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Peptide record

TPDB01216

ACE inhibitor oligopeptide Renin inhibitor ACE inhibitors Antihypertensive Antioxidant Antiparasitic Bitter Neuropeptide iDPPIV Selfassembly standard
2 amino acids
Basic Information
3D PDB MODEL
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TPDB01216
ACE inhibitor oligopeptide Renin inhibitor
ACE inhibitors Antihypertensive Antioxidant Antiparasitic Bitter Neuropeptide iDPPIV Selfassembly
Anti-infective peptides Cardiometabolic peptides Neuroactive peptides Food sensory peptides Functional / health-promoting peptides Self-assembling and biomaterial peptides
Peptipedia AHTPDB AHTpin AnOxPePred - 1.0 AODB Multi-AOP Tastepeptides-Meta iDPPIV SAPdb
standard
No
A 2-aa standard natural multi-activity (ACE inhibitors, Antihypertensive, Antioxidant, and other sources) peptide sequence curated from Peptipedia, AHTPDB, AHTpin, and other sources, with an available 3D structural model.
Sequence
LY
Physicochemical Analysis
C15H22N2O4
ARNDCEQGHIKMFPSTWV
LY
294.35
5.94
0
0
2
-0
-1.50
1.250
195.00
Mammalian: 5.5 hour Yeast: 3 min E.coli: 2 min
1490
506.20
1
Residue Composition
number
0
A
0
R
0
N
0
D
0
C
0
E
0
Q
0
G
0
H
0
I
1
L
0
K
0
M
0
F
0
P
0
S
0
T
0
W
1
Y
0
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: 1 K: 0 M: 0 F: 0 P: 0 S: 0 T: 0 W: 0 Y: 1 V: 0
Chemical Descriptors
2
C15H22N2O4
294.35
5.94
-0
-1.50
1.250
294.3453
294.1574
Self-Assembly Information 1 records
Record 1 Selfassembly

Source

30892363
10.1016/j.compbiomed.2021.104391
SAPdb: A database of short peptides and the corresponding nanostructures formed by self-assembly

Self-Assembly

Nanostructure formation
supramolecular complexes
pH: 7 temperature: Room temperature solvent: sodium pHospHate buffer concentration: 10mM
Selfassembly; Nanostructure=supramolecular complexes; Trigger=pH: 7; temperature: Room temperature; solvent: sodium pHospHate buffer; concentration: 10mM
Selfassembly
Evidence Records 5 records
Evidence 1 Activity

Activity

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

Source & Reference

NA
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: [H][C@](N)(CC(C)C)C(=O)N[C@@]([H])(Cc1ccc(O)cc1)C(O)=O InChI=1S/C15H22N2O4/c1-9(2)7-12(16)14(19)17-13(15(20)21)8-10-3-5-11(18)6-4-10/h3-6,9,12-13,18H,7-8,16H2,1-2H3,(H,17,19)(H,20,21)/t12-,13-/m0/s1 InChIKey=LHSGPCFBGJHPCY-STQMWFEESA-N Information concerning Angiotensin-Converting Enzyme (ACE) is available in MEROPS database of proteolytic enzymes (http://merops.sanger.ac.uk/) ID: M02-001 Peptide was obtained from the following resources: soybean protein hydrolysate Beermann C., Euler M., Herzberg J., Stahl B., 2009, Anti-oxidative capacity of enzymatically released peptides from soybean protein isolate. Eur. Food Res. Technol., 229, 637–644 amaranth proteins: 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 bovine collagen hydrolysate: Herregods G., Van Camp J., Morel N., Ghesquière B., Gevaert K., Vercruysse L., Dierckx S., Quanten E., Smagghe G., 2011, Angiotensin I-converting enzyme inhibitory activity of gelatin hydrolysates and identification of bioactive peptides. J. Agric. Food Chem., 59, 552-558 Peptide reveals antihypertensive activity in vivo in spontaneously hypertensive rats: He R., Yang Y.-J., Wang Z., Xing C., Yuan J., Wang L.-F., Udenigwe C., Ju X.-R., 2019, Rapeseed protein-derived peptides, LY, RALP, and GHS, modulates key enzymes and intermediate products of renin–angiotensin system pathway in spontaneously hypertensive rat. Sci. Food, 3, 1 Antioxidative peptide according to the BIOPEP-UWM database of bioactive peptides (ID 7872) Inhibitor of Renin (EC 3.4.23.15) (MEROPS ID A01.007) according to the BIOPEP-UWM database of bioactive peptides (ID 9470) Bitter peptide according to the BIOPEP-UWM database of sensory peptides and amino acids (ID 482)
Evidence 2 Activity

