桑黄素与钙调蛋白磷酸酶相互作用的研究

INTERACTION BETWEEN CALCINEURIN AND MORIN

利用荧光光谱法和紫外吸收光谱研究药物小分子桑黄素(morin)与钙调蛋白磷酸酶(calcineurin,CN)在缓冲液中的相互作用,并结合Doking分子模拟对接进一步分析桑黄素与CNA的结合位点.结果表明:在缓冲液中,桑黄素与CNA的相互作用引起的荧光淬灭属于静态淬灭.采用位点结合模型公式和福斯特Foster非辐射能量转移机理求解出结合常数、结合位点数以及结合距离.结果显示桑黄素基本可以与CNA以1∶1的比例结合,主要结合位置位于催化区.Docking分子模拟对接实验结果也显示桑黄素与靶酶最可能的结合位点位于催化区.

Interaction between calcineurin and morin was investigated by fluorescent spectrometry, ultraviolet absorption spectroscopy and molecular docking simulation. It was found that interaction between calcineurin and morin was a static quenching progress. The binding constants, number of binding sites and binding distance were found by the equation of site-binding and Foster theory of transfer of non-radiation energy. Morin could bind ealcineurin CNA with a stoichiometry of 1 ： 1. Distance from morin to each tryptophan （Trp） in calcineurin CNA in energy transfer experiments and docking studies interestingly provided the same binding sites for the drug molecule, which all located in a non-active site area of calcineurin CNA catalytic domain.