CAJ | 학술논문

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。
이용형광광보법화자외흡수광보연구약물소분자상황소(morin)여개조단백린산매(calcineurin,CN)재완충액중적상호작용,병결합Doking분자모의대접진일보분석상황소여CNA적결합위점。결과표명：재완충액중,상황소여CNA적상호작용인기적형광쉬멸속우정태쉬멸。채용위점결합모형공식화복사특 Foster비복사능량전이궤리구해출결합상수、결합위점수이급결합거리。결과현시상황소기본가이여 CNA 이1∶1적비례결합,주요결합위치위우최화구。 Docking분자모의대접실험결과야현시상황소여파매최가능적결합위점위우최화구。
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 calcineurin 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.