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MYP_002472
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Basic Information
Unnamed
Anticancer
Antimicrobial
Antimicrobial ▸ Antibacterial
Antimicrobial ▸ Antifungal
Antiparasitic ▸ Antimalarial
Antiparasitic ▸ Antiprotozoal ▸ Antimalarial ▸ Anti-Plasmodium
Antiparasitic ▸ General antiparasitic ▸ Antiparasitic
Antiviral
Enzyme modulation ▸ Enzyme inhibition ▸ Tripeptidyl Peptidase II Inhibitory
Toxicity / Safety ▸ Blood cell toxicity ▸ Hemolysis ▸ Hemolytic
Toxicity / Safety ▸ Cytotoxicity ▸ Cytotoxic
Venom / Toxin ▸ General toxin ▸ Toxin
not Standard
2 amino acids
-
contains X representing unresolved or non-standard residue
Sequence
VX
Physicochemical Analysis
0.00 Da
0.00
0.00
0.00
0.00
0.00
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Residue Composition
Amino Acid Composition
Chemical Descriptors
Structural Visualization
3D PDB MODEL
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2D CHEMICAL STRUCTURE
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Experimental Records
RECORD: Rec_0336277 VERIFIED: YES
Provenance & Taxonomy
synthetic construct [Synthetic]
32630.0
Structure & Mods
linear peptide [Linear]
noncanonical stereochemical modification [Modified]
Nle; noncanonical token !OC4:0
Bio-Activity Profile
Tripeptidyl Peptidase II Inhibitory
Tripeptidyl peptidase II / CCK-8-inactivating peptidase
Fluorimetric tripeptidyl peptidase II inhibition assay
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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