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MYP_128514
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Basic Information
4318(derived from the RNase H domain of HIV-1 RT (20-mes)),65(derived from the HIV-1 HXB2 Pol region of the viral genome)
Antimicrobial
Antiviral
Antiviral ▸ Anti-HIV
Antiviral ▸ Antiviral mechanism ▸ Viral replication inhibition
Enzyme modulation ▸ Enzyme inhibition ▸ Integrase inhibition
Standard
20 amino acids
C93H151N23O34
Standard
Sequence
LQDSGLEVNIVTDSQYALGI
Physicochemical Analysis
2135.33 Da
4.05
-3.24
-3.44
-0.1618
0.26
0.28
0.23
81.62
131.50
0.0500
1490.00
1490.00
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
938.31
-10.03
31.0
31.0
71.0
150.0
1.0
22.0
Structural Visualization
3D PDB MODEL
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2D CHEMICAL STRUCTURE
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Experimental Records
RECORD: Rec_0004578 VERIFIED: YES
Provenance & Taxonomy
synthetic construct [Synthetic]
Protein-derived synthetic peptide
32630
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
None
None
Bio-Activity Profile
Antiviral Replication inhibition
inhibition of strand transfer catalyzed by C130A integrase
20 μM
IC50
Mammalian: 5.5 h; Yeast: 3 min; E. coli: 2 min
PaperInhibition of HIV-1 integrase activity by synthetic peptides derived from the HIV-1 HXB2 Pol region of the viral genome. | Zawahir Z, Neamati N. | Bioorg Med Chem Lett. 2006 Oct 1;16(19):5199-202. | DOI:10.1016/j.bmcl.2006.07.022 | PMID:16879966 PMID16879966 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/16879966/
RECORD: Rec_0024551 VERIFIED: YES
Provenance & Taxonomy
synthetic construct [Synthetic]
Protein-derived synthetic peptide
32630
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
None
None
Bio-Activity Profile
Antiviral Replication inhibition
inhibition of strand transfer catalyzed by wild-type integrase
2±1 μM
IC50
Mammalian: 5.5 h; Yeast: 3 min; E. coli: 2 min
PaperInhibition of HIV-1 integrase activity by synthetic peptides derived from the HIV-1 HXB2 Pol region of the viral genome. | Zawahir Z, Neamati N. | Bioorg Med Chem Lett. 2006 Oct 1;16(19):5199-202. | DOI:10.1016/j.bmcl.2006.07.022 | PMID:16879966 PMID16879966 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/16879966/
RECORD: Rec_0050729 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
inhibition of strand transfer catalyzed by wild-type integrase
2±1 μM
IC50
PaperPeptides derived from the reverse transcriptase of human immunodeficiency virus type 1 as novel inhibitors of the viral integrase. J Biol Chem. 2005 Jun 10;280(23):21987-21996. doi: 10.1074/jbc.M414679200. PMID: 15790559 PMID15790559;16879966 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/15790559/
RECORD: Rec_0125169 VERIFIED: YES
Provenance & Taxonomy
synthetic construct [Synthetic]
Protein-derived synthetic peptide
32630
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
None
None
Bio-Activity Profile
Antiviral Replication inhibition
inhibition of strand transfer catalyzed by C130S integrase
4±1 μM
IC50
Mammalian: 5.5 h; Yeast: 3 min; E. coli: 2 min
PaperInhibition of HIV-1 integrase activity by synthetic peptides derived from the HIV-1 HXB2 Pol region of the viral genome. | Zawahir Z, Neamati N. | Bioorg Med Chem Lett. 2006 Oct 1;16(19):5199-202. | DOI:10.1016/j.bmcl.2006.07.022 | PMID:16879966 PMID16879966 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/16879966/
RECORD: Rec_0197578 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
C130S integrase are mutant IN
PaperPeptides derived from the reverse transcriptase of human immunodeficiency virus type 1 as novel inhibitors of the viral integrase. J Biol Chem. 2005 Jun 10;280(23):21987-21996. doi: 10.1074/jbc.M414679200. PMID: 15790559 PMID15790559;16879966 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/15790559/
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