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荧光光谱法研究氢化可的松与牛血清白蛋白的结合作用

Study on Binding of Hydrocortisone with Bovine Serum Albumin by Fluorescence Spectroscopy

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【作者】 徐科黄亚励刘红徐红

【Author】 XU Ke,HUANG Ya-li,LIU Hong,XU Hong(Department of Chemistry,Guiyang Medical College,Guiyang 550004,China)

【机构】 贵阳医学院化学教研室

【摘要】 模拟人体pH值,在不同温度下采用荧光光谱和同步荧光光谱研究了氢化可的松与牛血清白蛋白(BSA)的相互作用及对其同步荧光的影响。结果表明,在pH值7.37的Tris-HCl缓冲溶液中,氢化可的松和BSA彼此扩散和碰撞达到动态平衡导致BSA荧光猝灭,属于动态猝灭机制。计算得到BSA与氢化可的松在25℃和37℃下动态猝灭的猝灭常数分别为1.98105×107 L.mol-1.s-1和2.05933×107 L.mol-1.s-1。根据热力学方程得出氢化可的松与BSA相互作用的参数,ΔH<0、ΔS>0,说明氢化可的松与BSA相互作用以静电引力为主。氢化可的松加入后,BSA同步荧光光谱(Δλ=60nm)的最大发射波长发生红移,表明色氨酸残基所处环境的极性增加。

【Abstract】 The binding characteristics of hydrocortisone and bovine serum albumin(BSA) were studied by fluorescence and synchronous fluorescence spectroscopy at different temperatures in simulated human body pH value.The results showed that hydrocortisone had a powerful ability to quench the BSA fluorescence via a diffusion and impact energy transfer mechanism in the Tris-HCl buffer system with a pH value of 7.37.The quenching rate constants,the binding constants and the binding sites of the dynamic quenching were calculated at different temperatures.And according to the thermodynamic parameters calculated,the binding of BSA at Δλ=60 nm and hydrocortisone was mainly attributed to the electrostatic attraction force.The maximum emission wavelength of the synchronous fluorescence spectrum of BSA had a red shift in the presence of bydrocortisone,indicating that it enhanced the polarity of the environment in which Trp residues existed.

【基金】 黔科合SY字[2011]3128项目资助
  • 【文献出处】 化学与生物工程 ,Chemistry & Bioengineering , 编辑部邮箱 ,2012年11期
  • 【分类号】R96
  • 【被引频次】11
  • 【下载频次】178
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