Non-thiol farnesyltransferase inhibitors: utilization of the far aryl binding site by arylthienylacryloylaminobenzophenones

Arch Pharm (Weinheim). 2005 Jan;338(1):9-17. doi: 10.1002/ardp.200400886.

Abstract

We recently described two novel aryl binding sites of farnesyltransferase. The 4- and 5-arylsubstituted thienylacryloyl moieties turned out as appropriate substituents for our benzophenone-based AAX-peptidomimetic capable for occupying the far aryl binding site.

Publication types

  • Comparative Study

MeSH terms

  • Acrylamides / chemistry*
  • Alkyl and Aryl Transferases / antagonists & inhibitors*
  • Alkyl and Aryl Transferases / chemistry*
  • Benzophenones / chemistry*
  • Binding Sites
  • Farnesyltranstransferase
  • Structure-Activity Relationship
  • Thiophenes / chemistry*

Substances

  • Acrylamides
  • Benzophenones
  • Thiophenes
  • Alkyl and Aryl Transferases
  • Farnesyltranstransferase