Targeting the dimerization interface for irreversible inhibition of HIV-1 protease

Bioorg Med Chem Lett. 2000 Sep 4;10(17):1901-3. doi: 10.1016/s0960-894x(00)00369-3.

Abstract

A novel strategy was used to irreversibly inhibit HIV-1 protease. The inhibitor was designed to form a disulfide bond with Cys95, present at the dimerization interface of HIV-1 protease. The inhibitor was shown to be active against HIV-1 protease with K(inact) = 3.7 microM and V(inact) = 0.012 min(-1).

Publication types

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

MeSH terms

  • Dimerization
  • HIV Protease / chemistry*
  • HIV Protease Inhibitors / pharmacology*
  • Structure-Activity Relationship

Substances

  • HIV Protease Inhibitors
  • HIV Protease