桑黄素与钙调蛋白磷酸酶相互作用的研究  

INTERACTION BETWEEN CALCINEURIN AND MORIN

作　　者：高雅丹[1] 黄慧辉 岑举人[2] 王梦奇[2] 尹瑞坚 魏群[2] 

机构地区：[1]北京师范大学励耘学院,北京100875 [2]北京师范大学生命科学学院、北京市基因工程药物及生物技术重点实验室,北京100875

出　　处：《北京师范大学学报（自然科学版）》2014年第2期169-173,108,共5页Journal of Beijing Normal University(Natural Science)

基　　金：国家级大学生创新创业训练计划资助项目(105-105602)

摘　　要：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.

关 键 词：荧光光谱 紫外吸收光谱 分子模拟对接 桑黄素 

分 类 号：O657[理学—分析化学]