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MYP_002472
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Basic Information
Unnamed
Anticancer
Anticancer ▸ Cytotoxic anticancer activity ▸ Cytotoxic
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 ▸ 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_0280734 VERIFIED: YES
Provenance & Taxonomy
synthetic construct [Synthetic]
32630.0
Structure & Mods
linear peptide [Linear]
noncanonical stereochemical modification [Modified]
Nva
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_0297854 VERIFIED: YES
Provenance & Taxonomy
not reported [other]
coronatine
Structure & Mods
linear peptide [Linear]
noncanonical stereochemical modification [Modified]
Non-proteinogenic/modified monomers: CFA
Bio-Activity Profile
Toxin
RECORD: Rec_0305788 VERIFIED: YES
Provenance & Taxonomy
synthetic construct [Synthetic]
32630.0
Structure & Mods
linear peptide [Linear]
noncanonical stereochemical modification [Modified]
Aromatic acylation
noncanonical token [ph]C1!; Nva
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_0305955 VERIFIED: YES
Provenance & Taxonomy
synthetic construct [Synthetic]
32630.0
Structure & Mods
linear peptide [Linear]
noncanonical stereochemical modification [Modified]
Nle; noncanonical token ~!C3:0[3ph]
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_0324427 VERIFIED: YES
Provenance & Taxonomy
not reported [other]
Structure & Mods
cyclic peptide; DSSP H 0.0%, E 0.0%, T 0.0%, C 100.0% [Cyclic]
D-residue-containing modified peptide [Mixed]
None
None
Z=D-Ornithine
Bio-Activity Profile
Anticancer Antibacterial Antiviral Antiparasitic Antimicrobial Antifungal Antiplasmodial
PaperParaPep: a web resource for experimentally validated antiparasitic peptide sequences and their structures PMID24923818 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/24923818/
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