In silico identification and biochemical characterization of novel inhibitors of NQO1

Bioorg Med Chem Lett. 2006 Dec 15;16(24):6246-54. doi: 10.1016/j.bmcl.2006.09.015. Epub 2006 Sep 29.

Abstract

From in silico docking and COMPARE analysis, novel inhibitors of human NAD(P)H quinone oxidoreductase (NQO1) have been identified from the NCI compound database, the most potent of which has an observed IC(50) of 0.7muM. The inhibitors exhibit a diverse range of scaffolds. The ability of docking calculations to predict experimentally determined binding affinities for NQO1 is discussed, considering the influence of target flexibility and scoring function.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Binding Sites
  • Enzyme Inhibitors / chemical synthesis*
  • Enzyme Inhibitors / pharmacology*
  • Humans
  • Models, Molecular
  • NAD(P)H Dehydrogenase (Quinone) / antagonists & inhibitors*
  • Protein Conformation

Substances

  • Enzyme Inhibitors
  • NAD(P)H Dehydrogenase (Quinone)
  • NQO1 protein, human