Design and synthesis of selective, high-affinity inhibitors of human cytochrome P450 2J2

Bioorg Med Chem Lett. 2006 May 15;16(10):2777-80. doi: 10.1016/j.bmcl.2006.02.004. Epub 2006 Feb 21.


The active site topology, substrate specificity, and biological roles of the human cytochrome P450 CYP2J2, which is mainly expressed in the cardiovascular system, are poorly known even though recent data suggest that it could be a novel biomarker and potential target for therapy of human cancer. This paper reports a first series of high-affinity, selective CYP2J2 inhibitors that are related to terfenadine, with K(i) values as low as 160nM, that should be useful tools to determine the biological roles of CYP2J2.

MeSH terms

  • Cytochrome P-450 CYP2J2
  • Cytochrome P-450 Enzyme Inhibitors*
  • Cytochrome P-450 Enzyme System / metabolism
  • Drug Design
  • Enzyme Inhibitors / chemical synthesis*
  • Enzyme Inhibitors / pharmacology*
  • Humans
  • Magnetic Resonance Spectroscopy
  • Oxygenases / antagonists & inhibitors*
  • Oxygenases / metabolism
  • Substrate Specificity


  • CYP2J2 protein, human
  • Cytochrome P-450 Enzyme Inhibitors
  • Enzyme Inhibitors
  • Cytochrome P-450 Enzyme System
  • Oxygenases
  • Cytochrome P-450 CYP2J2