双氯芬酸钠与牛血清白蛋白结合反应的特征

双氯芬酸钠与牛血清白蛋白结合反应的特征 Binding Feature Between Diclofenac Sodium and Bovine Serum Albumin 颜承农 YAN Cheng-nong~1 1 2 3 first-author 上官云凤 SHANGGUAN Yun-feng~1 1 2 3 张华新 ZHANG Hua-xin~1 1 2 3 吴薇 WU Wei~1 1 2 3 李凡霞 LI Fan-xia~1 1 2 3 刘义 LIU Yi~2 1 2 3 长江大学化学与环境工程学院 长江大学化学与环境工程学院 College of Chemistry and Enviornmental Engineering, Yangtze University College of Chemistry and Enviornmental Engineering, Yangtze University 武汉大学化学与分子科学学院,湖北,荆州,434020 武汉大学化学与分子科学学院,湖北,荆州,434020 College of Chemistry and Molecule Sciences, Wuhan University College of Chemistry and Molecule Sciences, Wuhan University ,湖北,武汉,430072 ,湖北,武汉,430072 在模拟人体生理条件下,采用荧光光谱和紫外 可见吸收光谱法研究了双氯芬酸钠与牛血清白蛋白的结合反应.实验结果显示,双氯芬酸钠对牛血清白蛋白有较强的荧光猝灭作用,该猝灭过程主要为静态荧光猝灭过程;二者结合常数KLB=2.167×105mol·L-1;二者的结合位置距212位色氨酸2.13nm;同时,由结合反应的热力学参数得出二者作用力主要是氢键或VanderWall’s力. The binding feature between diclofenac sodium and bovine serum albumin （BSA） was studied using fluorescence spectroscopy.It was shown that diclofenac sodium had a powerful ability to quench the BSA fluorescence via a nonradiative nenergy transfer mechanism.The fluorescence quenching data show that this quenching belonged to static fluorescence quenching,the binding constant was 2.167×10 5 mol·L -1 , the binding locality was an area 2.13 nm away from tryptophan residue; the binding power was hydrogen bond or Van der Wall’s power. 双氯芬酸钠 牛血清白蛋白 荧光光谱法 热力学参数 deiclofenac sodium bovine serum albumin fluorescence spectrum thermodynamic parameters O629 国家自然科学基金（30170010）;湖北省教育厅科学研究重点资助项目（2003A003） 2004-06-01 2021-04-01 6