Synthesis of dammarane-type triterpene derivatives and their ability to inhibit HIV and HCV proteases

Bioorg Med Chem. 2009 Apr 15;17(8):3003-10. doi: 10.1016/j.bmc.2009.03.019. Epub 2009 Mar 14.

Abstract

We synthesized dammarane-type triterpene derivatives and evaluated their ability to inhibit HIV-1 and HCV proteases to understand their structure-activity relationships. All of the mono- and di-succinyl derivatives (5a-5f) were powerful inhibitors of HIV-1 protease (IC(50)<10 microM). However, only di-succinyl (5e) and 2,3-seco-2,3-dioic acid (3b) derivatives similarly inhibited HCV protease (IC(50)<10 microM). A-nor dammarane-type triterpenes (4a and 4b, IC(50) 10.0 and 29.9 microM, respectively) inhibited HIV-1 protease moderately or strongly, but were inactive against HCV protease. All compounds that powerfully inhibited HIV-1 or HCV protease did not appreciably inhibit the general human proteases, renin and trypsin (IC(50)>1000 microM). These findings indicated that the mono-succinyl dammarane type derivatives (5a-5d) selectively inhibited HIV-1 protease and that the di-succinyl (5e, 5f) as well as 2,3-seco-2,3-dioic acid (3b) derivatives preferably inhibited both viral proteases.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Anti-HIV Agents / chemical synthesis
  • Anti-HIV Agents / isolation & purification
  • Anti-HIV Agents / pharmacology
  • HIV Protease / metabolism
  • HIV Protease Inhibitors / chemical synthesis
  • HIV Protease Inhibitors / isolation & purification
  • HIV Protease Inhibitors / pharmacology
  • HIV-1 / enzymology*
  • Hepacivirus / enzymology*
  • Hepatitis C / enzymology*
  • Humans
  • Protease Inhibitors / chemical synthesis*
  • Protease Inhibitors / isolation & purification
  • Protease Inhibitors / pharmacology*
  • Renin / metabolism
  • Structure-Activity Relationship
  • Triterpenes / chemical synthesis*
  • Triterpenes / isolation & purification
  • Triterpenes / pharmacology*
  • Trypsin / metabolism

Substances

  • Anti-HIV Agents
  • HIV Protease Inhibitors
  • Protease Inhibitors
  • Triterpenes
  • Trypsin
  • HIV Protease
  • Renin