Differential inhibition of polymerase and strand-transfer activities of HIV-1 reverse transcriptase

Bioorg Med Chem Lett. 2002 Feb 25;12(4):525-8. doi: 10.1016/s0960-894x(01)00827-7.

Abstract

A new class of inhibitors of HIV-1 reverse transcriptase obtained by the systematic structural simplification of epicatechin and epigallocatechin gallates are also shown here to inhibit DNA-strand-transfer, a process critical to the completion of the HIV-1-RT reproduction and to recombination-associated mutation of the virus. Up to 80-fold selectivity for DNA-strand-transfer inhibition over polymerase inhibition was observed for a defined subset of these agents. Such specific DNA-strand-transfer inhibitors may have important therapeutic potential.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Anti-HIV Agents / chemical synthesis*
  • Anti-HIV Agents / pharmacology
  • Catechin / analogs & derivatives*
  • Catechin / chemical synthesis
  • Catechin / pharmacology
  • DNA, Single-Stranded / antagonists & inhibitors*
  • DNA, Single-Stranded / metabolism
  • Gallic Acid / analogs & derivatives
  • Gallic Acid / chemical synthesis
  • Gallic Acid / pharmacology
  • HIV Reverse Transcriptase / antagonists & inhibitors*
  • HIV Reverse Transcriptase / metabolism
  • Humans
  • Ribonuclease H / antagonists & inhibitors*
  • Ribonuclease H / metabolism
  • Structure-Activity Relationship

Substances

  • Anti-HIV Agents
  • DNA, Single-Stranded
  • Gallic Acid
  • Catechin
  • HIV Reverse Transcriptase
  • Ribonuclease H
  • gallocatechol