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荧光光谱法研究香豆素-3-羧酸与牛血清白蛋白的相互作用
引用本文:郁有祝,王芳,郭玉华,牛永生,石蔚云,申艳红.荧光光谱法研究香豆素-3-羧酸与牛血清白蛋白的相互作用[J].信阳师范学院学报(自然科学版),2015(1):113-116.
作者姓名:郁有祝  王芳  郭玉华  牛永生  石蔚云  申艳红
作者单位:安阳工学院化学与环境工程学院,河南安阳,455000
基金项目:国家自然科学基金项目(21302003);安阳工学院青年科研基金项目
摘    要:利用荧光光谱、紫外吸收光谱法研究了香豆素-3-羧酸与牛血清白蛋白(BSA)的相互作用.结果表明:香豆素-3-羧酸对BSA的荧光猝灭为静态猝灭,香豆素-3-羧酸与BSA 1∶1结合形成复合物,结合常数与结合位点分别为3.21×104L·mo L-1,0.974 6(298 K)和2.00×104L·mo L-1,0.949 5(310 K),两者之间的作用力以氢键和范德华力为主.同步荧光光谱表明,香豆素-3-羧酸与色氨酸残基发生了作用,从而使其所处的微环境发生了改变.

关 键 词:香豆素-3-羧酸  牛血清白蛋白  相互作用  荧光光谱

Interaction of Coumarin-3-carboxylic Acid with Bovine Serum Albumin by Fluorescence Spectroscopy
Yu Youzhu,Wang Fang,Guo Yuhua,Niu Yongsheng,Shi Weiyun,Shen Yanhong.Interaction of Coumarin-3-carboxylic Acid with Bovine Serum Albumin by Fluorescence Spectroscopy[J].Journal of Xinyang Teachers College(Natural Science Edition),2015(1):113-116.
Authors:Yu Youzhu  Wang Fang  Guo Yuhua  Niu Yongsheng  Shi Weiyun  Shen Yanhong
Institution:Yu Youzhu;Wang Fang;Guo Yuhua;Niu Yongsheng;Shi Weiyun;Shen Yanhong;College of Chemistry and Environmental Engineering,Anyang Institute of Technology;
Abstract:The interaction of coumarin-3-carboxylic acid with bovine serum albumin( BSA) was investigated by fluorescence and UV spectroscopy. The results showed that coumarin-3-carboxylic acid could quench the intrinsic fluorescence of BSA,and the quenching mechanism was a static quenching process. The number of binding points demonstrated that coumarin-3-carboxylic acid and BSA formed the complex of mole ratio 1 ∶ 1. The binding constants and the number of binding sites were determined to be 3. 21 × 104L·mo L- 1,0. 974 6( 298 K) and 2. 00 × 104L·mo L- 1,0. 949 5( 310 K),respectively. The driving forces were mainly hydrogen bond and Vander Waals. Synchronous spectra showed that coumarin-3-carboxylic acid binded to tryptophan residue and changed the microenvironment of tryptophan residue.
Keywords:coumarin-3-carboxylic acid  bovine serum albumin  interaction  fluorescence spectroscopy
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