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

Sluis-Cremer N, Tachedjian G

  • Journal European journal of biochemistry

  • Published 13 Dec 2002

  • Volume 269

  • ISSUE 21

  • Pagination 5103-11

  • DOI 10.1046/j.1432-1033.2002.03216.x


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.