‹ ›
MYP_059864
← PREVIOUS NEXT → BACK
Basic Information
CPR
Anticancer ▸ Cytotoxic anticancer activity ▸ Cytotoxic
Antimicrobial
Antiviral
Antiviral ▸ Anti-HIV ▸ Anti-HIV-1
Antiviral ▸ Antiviral mechanism ▸ Viral fusion inhibition
Toxicity / Safety ▸ Cytotoxicity ▸ Cytotoxic
Venom / Toxin ▸ General toxin ▸ Cytotoxic
Standard
7 amino acids
C43H64N10O8S
Standard
Sequence
CPFVFLR
Physicochemical Analysis
881.10 Da
8.25
0.75
0.53
0.1072
1.43
0.38
0.34
91.11
97.14
0.2857
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
291.03
0.19
11.0
10.0
24.0
62.0
3.0
6.0
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_0005159 VERIFIED: YES
Provenance & Taxonomy
synthetic construct [Synthetic]
Protein-derived synthetic peptide
32630
Structure & Mods
cyclic peptide architecture [Cyclic]
canonical L-amino-acid peptide [L]
Cyclization (N termini to C termini)
Cyclization (N termini to C termini)
Bio-Activity Profile
Antiviral Anti-HIV-1 Fusion inhibition
HIV-1 IIIB
74.07±22.84 μM
IC50
Mammalian: 1.2 h; Yeast: >20 h; E. coli: >10 h
PaperShort cyclic peptides derived from the C-terminal sequence of α1-antitrypsin exhibit significant anti-HIV-1 activity. | Jia Q, Jiang X, Yu F, Qiu J, Kang X, Cai L, Li L, Shi W, Liu S, Jiang S, Liu K. | Bioorg Med Chem Lett. 2012 Apr 1;22(7):2393-5. | DOI:10.1016/j.bmcl.2012.02.037 | PMID:22406118 PMID22406118 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/22406118/
RECORD: Rec_0206584 VERIFIED: YES
Provenance & Taxonomy
synthetic construct [Synthetic]
32630
Structure & Mods
cyclic/stapled peptide [Cyclic]
canonical L-amino-acid peptide [L]
Cyclization
Cyclization
Bio-Activity Profile
Antimicrobial Antiviral
inhibition of cell-cell fusion between H9/HIV-1IIIB cells and MT-2 cells
73.98±7.44 μM
IC50
PaperPubMed PMID: 22406118 PMID22406118 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/22406118/
RECORD: Rec_0210228 VERIFIED: YES
Provenance & Taxonomy
synthetic construct [Synthetic]
32630
Structure & Mods
cyclic/stapled peptide [Cyclic]
canonical L-amino-acid peptide [L]
Cyclization
Cyclization
Bio-Activity Profile
Antimicrobial Antiviral
HIV-1 IIIB:inhibition of virus replication
74.07±22.84 μM
IC50
PaperPubMed PMID: 22406118 PMID22406118 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/22406118/
RECORD: Rec_0261137 VERIFIED: YES
Provenance & Taxonomy
synthetic construct [Synthetic]
Protein-derived synthetic peptide
32630
Structure & Mods
cyclic peptide architecture [Cyclic]
canonical L-amino-acid peptide [L]
Cyclization (N termini to C termini)
Cyclization (N termini to C termini)
Bio-Activity Profile
Antiviral Anti-HIV-1 Fusion inhibition
inhibition of cell-cell fusion between H9/HIV-1IIIB cells and MT-2 cells
73.98±7.44 μM
IC50
Mammalian: 1.2 h; Yeast: >20 h; E. coli: >10 h
PaperShort cyclic peptides derived from the C-terminal sequence of α1-antitrypsin exhibit significant anti-HIV-1 activity. | Jia Q, Jiang X, Yu F, Qiu J, Kang X, Cai L, Li L, Shi W, Liu S, Jiang S, Liu K. | Bioorg Med Chem Lett. 2012 Apr 1;22(7):2393-5. | DOI:10.1016/j.bmcl.2012.02.037 | PMID:22406118 PMID22406118 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/22406118/
RECORD: Rec_0276298 VERIFIED: YES
Provenance & Taxonomy
synthetic construct [Synthetic]
32630
Structure & Mods
cyclic/stapled peptide [Cyclic]
canonical L-amino-acid peptide [L]
Cyclization
Cyclization
Bio-Activity Profile
Antimicrobial Antiviral Cytotoxic
MT-2 cells
200 μM
CC50
PaperPubMed PMID: 22406118 PMID22406118 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/22406118/
1 2 NEXT LAST
Showing 5 records on this page · Page 1 of 2