Rational design of an organometallic glutathione transferase inhibitor

Angew Chem Int Ed Engl. 2009;48(21):3854-7. doi: 10.1002/anie.200900185.

Abstract

Double trouble: A hybrid organic-inorganic (organometallic) inhibitor was designed to target glutathione transferases. The metal center is used to direct protein binding, while the organic moiety acts as the active-site inhibitor (see picture). The mechanism of inhibition was studied using a range of biophysical and biochemical methods.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Crystallography, X-Ray
  • Drug Design*
  • Enzyme Inhibitors / chemical synthesis
  • Enzyme Inhibitors / chemistry*
  • Enzyme Inhibitors / pharmacology*
  • Glutathione Transferase / antagonists & inhibitors*
  • Glutathione Transferase / genetics
  • Glutathione Transferase / metabolism*
  • Models, Molecular
  • Molecular Structure
  • Mutation / genetics
  • Organometallic Compounds / chemical synthesis
  • Organometallic Compounds / chemistry*
  • Organometallic Compounds / pharmacology*

Substances

  • Enzyme Inhibitors
  • Organometallic Compounds
  • Glutathione Transferase