| 邻菲咯啉乳酸镍配合物的合成与表征及其与牛血清白蛋白相互作用的荧光分析 |
| Synthesis and Characterization of [Ni(Hlact)2(phen)]·2H2O and Its Interaction with BSA Studied by Fluorescence Spectroscopy |
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| 摘要: 利用溶液法合成了配合物[Ni(Hlact)2(phen)]·2H2O(1),并对该配合物进行了元素分析、红外光谱和X-射线单晶衍射表征。通过荧光光谱法研究了不同温度下配合物1与牛血清白蛋白相互作用时的荧光强度的变化,计算了在不同温度下,配合物1与牛血清白蛋白(BSA)的结合常数、结合位点数以及热力学函数,并进一步讨论了配合物1与BSA相互作用时的作用力类型和两者之间的距离。结果表明,配合物1对牛血清白蛋白的荧光猝灭为静态猝灭过程,它与牛血清白蛋白的相互作用有一个位点,结合常数的平均值5.06×105L·mol-1,作用距离为2.35nm,相互作用力表现为氢键和范德华力。 |
| 关键词: 牛血清白蛋白 荧光光谱 乳酸 邻菲咯啉 镍配合物 |
| 基金项目: 国家自然科学基金(No.21073150)资助项目。 |
| Abstract: The compound [Ni(Hlact)2(phen)]·2H2O is synthesized in the solution and fully characterized by elemental analysis, IRand X-ray structural analyses. The interaction of Bovine Serum Albumin (BSA) and [Ni(Hlact)2(phen)]·2H2O at different temperatures are investigated with fluorescence spectra. The binding constant, binding sites and thermodynamic functions are calculated at different temperatures. The binding force and distance are discussed for BSA with complex 1. In the result, the model of fluorescence quenching is considered as static quenching process based on Stern-Volmer equation. The binding constant and binding sites are calculated for BSA and [Ni(Hlact)2(phen)]·2H2O as 5.06×105 L·mol-1 and 2.35nm respectively. Parameters of thermodynamic functions are calculated and the interaction is determined as hydrogen bonding and van der Waal interactions between BSA and complex. CCDC: 897985. |
| Keywords: bovine serum albumin (BSA) fluorescence spectrum lactic acid phenanthroline nickel complex |
| 投稿时间：2012-08-26 修订日期：2013-02-03 |
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| 林海彬,张美鑫,林凉凉,周朝晖.邻菲咯啉乳酸镍配合物的合成与表征及其与牛血清白蛋白相互作用的荧光分析[J].无机化学学报,2013,29(11):2315-2322. |
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