二苯甲酮与人血清白蛋白相互作用的研究  

Study on the interaction between benzophenone and human serum albumin

作　　者：邹雪晴[1] 周雄威 邹婷[1] 张业中[1] 戴捷[1] 

机构地区：[1]长江大学化学与环境工程学院,湖北荆州434023

出　　处：《化学研究与应用》2014年第7期1048-1052,共5页Chemical Research and Application

基　　金：国家自然科学基金项目(21173026)资助;国家大学生创新性实验计划项目(104892013019)资助

摘　　要：在模拟人体生理条件下(pH=7.4),采用荧光光谱、位点竞争、三维荧光光谱研究了二苯甲酮(BP)与人血清白蛋白(HSA)之间的相互作用。根据修正的Stern-Volmer方程计算了不同温度下的结合常数,并结合Van't Hoff方程计算出相应的热力学参数。实验结果表明,BP对HSA的猝灭机制为静态猝灭过程,氢键和范德华力是维持BP-HSA复合物稳定的主要作用力;位点竞争实验揭示了BP在HSA上的结合位点位于亚域结构II A上的疏水腔中(site I位);三维荧光光谱分析表明BP使HSA发生了轻微地解旋,HSA的二级结构发生了改变。The interaction between Benzophenone and human serum albumin was studied by the methods of fluorescence spectrosco-py combined with site marker competitive experiment and three-dimensional fluorescence spectra under the simulative physiological conditions. The corresponding association contants （ Ka ） at different temperatures have been determined by the modified Stern-Volmer equation,and the thermodynamic parameters were obtained by Van’ t Hoff equation. The experimental results indicated that the quenching mechanism of BP-HSA is a static process and the hydrogen bond and van der Waals played a great role in forming a stable complex. Site marker competitive experiments revealed that the binding site of BP to HSA located in sub-domainIIA（ siteⅠ） . The change in the secondary structure of the protein was evident according to three dimensional fluorescence spectra,which showed that the presence of BP caused the slight looseness of the polypeptide of protein.

关 键 词：二苯甲酮 人血清白蛋白 荧光光谱 位点竞争 三维荧光光谱 

分 类 号：O641.3[理学—物理化学]