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MYP_123663
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Basic Information
Unnamed
Cardiovascular ▸ Blood pressure regulation ▸ Antihypertensive
Enzyme modulation ▸ Enzyme inhibition ▸ DPP-IV inhibition ▸ DPP-IV inhibitory
Enzyme modulation ▸ Enzyme inhibition ▸ Tripeptidyl Peptidase II Inhibitory
Metabolic ▸ Glucose metabolism ▸ Antidiabetic
Other / Curated residual function label ▸ Generic enzyme inhibition annotation
Sensory / Food function ▸ Taste-active peptide
Sensory / Food function ▸ Taste-active peptide ▸ Bitter peptide
Standard
2 amino acids
C8H16N2O3
Standard
Sequence
VA
Physicochemical Analysis
188.22 Da
5.50
-0.27
-0.48
-0.1330
3.00
0.57
0.85
5.00
195.00
0.0000
0.00
0.00
The radar chart summarizes major physicochemical dimensions for quick comparison, while exact numerical values remain listed on the left.
Residue Composition
Amino Acid Composition
Chemical Descriptors
92.42
-0.44
3.0
3.0
4.0
13.0
0.0
1.0
Structural Visualization
3D PDB MODEL
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2D CHEMICAL STRUCTURE
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Experimental Records
RECORD: Rec_0020392 VERIFIED: YES
Provenance & Taxonomy
synthetic construct [Synthetic]
32630.0
Structure & Mods
linear peptide [Linear]
noncanonical stereochemical modification [Modified]
noncanonical token A[3!cC6:0]
Bio-Activity Profile
Tripeptidyl Peptidase II Inhibitory
Tripeptidyl peptidase II / CCK-8-inactivating peptidase
PaperGanellin C. R., Bishop P. B., Bambal R. B., Chan S. M., Law J. K., Marabout B., Luthra P. M., Moore A. N., Peschard O., Bourgeat P., Rose C., Vargas F. Inhibitors of tripeptidyl peptidase II. 2. Generation of the first novel lead inhibitor of cholecystokinin-8-inactivating peptidase: a strategy for the design of peptidase inhibitors. J. Med. Chem., 43, 664-674, 2000. PMID10691692 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/10691692/
RECORD: Rec_0020703 VERIFIED: YES
Provenance & Taxonomy
synthetic construct [Synthetic]
Model sensory peptide
32630
Structure & Mods
linear contiguous peptide sequence [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Bitter
168.24 μM
EC50
PaperQuantitative structure-activity relationships of the bitter thresholds of amino acids, peptides, and their derivatives. J. Med. Chem., 1987, 30, 1873-1879
RECORD: Rec_0081059 VERIFIED: YES
Provenance & Taxonomy
Homo sapiens [Animal]
Lactoferrin-derived
9606
Structure & Mods
synthetic linear peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
DPP-IV inhibitory Antidiabetic
Dipeptidyl peptidase-IV (DPP-IV)
168.2 μM
IC50
PaperIdentification of short peptide sequences in the nanofiltration permeate of a bioactive whey protein hydrolysate | Le Maux, S. et al. | DOI: 10.1016/j.foodres.2015.09.012 Evidence URLhttps://www.uniprot.org/uniprotkb/P02788/entry
RECORD: Rec_0088884 VERIFIED: YES
Provenance & Taxonomy
synthetic construct [Synthetic]
32630.0
Structure & Mods
linear peptide [Linear]
noncanonical stereochemical modification [Modified]
noncanonical token A[3!cC6:0]; noncanonical token ~!C4:0
Bio-Activity Profile
Tripeptidyl Peptidase II Inhibitory
Tripeptidyl peptidase II / CCK-8-inactivating peptidase
PaperGanellin C. R., Bishop P. B., Bambal R. B., Chan S. M., Law J. K., Marabout B., Luthra P. M., Moore A. N., Peschard O., Bourgeat P., Rose C., Vargas F. Inhibitors of tripeptidyl peptidase II. 2. Generation of the first novel lead inhibitor of cholecystokinin-8-inactivating peptidase: a strategy for the design of peptidase inhibitors. J. Med. Chem., 43, 664-674, 2000. PMID10691692 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/10691692/
RECORD: Rec_0172608 VERIFIED: YES
Provenance & Taxonomy
not reported [other]
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Antidiabetic DPP-IV Inhibitory
Dipeptidyl peptidase IV
168.24
IC50
PaperNongonierma A. B., Mooney C., Shields D. C., FitzGerald R. J.. Inhibition of dipeptidyl peptidase IV and xanthine oxidase by amino acids and dipeptides. Food Chemistry, 141, 644-653.
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