光谱法研究刺芒柄花素与牛血清白蛋白的相互作用  

Interaction between Formononetin and bovine serum albumin by spectroscopy

作　　者：倪永年[1,2] 张方圆[2] 张秋兰[1,2] 

机构地区：[1]南昌大学食品科学与技术国家重点实验室,江西南昌330047 [2]南昌大学化学系,江西南昌330031

出　　处：《南昌大学学报（理科版）》2011年第2期146-150,共5页Journal of Nanchang University(Natural Science)

基　　金：国家自然科学基金资助项目(21065007);南昌大学食品科学与技术国家重点实验室基金资助项目(SKLF-MB-200807 and SKLF-TS-200919)

摘　　要：在生理pH7.4条件下,应用光谱法研究药物小分子刺芒柄花素与牛血清白蛋白相互作用机理。通过荧光法和紫外吸收光谱法确定了刺芒柄花素对牛血清白蛋白的荧光猝灭机制。采用Stern-Volmer方程求出相互作用的猝灭常数,双对数方程求出结合常数Ka和结合位点数n,进而利用热力学公式判别作用力类型。结果表明:刺芒柄花素与牛血清白蛋白的相互作用的荧光猝灭属于静态方式,298 K时结合常数Ka为1.39×106L.mol-1,结合位点数为1,而主要作用力类型是静电作用。用紫外与同步荧光光谱法研究了刺芒柄花素对BSA构象的影响。The interaction between formononetin and bovine serum albumin（BSA） was studied under physiological condition by spectroscopic method.The quenching mechanism of the fluorescence of BSA by formononetin was studied with the fluorescence and UV-vis spectrosmetry.The binding constants,number of binding sites and types of the binding force were evaluated by using the Stern-Volmer,double-reciprocal and thermodynamic equations.It was found that fluorescence quenching of the interaction was due to the static quenching.There is one binding site between formononetin and BSA,and the binding force is electrostatic interaction.The synchronous fluorescence spectra showed that the binding of formononetin to BSA confirm some micro-environmental and conformational changes of BSA.

关 键 词：刺芒柄花素 牛血清白蛋白 相互作用 荧光光谱 紫外吸收光谱 

分 类 号：O657[理学—分析化学]