In silico identification and biochemical characterization of novel inhibitors of NQO1

Karen A. Nolan; David J. Timson; Ian J. Stratford; Richard A. Bryce

doi:10.1016/j.bmcl.2006.09.015

In silico identification and biochemical characterization of novel inhibitors of NQO1

Karen A. Nolan, David J. Timson, Ian J. Stratford, Richard A. Bryce

Research output: Contribution to journal › Article › peer-review

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 IC₅₀ of 0.7 μM. 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.

Original language	English
Pages (from-to)	6246-6254
Number of pages	9
Journal	Bioorganic and Medicinal Chemistry Letters
Volume	16
Issue number	24
DOIs	https://doi.org/10.1016/j.bmcl.2006.09.015
Publication status	Published - 15 Dec 2006

Keywords

Docking
Inhibitors
NQO1
Rational drug design
Scoring functions
Virtual screening

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10.1016/j.bmcl.2006.09.015

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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 IC50 of 0.7 μM. 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.",

keywords = "Docking, Inhibitors, NQO1, Rational drug design, Scoring functions, Virtual screening",

author = "Nolan, {Karen A.} and Timson, {David J.} and Stratford, {Ian J.} and Bryce, {Richard A.}",

year = "2006",

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doi = "10.1016/j.bmcl.2006.09.015",

language = "English",

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journal = "Bioorganic and Medicinal Chemistry Letters",

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AU - Nolan, Karen A.

AU - Timson, David J.

AU - Stratford, Ian J.

AU - Bryce, Richard A.

PY - 2006/12/15

Y1 - 2006/12/15

N2 - 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 IC50 of 0.7 μM. 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.

AB - 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 IC50 of 0.7 μM. 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.

KW - Docking

KW - Inhibitors

KW - NQO1

KW - Rational drug design

KW - Scoring functions

KW - Virtual screening

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DO - 10.1016/j.bmcl.2006.09.015

M3 - Article

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EP - 6254

JO - Bioorganic and Medicinal Chemistry Letters

JF - Bioorganic and Medicinal Chemistry Letters

IS - 24

ER -

In silico identification and biochemical characterization of novel inhibitors of NQO1

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Keywords

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