<b>Binding properties between curcumin and malarial tubulin: molecular-docking and </b><i><b>ab initio</b></i><b> fragment molecular orbital calculations</b>

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  • Ota Shintaro
    Department of Computer Science and Engineering, Toyohashi University of Technology
  • Tomioka Shougo
    Department of Computer Science and Engineering, Toyohashi University of Technology
  • Sogawa Haruki
    Department of Computer Science and Engineering, Toyohashi University of Technology
  • Satou Riku
    Department of Computer Science and Engineering, Toyohashi University of Technology
  • Fujimori Mitsuki
    Department of Computer Science and Engineering, Toyohashi University of Technology
  • Karpov Pavel
    Institute of Food Biotechnology and Genomics, National Academy of Sciences of Ukraine,
  • Shulga Sergey
    Institute of Food Biotechnology and Genomics, National Academy of Sciences of Ukraine,
  • Blume Yaroslav
    Institute of Food Biotechnology and Genomics, National Academy of Sciences of Ukraine,
  • Kurita Noriyuki
    Department of Computer Science and Engineering, Toyohashi University of Technology

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Other Title
  • 分子ドッキング及びフラグメント分子軌道計算によるクルクミンとチューブリン間の結合特性の解析

Abstract

<p>Curcumin can bind to tubulin and inhibit the formation of tubulin polymer, which contributes to the formation of microtubule. Binding sites of curcumin on the α- and β-tubulin heterodimer were predicted by a molecular docking study to ascertain probable causes for the observed anti-microtubule effects of curcumin. However, the specific interactions between curcumin and the tubulins have yet to be elucidated at an electronic level. We here investigated the binding properties between curcumin and α- or β-tubulin of Plasmodium falciparum, using ab initio fragment molecular orbital (FMO) calculations, in order to reveal the preferable binding sites of curcumin on these tubulins. The results were compared with those for some microtubule destabilizing drugs evaluated by the same method to confirm the efficiency of curcumin as an inhibitor to the tubulins. Our ab initio FMO calculations might provide useful information for proposing novel therapeutic agents with significant binding affinity to both the α- and β-tubulins. </p>

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