title: In silico identification and biochemical characterization of novel inhibitors of NQO1.
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.
authors.affiliation: School of Pharmacy and Pharmaceutical Sciences, University of Manchester, Oxford Road Manchester M13 9PL, UK.
authors.forename: Karen A
authors.initials: KA
authors.lastname: Nolan
authors.forename: David J
authors.initials: DJ
authors.lastname: Timson
authors.forename: Ian J
authors.initials: IJ
authors.lastname: Stratford
authors.forename: Richard A
authors.initials: RA
authors.lastname: Bryce
mesh_terms: D000595:Amino Acid Sequence; D001665:Binding Sites; D004791:Enzyme Inhibitors / Q000138:chemical synthesis* / Q000494:pharmacology*; D006801:Humans; D008958:Models, Molecular; D016660:NAD(P)H Dehydrogenase (Quinone) / Q000037:antagonists & inhibitors*; D011487:Protein Conformation
chemical_list: D004791:Enzyme Inhibitors; D016660:NAD(P)H Dehydrogenase (Quinone); C447479:NQO1 protein, human