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MYP_171060
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Basic Information
NQW (L)
Antimicrobial
Antiviral
Antiviral ▸ Anti-Hepatitis virus ▸ Anti-HCV
Antiviral ▸ Antiviral mechanism ▸ Viral replication inhibition ▸ Replication inhibitor
Standard
13 amino acids
C66H88N18O16S2
Standard
Sequence
ACFPWGNQWCGGK
Physicochemical Analysis
1453.65 Da
8.10
0.78
0.56
0.0596
-0.45
0.20
0.19
38.28
7.69
0.2308
11000.00
11125.00
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
547.51
-4.54
20.0
19.0
41.0
102.0
6.0
14.0
Structural Visualization
3D PDB MODEL
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2D CHEMICAL STRUCTURE
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Experimental Records
RECORD: Rec_0118490 VERIFIED: YES
Provenance & Taxonomy
synthetic construct [Synthetic]
32630
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
None
None
Bio-Activity Profile
Antimicrobial Antiviral
PaperPubMed PMID: 12951030 PMID12951030 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/12951030/
RECORD: Rec_0124809 VERIFIED: YES
Provenance & Taxonomy
synthetic construct [Synthetic]
Library-derived peptide
32630
Structure & Mods
synthetic linear peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Antiviral Replication inhibitor
Hepatitis C virus (RdRp); Huh7
37 μM
Surface plasmon resonance
PaperIdentification of constrained peptides that bind to and preferentially inhibit the activity of the hepatitis C viral RNA-dependent RNA polymerase. | Amin A, Zaccardi J, Mullen S, Olland S, Orlowski M, Feld B, Labonte P, Mak P. | Virology. 2003 | PMID:12951030 PMID12951030 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/12951030/
RECORD: Rec_0142209 VERIFIED: YES
Provenance & Taxonomy
synthetic construct [Synthetic]
Synthetic peptide
32630
Structure & Mods
disulfide-constrained cyclic peptide [Cyclic]
canonical L-amino-acid peptide [L]
None
None
2-10
Disulfide bond between Cys2 and Cys10
Bio-Activity Profile
Antiviral Anti-HCV
Hepatitis C virus(HCV)
6 μM
IC50
Mammalian: 4.4 h; Yeast: >20 h; E. coli: >10 h
PaperIdentification of constrained peptides that bind to and preferentially inhibit the activity of the hepatitis C viral RNA-dependent RNA polymerase. | Amin A, Zaccardi J, Mullen S, Olland S, Orlowski M, Feld B, Labonte P, Mak P. | Virology. 2003 Aug 15;313(1):158-69. | DOI:10.1016/s0042-6822(03)00313-1 | PMID:12951030 PMID12951030 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/12951030/
RECORD: Rec_0209036 VERIFIED: YES
Provenance & Taxonomy
synthetic construct [Synthetic]
32630
Structure & Mods
cyclic/stapled peptide [Cyclic]
canonical L-amino-acid peptide [L]
None
None
2-10
Bio-Activity Profile
Antimicrobial Antiviral
PaperPubMed PMID: 12951030 PMID12951030 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/12951030/
RECORD: Rec_0216013 VERIFIED: YES
Provenance & Taxonomy
synthetic construct [Synthetic]
Synthetic peptide
32630
Structure & Mods
synthetic linear peptide [Linear]
canonical L-amino-acid peptide [L]
None
None
Bio-Activity Profile
Antiviral Anti-HCV
Hepatitis C virus(HCV)
37 μM
IC50
Mammalian: 4.4 h; Yeast: >20 h; E. coli: >10 h
PaperIdentification of constrained peptides that bind to and preferentially inhibit the activity of the hepatitis C viral RNA-dependent RNA polymerase. | Amin A, Zaccardi J, Mullen S, Olland S, Orlowski M, Feld B, Labonte P, Mak P. | Virology. 2003 Aug 15;313(1):158-69. | DOI:10.1016/s0042-6822(03)00313-1 | PMID:12951030 PMID12951030 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/12951030/
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