依巴斯汀与牛血清蛋白相互作用的荧光光谱研究  

Interaction between Ebastine and Bovine Serum Albumin by Fluorescence Spectroscopy

作　　者：陆从文 兰秀风[1] 张林[2] 陈霞[1] 

机构地区：[1]南京航空航天大学理学院,南京211106 [2]河海大学理学院,南京211100

出　　处：《光子学报》2015年第10期70-75,共6页Acta Photonica Sinica

基　　金：中央高校基本科研业务费专项资金(No.NS2015080);国家自然科学基金青年基金(No.61205201)资助~~

摘　　要：在PH=7.4的PBS缓冲溶液中,利用荧光光谱研究了在依巴斯汀存在下牛血清蛋白的荧光猝灭特征.通过实验得到三个温度(298K,305K,312K)下的猝灭光谱曲线组,根据Stern-Volmer方程计算各相应温度下的猝灭常数发现:依巴斯汀对牛血清蛋白的荧光猝灭机制属于静态猝灭.通过对依巴斯汀-牛血清蛋白体系的热力学参量的计算得出依巴斯汀与牛血清蛋白间的相互作用力类型为疏水作用力.通过拟合双对数方程计算出在以上三个温度下结合常数分别为3.27×104 L·mol-,4.11×104 L·mol-,7.59×104 L·mol-,结合位点数为0.98、1.02、1.08.依据Frster非辐射能量转移理论计算出荧光供能体(牛血清蛋白)与受能体(依巴斯汀)之间的结合距离为2.8nm,利用同步荧光光谱及三维荧光光谱技术分析了依巴斯汀对牛血清蛋白构象的影响.In the Phosphate Buffer Saline buffer solution at PH 7.4,the fluorescence quenching characteristics of Bovine Serum Albumin when Ebastine existed were studied by Fluorescence spectra.After experiments,three quenching spectral curve groups were obtained under corresponding temperatures（298K,305 K,312K）.According to the Stern-Volmer equation,the quenching constants were calculated and then it was concluded：the quenching was belonged to static quenching mechanism.By calculating the thermodynamic parameters of the Ebastine-Bovine Serum Albumin system,it was shown that the binding power between Bovine Serum Albumin and Ebastine was mainly the hydrophobic force.By fitting the double logarithmic equation,the binding constants KAbetween Bovine Serum Albumin and Ebastine at three temperatures were obtained to be 3.27×10^4 L·mol^-,4.11×10^4 L·mol^-and 7.59×10^4 L·mol^-,respectively.The number of binding sites were 0.98,1.02,1.08.The binding distance between the donor（Bovine Serum Albumin）and the acceptor（Ebastine）was determined based on the Frster′s non-radiation energy transfer theory and it turned out to be 2.8nm.The effect of Ebastine on the conformation of Bovine Serum Albumin was analysed by synchronous fluorescence spectra and three-dimensional fluorescence spectra.

关 键 词：牛血清蛋白 依巴斯汀 荧光光谱 相互作用 蛋白质构象 

分 类 号：O657.31[理学—分析化学]