Farnesyl protein transferase inhibitors targeting the catalytic zinc for enhanced binding

Bioorg Med Chem Lett. 2004 Dec 6;14(23):5877-80. doi: 10.1016/j.bmcl.2004.09.026.

Abstract

Successful efforts to make farnesyl transferase (FT) inhibitors with appropriately tethered ligands designed to interact with a catalytic zinc that exist in the enzyme have been realized. Thus, by introducing either a pyridylmethylamino or propylaminolimidazole amide moieties off the 2-position of the piperidine ring, FT inhibitors with activities in the picomolar range have been achieved as exemplified by compounds 12a and 12b. An X-ray structure of 11b bound to FT shows the enhanced activity is a result of interacting with the active-site zinc.

MeSH terms

  • Alkyl and Aryl Transferases / antagonists & inhibitors*
  • Alkyl and Aryl Transferases / metabolism
  • Catalytic Domain / drug effects
  • Catalytic Domain / physiology*
  • Drug Delivery Systems / methods*
  • Enzyme Inhibitors / administration & dosage
  • Enzyme Inhibitors / chemistry
  • Enzyme Inhibitors / metabolism*
  • Protein Binding / physiology
  • Protein Conformation
  • Zinc / metabolism*

Substances

  • Enzyme Inhibitors
  • Alkyl and Aryl Transferases
  • p21(ras) farnesyl-protein transferase
  • Zinc