Evaluation of triazolamers as active site inhibitors of HIV-1 protease

Bioorg Med Chem Lett. 2009 Nov 1;19(21):6023-6. doi: 10.1016/j.bmcl.2009.09.049. Epub 2009 Sep 17.

Abstract

Proteases typically recognize their peptide substrates in extended conformations. General approaches for designing protease inhibitors often consist of peptidomimetics that feature this conformation. Herein we discuss a combination of computational and experimental studies to evaluate the potential of triazole-linked beta-strand mimetics as inhibitors of HIV-1 protease activity.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Anti-HIV Agents / chemistry*
  • Anti-HIV Agents / pharmacology
  • Catalytic Domain
  • Computer Simulation
  • HIV Protease / chemistry*
  • HIV Protease / metabolism
  • HIV Protease Inhibitors / chemistry*
  • HIV Protease Inhibitors / pharmacology
  • Humans
  • Software
  • Triazoles / chemistry*
  • Triazoles / pharmacology

Substances

  • Anti-HIV Agents
  • HIV Protease Inhibitors
  • Triazoles
  • HIV Protease
  • p16 protease, Human immunodeficiency virus 1