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MYP_023351
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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
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2D CHEMICAL STRUCTURE
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Experimental Records
RECORD: Rec_0311086 VERIFIED: YES
Provenance & Taxonomy
not reported [other]
Structure & Mods
topology not specified [Not included yet]
canonical L-amino-acid peptide [L]
None
None
Bio-Activity Profile
Antimicrobial Anticancer Cytotoxic
PMID23084276 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/23084276/
RECORD: Rec_0314861 VERIFIED: YES
Provenance & Taxonomy
not reported [other]
Structure & Mods
cyclic peptide [Cyclic]
canonical L-amino-acid peptide [L]
None
None
Bio-Activity Profile
Antimicrobial Antibacterial Antifungal Anticancer Antiviral Antiparasitic Antiplasmodial
PaperParaPep: a web resource for experimentally validated antiparasitic peptide sequences and their structures PMID24923818 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/24923818/
RECORD: Rec_0328723 VERIFIED: NO
Provenance & Taxonomy
not reported [other]
ACE-inhibitory peptide
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Antihypertensive ACE inhibitory
ACE
4.28 pIC50
pIC50
PaperQSAR study on angiotensin-converting enzyme inhibitor oligopeptides based on a novel set of sequence information descriptors. PMID20941517 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/20941517/
RECORD: Rec_0329066 VERIFIED: YES
Provenance & Taxonomy
not reported [other]
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Calpain 1 Inhibitor
PaperIqbal M., Messina P. A., Freed B., Das M., Chatterjee S., Tripathy R., Tao M., Josef K. A., Dembofsky B., Dunn D., Griffith E., Siman R., Senadhi S. E., Biazzo W., Bozyczko-Coyne D., Meyer S. L., Ator M. A., Bihovsky R.. Subsite requirements for peptide aldehyde inhibitors of human calpain I. Bioorg. Med. Chem. Lett., 7, 539-544, 1997.
RECORD: Rec_0331756 VERIFIED: YES
Provenance & Taxonomy
synthetic construct [Synthetic]
32630.0
Structure & Mods
linear peptide [Linear]
noncanonical stereochemical modification [Modified]
noncanonical token !OC4:0
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/
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