荧光光度法研究微乳介质中丹参酮ⅡA与牛血清白蛋白的相互作用  

Study of the interaction between tanshinone-ⅡA and bovine serum albumin

作　　者：吴祎[1] 孙悦[1] 潘旭旭[1] 周锦梅[1] 沈志滨[1] 

机构地区：[1]广东药学院中药学院

出　　处：《广东药学院学报》2009年第4期335-338,共4页Academic Journal of Guangdong College of Pharmacy

基　　金：广东省自然科学基金博士启动项目(845102240100160);广东药学院博士科研启动项目(43548021)

摘　　要：目的研究微乳介质中丹参酮ⅡA和牛血清白蛋白的相互作用行为。方法采用荧光光度法,通过Stern-Volmer公式计算荧光猝灭数据和结合常数,通过计算热力学数据探讨丹参酮ⅡA和牛血清白蛋白的相互作用机理。结果常温下结合常数为1.93×104L·moL-1,且结合常数、猝灭常数均随温度升高而降低,热力学数据ΔH0、ΔS0和ΔG0均为负值。结论在微乳液中,丹参酮ⅡA对牛血清白蛋白的猝灭机制属于复合物的静态猝灭过程,其结合机制可能为范德华力和氢键作用力。Objective To study the interaction between tanshinone- ⅡA and bovine serum albumin （BSA） in the microemulsion system by fluorometry. Methods The binding constant KA was calculated by SternVolmer equation,The enthalpy variation （△H^0）,Gibbs free energy variation （△G^0） and entropy variation （ △S^0） were used to explore the interaction mechanism of tanshinone - ⅡA and BSA. Results The binding constant KA was 1.93×10^4L·moL^-1 at 293 K, the quenching constant and the binding constant both decreased with the increase of temperature,the values of △H^0、△S^0and△G^0 were all negative. Conclusion It was found that the binding of tanshinone- ⅡA to BSA in microemulsion system might be concerned with van der Waals force and hydrogen bonding force.

关 键 词：丹参酮ⅡA 牛血清白蛋白 微乳液 结合力 

分 类 号：R285[医药卫生—中药学]