稀土钐水杨醛氨基酸Schiff碱配合物与BSA相互作用研究  

Interactions between Rare Earth Samarium Complex with Salicylaldehyde Amino Schiff Base and Bovine Serum Albumin

作　　者：陈芳[1] 吴亚伟[1] 胡冬梅[1] 陆江林[1] 

机构地区：[1]湖北师范学院化学化工学院,湖北黄石435002

出　　处：《化学世界》2015年第6期332-336,共5页Chemical World

基　　金：湖北师范学院科研基金资助项目(2007B01)

摘　　要：用荧光光谱法和紫外-可见吸收光谱法研究了稀土钐水杨醛氨基酸Schiff碱配合物([SmC16H12NO4ClH2O]·H2O)与牛血清白蛋白(BSA)作用的机理,结果表明,配合物对BSA有较强的荧光猝灭作用,根据Stern-Volmer方程和猝灭常数Ksv随温度的升高而减小,表明配合物与BSA的作用机理是由于形成基态复合物所引起的静态猝灭,根据双对数方程计算了不同温度下结合常数KA、结合位点数n;根据Frster非辐射能量转移理论求出BSA与配合物间的结合距离;用同步荧光光谱法探讨了配合物对BSA构象的影响。The mechanism of interactions between rare earth samarium complex with salicylaldehyde amino Schiff base （[SmC16H12NO4ClH2O] · H2O） and bovine serum albumin was studied by fluorescence spec- trometry and ultraviolet-visible spectrometry methods. The results show that strong fluorescence quench- ing effect between the complex and BSA exists. According to the Stern - Volmer equation and the decrease of quenching constant Knv with the increase of temperature, the mechanism of the complex with BSA is static quenching by formation of the complex. The binding constant KA and the binding sites n are obtained according to the double logarithmic equation at different temperatures. The binding distancer is obtained according to the Forster radiation energy transfer theory. The influence of conformation between the com- plex and BSA is investigated by synchronous fluorescence spectrometry.

关 键 词：稀土配合物 SCHIFF碱 牛血清白蛋白 荧光光谱 

分 类 号：O614.33[理学—无机化学]