Activity

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

Source & Reference

AHTPDB
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: [H][C@](N)(CC(C)C)C(=O)N[C@@]([H])(Cc1ccc(O)cc1)C(O)=O InChI=1S/C15H22N2O4/c1-9(2)7-12(16)14(19)17-13(15(20)21)8-10-3-5-11(18)6-4-10/h3-6,9,12-13,18H,7-8,16H2,1-2H3,(H,17,19)(H,20,21)/t12-,13-/m0/s1 InChIKey=LHSGPCFBGJHPCY-STQMWFEESA-N Information concerning Angiotensin-Converting Enzyme (ACE) is available in MEROPS database of proteolytic enzymes (http://merops.sanger.ac.uk/) ID: M02-001 Peptide was obtained from the following resources: soybean protein hydrolysate Beermann C., Euler M., Herzberg J., Stahl B., 2009, Anti-oxidative capacity of enzymatically released peptides from soybean protein isolate. Eur. Food Res. Technol., 229, 637–644 amaranth proteins: 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 bovine collagen hydrolysate: Herregods G., Van Camp J., Morel N., Ghesquière B., Gevaert K., Vercruysse L., Dierckx S., Quanten E., Smagghe G., 2011, Angiotensin I-converting enzyme inhibitory activity of gelatin hydrolysates and identification of bioactive peptides. J. Agric. Food Chem., 59, 552-558 Peptide reveals antihypertensive activity in vivo in spontaneously hypertensive rats: He R., Yang Y.-J., Wang Z., Xing C., Yuan J., Wang L.-F., Udenigwe C., Ju X.-R., 2019, Rapeseed protein-derived peptides, LY, RALP, and GHS, modulates key enzymes and intermediate products of renin–angiotensin system pathway in spontaneously hypertensive rat. Sci. Food, 3, 1 Antioxidative peptide according to the BIOPEP-UWM database of bioactive peptides (ID 7872) Inhibitor of Renin (EC 3.4.23.15) (MEROPS ID A01.007) according to the BIOPEP-UWM database of bioactive peptides (ID 9470) Bitter peptide according to the BIOPEP-UWM database of sensory peptides and amino acids (ID 482)
Evidence 3 Activity

Activity

IC50
Antihypertensive
1870.00 µM
Inhibitor of Renin (EC 3.4.23.15) (MEROPS ID A01.007)
renin inhibitor
ren

Source & Reference

AHTPDB
He R., Malomo S. A., Alashi A., Girgih A. T., Ju X., Aluko R. E.
Purification and hypotensive activity of rapeseed protein derived renin and angiotensin converting enzyme inhibitory peptides. J. Funct. Foods, 5, 781-789, 2013
2013
Journal

Other

2
BIOPEP-UWM database of bioactive peptides SMILES: [H][C@](N)(CC(C)C)C(=O)N[C@@]([H])(Cc1ccc(O)cc1)C(O)=O InChI=1S/C15H22N2O4/c1-9(2)7-12(16)14(19)17-13(15(20)21)8-10-3-5-11(18)6-4-10/h3-6,9,12-13,18H,7-8,16H2,1-2H3,(H,17,19)(H,20,21)/t12-,13-/m0/s1 InChIKey=LHSGPCFBGJHPCY-STQMWFEESA-N Peptide was obtained from the following resources: soybean protein hydrolysate Beermann C., Euler M., Herzberg J., Stahl B., 2009, Anti-oxidative capacity of enzymatically released peptides from soybean protein isolate. Eur. Food Res. Technol., 229, 637–644 amaranth proteins: 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 bovine collagen hydrolysate: Herregods G., Van Camp J., Morel N., Ghesquière B., Gevaert K., Vercruysse L., Dierckx S., Quanten E., Smagghe G., 2011, Angiotensin I-converting enzyme inhibitory activity of gelatin hydrolysates and identification of bioactive peptides. J. Agric. Food Chem., 59, 552-558 Peptide reveals antihypertensive activity in vio in spontaneously hypertensive rats: He R., Yang Y.-J., Wang Z., Xing C., Yuan J., Wang L.-F., Udenigwe C., Ju X.-R., 2019, Rapeseed protein-derived peptides, LY, RALP, and GHS, modulates key enzymes and intermediate products of renin–angiotensin system pathway in spontaneously hypertensive rat. Sci. Food, 3, 1 Antioxidative peptide according to the BIOPEP-UWM database of bioactive peptides (ID 7872) Inhibitor of Angiotensin-Converting Enzyme (ACE) (EC 3.4.15.1) (MEROPS ID: M02-001) according to the AHTPDB database the BindingDB database the BIOPEP-UWM database of bioactive peptids (ID 3381) the BRENDA database the ChEMBL database the EROP-Moscow database the PubChem database Bitter peptide according to the BIOPEP-UWM database of sensory peptides and amino acids (ID 482)
Evidence 4 Activity

Activity

Antioxidative activity
Antioxidant

Source & Reference

AODB
DFBP
Evidence 5 Selfassembly

Activity

Nanostructure formation
Selfassembly Nanostructure=supramolecular complexes Trigger=pH: 7 temperature: Room temperature solvent: sodium pHospHate buffer concentration: 10mM
supramolecular complexes

Source & Reference

SAPdb
10.1016/j.compbiomed.2021.104391

Other

None specified
pH: 7 temperature: Room temperature solvent: sodium pHospHate buffer concentration: 10mM
30892363
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: 7 temperature: Room temperature solvent: sodium pHospHate buffer concentration: 10mM
None specified
SAPdb ID NA low-detail seed row from experimentally curated self-assembly database.
2
30892363
SAPdb: A database of short peptides and the corresponding nanostructures formed by self-assembly