Inhibition of HIV-1 integrase activity by synthetic peptides derived from the HIV-1 HXB2 Pol region of the viral genome.
Peptides deriving from the HIV-1 HXB2 Pol gene sequence were evaluated for inhibitory activity against wild-type (WT) and mutant HIV-1 integrase (IN). The most potent peptide corresponding to a region on the reverse transcriptase (RT) subunit of the Pol polyprotein showed IC(50) value of 5 and 2 microM for 3'-processing and strand transfer, respectively. These peptides, and their analogs, may potentially be used in the elucidation of structural and functional epitopes of IN involved in protein-protein and protein-small molecule interactions.
Zawahir
Zahrah
Z
Department of Pharmaceutical Sciences, School of Pharmacy, University of Southern California, 1985 Zonal Avenue, Los Angeles, 90089, USA.
Neamati
Nouri
N
D000595:Amino Acid Sequence; D015684:Gene Products, pol / Q000737:chemistry*; D019427:HIV Integrase / Q000737:chemistry / Q000187:drug effects* / Q000235:genetics; D019428:HIV Integrase Inhibitors / Q000138:chemical synthesis* / Q000494:pharmacology; D006801:Humans; D020128:Inhibitory Concentration 50; D009154:Mutation; D010446:Peptide Fragments / Q000138:chemical synthesis* / Q000494:pharmacology*; D013329:Structure-Activity Relationship
D015684:Gene Products, pol; D019428:HIV Integrase Inhibitors; D010446:Peptide Fragments; D019427:HIV Integrase