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

作　　者：颜承农[1] 上官云凤[1] 张华新[1] 吴薇[1] 李凡霞[1] 刘义[2] 

机构地区：[1]长江大学化学与环境工程学院,湖北荆州434020 [2]武汉大学化学与分子科学学院,湖北武汉430072

出　　处：《武汉大学学报（理学版）》2004年第6期683-686,共4页Journal of Wuhan University:Natural Science Edition

基　　金：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)

摘　　要：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.

关 键 词：双氯芬酸钠 牛血清白蛋白 荧光光谱法 热力学参数 

分 类 号：O657.39[理学—分析化学]