荧光光谱法研究顺铂与牛血清白蛋白的键合  

Study on the Interaction between Cisplatin and Bovine Serum Albumin by Fluorescent Spectrometry

作　　者：郑茂东[1] 颜娟[1] 庞茜茜 梁江[1] 赵秀花[1] 张鹤鸣[1] 

机构地区：[1]河北北方学院附属第一医院药学部,河北张家口075000

出　　处：《中国药师》2017年第1期11-14,共4页China Pharmacist

基　　金：河北省医学科学研究重点课题计划项目(编号:ZD20140167);张家口市科技局项目(编号:1421132D)

摘　　要：目的:探讨在人体生理条件下顺铂与牛血清白蛋白(BSA)的结合作用。方法:采用荧光光谱法研究顺铂与BSA的作用机制;考察其结合常数、结合位点数和作用力类型;考察顺铂对BSA构象的影响。结果:顺铂对BSA的猝灭过程是形成基态复合物的静态猝灭,顺铂与BSA结合位点数和结合常数分别为1.36×10~4L·mol^(-1)和0.991,两者以氢键和范德华力为主。同步荧光表明两者结合作用影响色氨酸残基所处的微环境。结论:顺铂能与BSA结合并改变BSA的构象。Objective： To study the interaction between cisplatin and bovine serum albumin （BSA） under the simulated human physiological condition. Methods： The interaction mechanism of BSA and cisplatin was investigated by fluorescent spectrometry; the binding constant, binding site and interaction force were studied, and the interaction effects on the conformation change of BSA were investigated as well. Results ： The results of fluorescent spectrometry showed that a ground state complex was formed between cisplatin and BSA, and the mechanism of fluorescence quenching was static quenching. The binding parameters of cisplatin and BSA were as follows： the binding constant was 1.36 × 104 L mol-l, the binding site was 0.991, and the interaction was mainly driven by hydrogen bonds and Van Der Waals forces. The results of synchronous fluorescent spectrometry demonstrated that the interaction influenced the ml of amide acid residues. Conclusion： Cisplatin can interact with BSA and change the conformation of BSA.

关 键 词：顺铂 牛血清白蛋白 荧光光谱法 同步荧光光谱法 

分 类 号：R979.11[医药卫生—药品]