Inhibition of human immunodeficiency virus type-1 reverse transcriptase by a novel peptide derived from the viral integrase

Iris Oz Gleenberg, Alon Herschhorn, Yehuda Goldgur, Amnon Hizi

Research output: Contribution to journalArticle

15 Scopus citations

Abstract

Previous studies show that the reverse transcriptase (RT) of human immunodeficiency virus type-1 (HIV-1) and RT-derived peptides interact with and inhibit the viral integrase (IN). In the present study, we have performed the complementary study by screening a complete library of HIV-1 IN-derived peptides for their effects on the RT. We have identified a 20-residues long peptide, derived from the IN (residues 46-65) that binds the RT and inhibits its DNA-polymerase activities (without affecting the ribonuclease-H activity). The full 20-residues sequence is required for maximal inhibition. This inhibition is non-competitive and probably results from obstructing the formation of RT-DNA complexes by the peptide. The data and the molecular docking model presented suggest that this inhibition is probably caused by a steric hindrance or conformational changes of the RT. These results can facilitate the development of novel and specific peptide-based HIV-1 RT inhibitors that might help in the fight against AIDS.

Original languageEnglish (US)
Pages (from-to)202-212
Number of pages11
JournalArchives of Biochemistry and Biophysics
Volume458
Issue number2
DOIs
StatePublished - Feb 15 2007

Keywords

  • DNA-polymerase
  • HIV-1
  • Inhibition
  • Integrase
  • Modeling
  • Peptides
  • Reverse transcriptase

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