Publications & Reports

Modulation of the oligomeric structures of HIV-1 retroviral enzymes by synthetic peptides and small molecules.

Sluis-Cremer N, Tachedjian G
Department of Medicine, Division of Infectious Diseases, University of Pittsburgh, PA 15261, USA. CremerN@msx.dept-med.pitt.edu

Abstract

The efficacy of antiretroviral agents approved for the treatment of HIV-1 infection is limited by the virus’s ability to develop resistance.

As such there is an urgent need for new ways of thinking about anti-HIV drug development, and accordingly novel viral and cellular targets critical to HIV-1 replication need to be explored and exploited.

The retroviral RNA genome encodes for three enzymes essential for viral replication: HIV-1 protease (PR), HIV-1 reverse transcriptase (RT) and HIV-1 integrase (IN).

The enzymatic functioning of each of these enzymes is entirely dependent on their oligomeric structures, suggesting that inhibition of subunit-subunit assembly or modulation of their quaternary structures provide alternative targets for HIV-1 inhibition.

This review discusses the recent advances in the design and/or identification of synthetic peptides and small molecules that specifically target the subunit-subunit interfaces of these retroviral enzymes, resulting in the inactivation of their enzymatic functioning.

Publication

  • Journal: European journal of biochemistry / FEBS
  • Published: 01/11/2002
  • Volume: 269
  • Issue: 21
  • Pagination: 5103-5111

Author

Health Issue