发光学报, 2012, 33 (10): 1153, 网络出版: 2012-10-12   

光谱法研究稀土离子钇(Ⅲ)与牛血清白蛋白的相互作用

Study on Interaction of Y3+ and Bovine Serum Albumin by Spectrometry
吴锦绣 1,2,*李梅 1,2柳召刚 1,2胡艳宏 1,2王觅堂 1,2
作者单位
1 内蒙古科技大学 稀土学院, 内蒙古 包头 014010
2 内蒙古自治区高校稀土现代冶金新技术与应用重点实验室, 内蒙古 包头 014010
摘要
用荧光光谱和紫外-可见吸收光谱研究了稀土金属离子Y3+与牛血清白蛋白(BSA)的相互作用。实验结果发现:Y3+对BSA的紫外吸收光谱具有增强作用, 而对荧光光谱具有较强的荧光猝灭作用且峰位明显蓝移20~25 nm。用 Stern-Volmer 方程分别对实验数据进行分析,得出结论: Y3+对 BSA 的荧光猝灭作用是属于静态荧光猝灭, Y3+与BSA反应生成了新的复合物,发生了分子内的非辐射能量转移。求得相互作用过程的结合常数(KA)和热力学参数(ΔΗ、ΔS、ΔG), 确定了它们之间的主要作用力是范德华力、氢键等, 但静电作用力也不可忽略。同步荧光光谱法表明Y3+对牛血清白蛋白的构象有影响。
Abstract
The interaction between rare earth ion Y3+ and bovine serum albumin(BSA) was studied by fluorescence spectrum and ultraviolet-visible absorption spectrometry. It was shown that Y3+ has a quite strong effect to quench the fluorescence launching and enhance the UV absorption spectra of BSA. The maximum emission peak of BSA shifted to short wave by 20~25 nm. After the fluorescence quenching date was analyzed by Stern-Volmer equation, the results indicated that the reaction between bovine serum albumin and Y3+ generated the new complex-system. The quenching belonged to static fluorescence quenching, with non-radiation energy transfer happening within single molecule. The binding constants (KA) and thermodynamics parameters (ΔΗ, ΔS , ΔG) were calculated according to equation of fluorescence spectrometry at different temperatures. Based on thermodynamic data, the main reaction between Y3+ and BSA was van der Waals force and hydrogen bond, but electrostatic force can not be ignored. The effect of rare earth ion Y3+ on the conformation of BSA was researched by synchronous fluorescence spectrometry.

吴锦绣, 李梅, 柳召刚, 胡艳宏, 王觅堂. 光谱法研究稀土离子钇(Ⅲ)与牛血清白蛋白的相互作用[J]. 发光学报, 2012, 33(10): 1153. WU Jin-xiu, LI Mei, LIU Zhao-gang, HU Yan-hong, WANG Mi-tang. Study on Interaction of Y3+ and Bovine Serum Albumin by Spectrometry[J]. Chinese Journal of Luminescence, 2012, 33(10): 1153.

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