‹ ›
MYP_023351
← PREVIOUS NEXT → BACK
Basic Information
Bitter peptide, cyclo[Val-Phe] or cyclo[Phe-Val]
Anticancer
Anticancer ▸ Cytotoxic anticancer activity ▸ Cytotoxic
Antimicrobial
Antimicrobial ▸ Antibacterial
Antimicrobial ▸ Antifungal
Antiparasitic ▸ Antimalarial
Antiparasitic ▸ Antiprotozoal ▸ Antimalarial ▸ Anti-Plasmodium
Antiparasitic ▸ General antiparasitic ▸ Antiparasitic
Antiviral
Cardiovascular ▸ Blood pressure regulation ▸ Antihypertensive
Enzyme modulation ▸ Enzyme inhibition ▸ ACE inhibition ▸ ACE inhibitory
Enzyme modulation ▸ Enzyme inhibition ▸ Calpain 1 Inhibitor
Enzyme modulation ▸ Enzyme inhibition ▸ DPP-IV inhibition ▸ DPP-IV inhibitory
Enzyme modulation ▸ Enzyme inhibition ▸ Neprilysin 2 Inhibitor
Enzyme modulation ▸ Enzyme inhibition ▸ Tripeptidyl Peptidase II Inhibitory
Membrane / Ion-channel modulation ▸ Calcium channel modulation ▸ Calcium channel inhibitor
Metabolic ▸ Glucose metabolism ▸ Antidiabetic
Neurological / Signaling ▸ Neuropeptide activity ▸ Neuropeptide
Other / Curated residual function label ▸ Generic enzyme inhibition annotation
Sensory / Food function ▸ Taste-active peptide
Sensory / Food function ▸ Taste-active peptide ▸ Bitter peptide
Toxicity / Safety ▸ Blood cell toxicity ▸ Hemolysis ▸ Hemolytic
Toxicity / Safety ▸ Cytotoxicity ▸ Cytotoxic
Venom / Toxin ▸ General toxin ▸ Cytotoxic
Standard
2 amino acids
C14H20N2O3
Standard
Sequence
VF
Physicochemical Analysis
264.32 Da
5.50
-0.27
-0.48
-0.1330
3.50
0.73
1.14
5.00
145.00
0.5000
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
0.78
3.0
3.0
6.0
19.0
1.0
1.0
Structural Visualization
3D PDB MODEL
Drag to rotate. Click a residue or atom to inspect it; the selected residue is highlighted in amber in the current view mode. Use the buttons to zoom.
2D CHEMICAL STRUCTURE
Drag to move
Drag to move. Use the buttons to zoom.
Experimental Records
RECORD: Rec_0105787 VERIFIED: YES
Provenance & Taxonomy
synthetic construct [Synthetic]
32630.0
Structure & Mods
topology not specified [Not included yet]
noncanonical stereochemical modification [Modified]
noncanonical token ~!C1
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_0106164 VERIFIED: NO
Provenance & Taxonomy
Gallus gallus [Animal]
ACE-inhibitory peptide
9031
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Antihypertensive
PaperAnimal and Plant Proteins as Precursors of Peptides with ACE Inhibitory Activity – An in silico Strategy of Protein Evaluation
RECORD: Rec_0113850 VERIFIED: YES
Provenance & Taxonomy
synthetic construct [Synthetic]
32630.0
Structure & Mods
linear peptide [Linear]
noncanonical stereochemical modification [Modified]
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_0114667 VERIFIED: YES
Provenance & Taxonomy
not reported [other]
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Antihypertensive ACE inhibitory
Angiotensin-converting enzyme (ACE)
9.2
IC50
PaperMatsufuji 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.
RECORD: Rec_0122630 VERIFIED: YES
Provenance & Taxonomy
synthetic construct [Synthetic]
32630.0
Structure & Mods
linear peptide [Linear]
noncanonical stereochemical modification [Modified]
noncanonical token ~!C2:0
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/
FIRST PREV 1 2 3 4 5 ... 9 NEXT LAST
Showing 5 records on this page · Page 3 of 9