叶酸与人血清白蛋白结合作用的光谱研究

刘慧娟; 李鹏; 张亚东; 郭操; 邓畯元; 蔡健炜; 刘伯里

光谱学与光谱分析, 2009, 29 (7): 1915, 网络出版: 2010-05-26

叶酸与人血清白蛋白结合作用的光谱研究

Spectroscopic Study on Binding of Folic Acid to Human Serum Albumin

论文大纲

刘慧娟李鹏张亚东郭操邓畯元蔡健炜刘伯里

作者单位

放射性药物教育部重点实验室，北京师范大学化学学院，北京100875

叶酸人血清蛋白荧光光谱荧光猝灭 Folic acid Human serum albumin Fluorescence spectroscopy Fluorescence quenching

摘要

在不同温度下的pH 7.4的Tris-HCl缓冲溶液体系中, 采用荧光光谱、紫外吸收光谱和同步荧光光谱研究了人血清蛋白与叶酸的相互作用。研究表明，这种相互作用使人血清白蛋白发生内源荧光猝灭，属于静态猝灭机制。通过计算得到人血清蛋白与叶酸在17和37 ℃下静态猝灭的猝灭速率常数分别为7.396 6×104和7.2652×104 L·mol-1、结合常数分别为7.50×104和1.98×105 L·mol-1、结合位点数均为1。根据Frster非辐射能量转移机理，求算出给体（HSA）与受体（叶酸）间的作用距离和能量转移效率分别为1.77和0.052 65 nm，并结合热力学参数说明了叶酸分子与人血清白蛋白的作用以疏水作用为主，同时也存在静电引力。利用同步荧光光谱研究了人血清蛋白与叶酸的相互作用中HSA的构象变化，发现色氨酸残基所处环境的疏水性降低，说明叶酸分子进入了人血清白蛋白的疏水腔中。

Abstract

The interaction of human serum albumin and folic acid was studied using fluorescence spectroscopy, UV absorption and synchronous fluorescence spectroscopy in the pH 7.4 Tris-HCl buffer system at different temperatures. The research shows that these interactions result in the endogenous fluorescence quenching of HSA, which belongs to a static quenching mechanism. The quenching rate constants, the binding constants and the binding sites of the static quenching were calculated. The distance between the body (HSA) and receptor (folic acid) and the efficiency of energy transfer were obtained to be 1.77 nm and 0.052 65 respectively, based on the theory of Frster nonradiative energy transfer. And according to the thermodynamic parameters calculated the binding of HSA and folic acid is mainly attributed to the hydrophobic interaction, partly static force. Further more the synchronous fluorescence spectrum was utilized to investigate the conformational transformation; The decline result of the hydrophobic nature around Trp demonstrates that the folic acid is in the hydrophobic cavity of HSA.

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刘慧娟, 李鹏, 张亚东, 郭操, 邓畯元, 蔡健炜, 刘伯里. 叶酸与人血清白蛋白结合作用的光谱研究[J]. 光谱学与光谱分析, 2009, 29(7): 1915. LIU Hui-juan, LI Peng, ZHANG Ya-dong, GUO Cao, DENG Jun-yuan, CAI Jian-wei, LIU Bo-li. Spectroscopic Study on Binding of Folic Acid to Human Serum Albumin[J]. Spectroscopy and Spectral Analysis, 2009, 29(7): 1915.

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