黄腐酸与人血清白蛋白相互作用机制的光谱研究  

Spectroscopic study on the interaction of fulvic acid with human serum albumin

作　　者：杨光[1] 董宇 孙晓然[1] 陈蕾[1] 陈宏博[1] 张秀凤[1] 

机构地区：[1]河北联合大学化学工程学院,唐山063009 [2]唐山学院文法系,唐山063000

出　　处：《分析试验室》2014年第5期565-568,共4页Chinese Journal of Analysis Laboratory

基　　金：河北省高等学校科学技术研究青年基金(2011106);河北省自然科学基金青年科学基金(B2012401026);北京分子科学国家实验室开放课题资助

摘　　要：利用荧光光谱研究了黄腐酸与HSA的相互作用,黄腐酸对HSA有明显的荧光猝灭作用,计算了黄腐酸与HSA作用的结合常数(Ka=1.2×107L/mol)、结合位点数(n=1.45)及结合距离(r0=2.92 nm)。黄腐酸与HSA的猝灭机制属于静态猝灭,并发生了分子内非辐射能量转移,能量从HSA向黄腐酸转移。同时,通过圆二色谱探讨了黄腐酸对HSA构象的影响,HSA与黄腐酸结合后引起了HSA肽链收缩,改变了HSA的二级结构,使HSA的结构变得更加紧密。The mechanism of interaction between fulvic acid and HSA was studied by fluorescence spectroscopy and absorption spectroscopy, fulvic acid has a strong ability to quench the fluorescence of HSA. And further the binding constant（ Ka = 1.2 ×107 L/mol）, binding number（ n = 1.45 ） and binding distance（ r0 = 2.92 nm） were calculated. The results showed that the fluorescence quenching mechanism between fulvic acid and HSA was mainly static quenching, with non-radiation energy transfer occurring within single molecule, and the energy was transferred to fulvic acid from the HSA. Meanwhile, this paper explores the influence of FA on the HSA conformation change by circular dichroism spectroscopy, and the interaction of fulvic acid with HSA causes the contraction of HSA peptide chain and increase of a-helix structure, as well as change of the secondary structure of HSA. The results show that the fulvic acid makes the structure of HSA become more closely.

关 键 词：黄腐酸 人血清白蛋白 荧光光谱 圆二色谱 相互作用 

分 类 号：O657.3[理学—分析化学]