxide production through inhibition of ACE: antihypertensive role of amaranth peptides. Nitric Oxide, 23, 106-111 Inhibitor of Calpain 1 (EC 3.4.22.52) (MEROPS ID: C02.001) according to the BIOPEP-UWM database of bioactive peptides the ChEMBL database the PubChem database Inhibitor of Tripeptidyl peptidase 2 (EC 3.4.14.10) (MEROPS ID S08.090) according to the BIOPEP-UWM database of bioactive peptides the BRENDA database the ChEMBL database the PubChem database Inhibitor of Neprilysin-2 (EC 3.4.24.B14) (MEROPS ID: M13.008) according to the BIOPEP-UWM database of bioactive peptides the BRENDA database Inhibitor of Dipeptidyl Peptidase IV (EC 3.4.14.5) (MEROPS ID: S09.003) according to the BIOPEP-UWM database of bioactive peptides (ID 8917) Antiviral peptide according to the BIOPEP-UWM database of bioactive peptides the ChEMBL database Bitter peptide according to the BIOPEP-UWM database of sensory peptides and amino acids (ID 51)
Evidence 3 Activity

Activity

IC50
iDPPIV
0.00 µM
Inhibitor of Dipeptidyl Peptidase IV (EC 3.4.14.5) (MEROPS ID: S09.003)
dipeptidyl peptidase IV inhibitor
dpp

Source & Reference

iDPPIV
Lan V. T. T., Ito K., Ohno M., Motoyama T., Ito S., Kawarasaki Y.
Analyzing a dipeptide library to identify human dipeptidyl peptidase IV inhibitor. Food Chemistry 175, 66-73
2015
Journal

Other

2
BIOPEP-UWM database of sensory peptides and amino acids SMILES: N[C@H](C(=O)N[C@H](C(=O)O)Cc1ccccc1)C(C)C InChI=1S/C14H20N2O3/c1-9(2)12(15)13(17)16-11(14(18)19)8-10-6-4-3-5-7-10/h3-7,9,11-12H,8,15H2,1-2H3,(H,16,17)(H,18,19)/t11-,12-/m0/s1 InChIKey: GJNDXQBALKCYSZ-RYUDHWBXSA-N Peptide found in hydrolysate of sardine muscle proteins. Matsufuji H., Matsui T., Seki E., Osajima K., Nakashima M., Osajima Y., 1994, Angiotensin I-converting enzyme inhibitory peptides in an alkaline proteinase hydrolysate derived from sardine muscle. Biosci. Biotech. Biochem., 58, 2244-2245 Peptide found in amaranth protein hydrolysate. Barba de la Rosa A. P., Barba Montoya A., Martínez-Cuevas P., Hernández-Ledesma B., León-Galván M. F., De León-Rodríguez A., González C., 2010, Tryptic amaranth glutelin digests induce endothelial nitric oxide production through inhibition of ACE: antihypertensive role of amaranth peptides. Nitric Oxide, 23, 106-111 Inhibitor of Angiotensin-Converting Enzyme (ACE) (EC 3.4.15.1) (MEROPS ID: M02-001) according to the AHTPDB database the BIOPEP-UWM database of bioactive peptides (ID 3384) the ChEMBL database the EROP-Moscow database (ID E01330) the PubChem database Inhibitor of Calpain 1 (EC 3.4.22.52) (MEROPS ID: C02.001) according to the BIOPEP-UWM database of bioactive peptides (ID 9918) the ChEMBL database the PubChem database Inhibitor of Tripeptidyl peptidase 2 (EC 3.4.14.10) (MEROPS ID S08.090) according to the BRENDA database the ChEMBL database the PubChem database Inhibitor of Neprilysin-2 (EC 3.4.24.B14) (MEROPS ID: M13.008) according to the BRENDA database Antiviral peptide according to the BIOPEP-UWM database of bioactive peptides the ChEMBL database Bitter peptide according to the BIOPEP-UWM database of sensory peptides and amino acids (ID 51)
Evidence 4 Selfassembly

Activity

Nanostructure formation
Selfassembly Nanostructure=Nanofiber Nanofibrils Trigger=pH: 5.8 temperature: Room temperature solvent: Aqueous dispersion concentration: 2% (w/v)
Nanofiber Nanofibrils

Source & Reference

SAPdb
10.1016/j.compbiomed.2021.104391

Other

None specified
pH: 5.8 temperature: Room temperature solvent: Aqueous dispersion concentration: 2% (w/v)
Transmission Electron Microscopy (TEM), Scanning Electron Microscopy (SEM)
17172307
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
pH: 5.8 temperature: Room temperature solvent: Aqueous dispersion concentration: 2% (w/v)
None specified
SAPdb ID NA low-detail seed row from experimentally curated self-assembly database.
2
17172307
SAPdb: A database of short peptides and the corresponding nanostructures formed by self-assembly