荧光法和分子对接研究4种黄酮与血清白蛋白的相互作用  

Interaction Between Serum Albumin and Four Flavones by Fluorescence Spectroscopy and Molecular Docking

作　　者：徐倩[1] 邓丹丹[1] 曹志娟[1] 谢琼[1] 梁建英[1] 卢建忠[1] 

机构地区：[1]复旦大学药学院,上海201203

出　　处：《分析化学》2010年第4期483-487,共5页Chinese Journal of Analytical Chemistry

基　　金：国家自然科学基金(No.90409017);上海市中药现代化(No.08DZ1971201)资助项目

摘　　要：结合分子对接理论和荧光法研究4种黄酮类天然产物与白蛋白的相互作用及作用机理。用FlexX软件研究了黄芩素、黄芩苷、汉黄芩素、灯盏乙素和白蛋白的分子对接,然后用荧光法研究这4种黄酮类天然产物与牛血清白蛋白的结合反应,测定了结合常数KA、结合位点n等参数。研究表明:4种天然产物与牛血清白蛋白结合位点n≈1,温度对结合位点影响不大;黄芩素和汉黄芩素主要通过疏水作用力与白蛋白结合,而黄芩苷和灯盏乙素主要通过氢键和范德华力与白蛋白结合。荧光实验和分子对接理论研究结果一致,两者相互补充,能够从实验和理论两方面协同研究天然产物与蛋白之间的相互作用。Combined with molecular docking model,a fluorescence method was applied to investigate the interaction between BSA and four flavones and the acting mechanism.The interaction between BSA and four flavones,including baicalein,baicalin,wogonin and scutellarin was studied by the FlexX molecular docking model and fluorescence spectroscopy.The binding constant KA and the number of binding site n were thus determined.The results revealed that the binding site value between flavones and BSA was nearly one and the binding site was temperature-independent.It was found that baicalein and wogonin tended to bind with BSA mainly by hydrophobic interaction,whereas baicalin and scutellarin reacted with BSA mainly by hydrogen bond and van der waals forces.Both fluorescence spectroscopy and molecular docking model are complimentary to each other for the investigation of the interaction between albumin and natural product from the experimental and theoretical view.

关 键 词：牛血清白蛋白 黄芩素 黄芩苷 汉黄芩素 灯盏乙素 荧光光谱法 分子对接 

分 类 号：R96[医药卫生—药理学]