稀土金属离子与人血清白蛋白的相互作用  

Interaction of Rare Earth Ions with Human Serum Albumin

作　　者：宋玉民[1] 吴锦绣[1] 郑秀荣[1] 吴琼[1] 

机构地区：[1]西北师范大学化学化工学院,兰州730070

出　　处：《无机化学学报》2006年第9期1615-1622,共8页Chinese Journal of Inorganic Chemistry

基　　金：甘肃省自然科学基金(No.3ZS051-A25-021);甘肃省高分子材料重点实验室资助项目。

摘　　要：本文用荧光光谱、紫外-可见吸收光谱法和循环伏安法研究了稀土金属离子Eu髥、Pr髥与人血清白蛋白(HSA)的相互作用。实验发现:Eu髥和Pr髥对HSA有较强的荧光猝灭作用。用Stern-Volmer方程分别对实验数据进行处理,结果发现:HSA与Eu髥、Pr髥发生反应生成了新的复合物,发生了分子内的非辐射能量转移。Eu髥、Pr髥对HAS的荧光猝灭作用,属于静态荧光猝灭。荧光猝灭图表明:Eu3+和Pr3+在HSA分子中至少有两类结合位点,Eu3+与HSA形成2.76∶1的复合物,结合常数lgK分别为12.03和9.05;Pr3+与HSA形成2.2∶1的复合物,结合常数lgK分别为9.89和6.97。同时用圆二色谱及同步荧光光谱法探讨了Eu髥和Pr髥对HSA构象的影响。The interaction of Eu（Ⅲ） and Pr（Ⅲ） with HSA was studied by fluorescence spectrum and ultra-violet spectrum and electrochemistry. It was shown that these ions have a quite strong ability to quench the fluorescence launching of HSA. After analyzing the fluorescence quenching data according to Stern-Volmer equation, It was found that HSA reacted with Eu（Ⅲ） and Pr（Ⅲ） to form a new complex-system. The quenching belonged to static fluorescence quenching, with non-radiation energy transfer happening within single molecule, The composition of the Eu-HSA complex is Eu2.76：HSA and the binding constants： lgK=12.03, lgK=9.05; The composition of the Pr-HSA complex is Pr2.2：HSA and the binding constants： lgK=9.89, lgK=6.97 at room temperature. The effect of Eu （Ⅲ） and Pr（Ⅲ） on the conformation of HSA was analyzed by circular dichroism （CD） and synchronous fluorescence spectra.

关 键 词：稀土离子 人血清白蛋白 吸收光谱 荧光光谱 圆二色谱 电化学 

分 类 号：O614.334[理学—无机化学] O614.338[理学—化学]