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    Calculation of Binding Free Energies of NAD(P)H:Quinone Oxidoreductase 1 Inhibitors

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    BhattacharyyaSpr18.pdf (772.6Kb)
    BhattacharyyaSpr18.pptx (4.243Mb)
    Date
    2018-04
    Author
    Bhattacharyay, Sudeep
    Zajac, Jonathan W.P.
    Metadata
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    Abstract
    NAD(P)H:quinone oxidoreductase 1 (NQO1) plays a key role in cellular defense in humans. It is known to reduce quinones to hydroquinones, inhibiting their ability to become a free radical semiquinone state, and cause cellular damage. NQO1 also has the ability to stabilize the tumor suppressor protein, p53, by inhibiting proteasomal degradation. In particular, it has been observed that NQO1 is activated by the reduction of the cofactor flavin – an event that triggers binding and subsequent stabilization of p53. Due to this mechanism, NQO1 holds promise for drug-targeted cancer therapy. In the proposed work, a comparative study will be conducted to explore the binding characteristics of various ligands that have the potential to be used in the drug design, including menadione, resveratrol, melatonin, and other quinone analogs that have potential binding affinity to the active site of NQO1.
    Subject
    Posters
    Chemistry
    Quinones
    NQO1
    NAD(P)H:quinone oxidoreductase 1
    Permanent Link
    http://digital.library.wisc.edu/1793/79838
    Type
    Presentation
    Description
    Color poster with text, tables, charts, and images.
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