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 |
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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(Ⅲ)、Pr(Ⅲ)与人血清白蛋白(HSA)的相互作用。实验发现:Eu(Ⅲ)和Pr(Ⅲ)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(Ⅲ)、Pr(Ⅲ)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(Ⅲ)、Pr(Ⅲ)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(Ⅲ)和Pr(Ⅲ)对HSA构象的影响。 |
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 |
基金项目: |
Abstract: 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. |
Keywords: rare earth ions human serum albumin absorption spectra fluorescence spectra circular dichroism spectra electrochemistry |
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宋玉民,吴锦绣,郑秀荣,吴琼.稀土金属离子与人血清白蛋白的相互作用[J].无机化学学报,2006,22(9):1615-1622. |
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