光谱法与分子对接研究槲皮素与牛血清白蛋白的结合特性  

Interaction characteristics of quercetin and BSA using spectroscopic and molecular docking

作　　者：杨荣荣[1] 朱靖博[1,2] 寇自农[3] 丁燕[1,2] 王琳琳[1] 

机构地区：[1]大连工业大学食品学院,大连116034 [2]大连工业大学植物资源化学与应用研究所,大连116034 [3]大连工业大学实验仪器中心,大连116034

出　　处：《食品科技》2014年第7期93-98,共6页Food Science and Technology

基　　金：中药制药过程新技术国家重点实验室项目;辽宁省高等学校重大科技平台项目(辽教发[2011]191号)

摘　　要：采用荧光光谱、紫外吸收光谱及分子对接研究了槲皮素与牛血清白蛋白(BSA)分子间的相互作用。结果表明,槲皮素对BSA有明显的荧光猝灭作用,加入槲皮素后BSA的紫外图谱发生变化,荧光猝灭常数Ksv与温度呈负相关,22℃的猝灭速率Kq为1.68×1013 L/(mol·s),说明槲皮素对BSA的荧光猝灭属于静态猝灭范畴。22℃时槲皮素与BSA相互作用的结合常数K为6.93×105 L/mol,结合位点数n为1.1467。热力学参数表明二者的结合力主要为疏水作用力,同步荧光光谱表明槲皮素与BSA的结合影响BSA的构象。分子对接结果表明槲皮素结合在BSA的亚结构区域II(siteⅠ)中,主要通过疏水作用结合同时还存在氢键及静电作用力,槲皮素与Trp-213氨基酸残基的作用距离更近,分子对接研究结果与光谱实验结果对应一致。The interaction between quercetin and bovine serum albumin （BSA） was studied by fluorescence, UV-vis absorption spectrum and molecular docking. The results showed that the fluorescence of BSA is quenched obviously by quercetin. UV spectra of BSA changed after adding quercetin. Fluorescence quenching constant Ksv was negatively correlated with temperature and the fluorescence quenching rate Kq is 1.68×10^13L/（mol·s） at 22 %, which suggested the mechanism of fluorescence quench was static mode. The binding constant is 6.93×10^5L/mol and the number of binding sites is 1.1467 at 22 %. Thermodynamic parameters indicated that hydrophobic interaction play a main role in the combination of them. Synchronous fluorspar spectra show that the combination of them affected the conformation of BSA. Molecular docking results indicated that the binding of quercetin within the hydrophobic cavity in subdomain IIA （site I） of BSA, hydrophobic interactions play a main role there also exist hydrogen bonds and electrostatic force and the distance between quercetin and Trp-213 residues more closer. Molecular docking results consistent with the corresponding spectral results.

关 键 词：槲皮素 牛血清白蛋白(BSA) 荧光光谱 紫外可见光谱 分子对接 

分 类 号：R284[医药卫生—中药学]