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MYP_018608
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Basic Information
NL9-3
Antimicrobial
Antiviral
Antiviral ▸ Anti-HIV ▸ Anti-HIV-1
Antiviral ▸ Antiviral mechanism ▸ Viral replication inhibition
Enzyme modulation ▸ Enzyme inhibition ▸ Integrase inhibition
Standard
11 amino acids
C55H80N14O15S
Standard
Sequence
ACWGAGIKQEF
Physicochemical Analysis
1209.37 Da
6.04
-0.21
-0.42
-0.0193
0.07
0.24
0.25
76.98
53.64
0.1818
5500.00
5500.00
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
476.52
-3.25
17.0
16.0
38.0
85.0
3.0
11.0
Structural Visualization
3D PDB MODEL
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2D CHEMICAL STRUCTURE
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Experimental Records
RECORD: Rec_0077262 VERIFIED: YES
Provenance & Taxonomy
synthetic construct [Synthetic]
Protein-derived synthetic peptide
32630
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
None
Amidation
Bio-Activity Profile
Antiviral Anti-HIV-1 Replication inhibition
HIV-1
333 μM
IC50
Mammalian: 4.4 h; Yeast: >20 h; E. coli: >10 h
PaperSequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. | Li HY, Zawahir Z, Song LD, Long YQ, Neamati N. | J Med Chem. 2006 Jul 27;49(15):4477-86. | DOI:10.1021/jm060307u | PMID:16854053 PMID16854053 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/16854053/
RECORD: Rec_0093984 VERIFIED: YES
Provenance & Taxonomy
not reported [other]
Structure & Mods
linear peptide; DSSP H 0.0%, E 0.0%, T 36.4%, C 63.6% [Linear]
canonical L-amino-acid peptide [L]
None
None
Bio-Activity Profile
Antiviral Antimicrobial
PaperHIPdb: a database of experimentally validated HIV inhibiting peptides PMID23359817 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/23359817/
RECORD: Rec_0153892 VERIFIED: YES
Provenance & Taxonomy
synthetic construct [Synthetic]
Protein-derived synthetic peptide
32630
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
None
Amidation
Bio-Activity Profile
Antiviral Replication inhibition
inhibition of strand transfer catalyzed by integrase
333 μM
IC50
Mammalian: 4.4 h; Yeast: >20 h; E. coli: >10 h
PaperSequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. | Li HY, Zawahir Z, Song LD, Long YQ, Neamati N. | J Med Chem. 2006 Jul 27;49(15):4477-86. | DOI:10.1021/jm060307u | PMID:16854053 PMID16854053 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/16854053/
RECORD: Rec_0173689 VERIFIED: YES
Provenance & Taxonomy
synthetic construct [Synthetic]
32630
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
None
Amidation
Bio-Activity Profile
Antimicrobial Antiviral
inhibition of strand transfer catalyzed by integrase
333 μM
IC50
PaperSequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme PMID16854053 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/16854053/
RECORD: Rec_0266343 VERIFIED: YES
Provenance & Taxonomy
synthetic construct [Synthetic]
32630
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Antiviral Integrase inhibition
>333 μM
IC50
PaperSequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. PMID16854053 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/16854053/
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