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    Combretastatin-like chalcones as inhibitors of microtubule polymerisation. Part 2: Structure-based discovery of alpha-aryl chalcones.

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    Authors
    Ducki, Sylvie W
    Mackenzie, Grant
    Greedy, Ben
    Armitage, Simon
    Chabert, Jérémie Fournier Dit
    Bennett, Elizabeth
    Nettles, Jim
    Snyder, James P
    Lawrence, Nicholas J
    Affiliation
    Department of Chemistry, UMIST, Manchester M60 1QD, UK. Sylvie.DUCKI@univ-bpclermont.fr
    Issue Date
    2009-11-15
    
    Metadata
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    Abstract
    Tubulin is an important molecular target in cancer chemotherapy. Antimitotic agents able to bind to the protein are currently under study, commonly used in the clinic to treat a variety of cancers and/or exploited as probes to investigate the protein's structure and function. Here we report the binding modes for a series of colchicinoids, combretastatin A4 and chalcones established from docking studies carried out on the structure of tubulin in complex with colchicine. The proposed models, in agreement with published biochemical data, show that combretastatin A4 binds to the colchicine site of beta-tubulin and that chalcones assume an orientation similar to that of podophyllotoxin. The models can be used to design a new class of podophyllotoxin mimics, the alpha-aryl chalcones, capable of binding to the colchicine-binding site of beta-tubulin with higher affinity.
    Citation
    Combretastatin-like chalcones as inhibitors of microtubule polymerisation. Part 2: Structure-based discovery of alpha-aryl chalcones. 2009, 17 (22):7711-22 Bioorg. Med. Chem.
    Journal
    Bioorganic & Medicinal Chemistry
    URI
    http://hdl.handle.net/10541/109326
    DOI
    10.1016/j.bmc.2009.09.044
    PubMed ID
    19837594
    Type
    Article
    Language
    en
    ISSN
    1464-3391
    ae974a485f413a2113503eed53cd6c53
    10.1016/j.bmc.2009.09.044
    Scopus Count
    Collections
    All Paterson Institute for Cancer Research

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