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内蒙古大学 化学化工学院,内蒙古 呼和浩特,010021
收稿日期:2010-11-06,
修回日期:2010-12-24,
网络出版日期:2011-04-22,
纸质出版日期:2011-04-22
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敖登高娃, 金迎春. 芬布芬与牛血清白蛋白相互作用的荧光光谱检测[J]. 发光学报, 2011,32(4): 404-410
AODENG Gaowa, JIN Ying-chun. Spectroscopic Studies on The Interaction Between Fenbufen and Bovine Serum Albumin[J]. Chinese Journal of Luminescence, 2011,32(4): 404-410
敖登高娃, 金迎春. 芬布芬与牛血清白蛋白相互作用的荧光光谱检测[J]. 发光学报, 2011,32(4): 404-410 DOI: 10.3788/fgxb20113204.0404.
AODENG Gaowa, JIN Ying-chun. Spectroscopic Studies on The Interaction Between Fenbufen and Bovine Serum Albumin[J]. Chinese Journal of Luminescence, 2011,32(4): 404-410 DOI: 10.3788/fgxb20113204.0404.
在模拟生理条件下
用荧光光谱法和紫外-可见吸收光谱法研究芬布芬(FBF)和牛血清白蛋白(BSA)结合反应的特征。研究表明:芬布芬与牛血清白蛋白形成复合物
从而猝灭牛血清白蛋白的内源性荧光
该过程为静态猝灭过程。根据Stern-Vlmer方程得出了不同温度下结合位点数和结合常数;根据Frster非辐射能量转移理论得出了不同温度下的作用距离;通过计算相应的热力学参数
确定了芬布芬与牛血清白蛋白之间的作用力主要为静电引力。利用同步荧光光谱及三维荧光光谱法探讨了芬布芬与牛血清白蛋白作用前后白蛋白的构型变化
以及共存金属离子对芬布芬与牛血清白蛋白结合常数的影响。
The interaction between Fenbufen and bovine serum albumin(BSA) was studied with fluorescence spectra and UV-visible absorption spectra in the presence of simulating physiological systems.It showed that the complex formated by BSA and Fenbufen lead to the static quenching of the intrinsic fluorescence of BSA. The binding site number n and apparent binding constant
K
A
were measured according to Stern-Volmer equation.The distance between BSA and Fenbufen was obtained based on the Frster nonradiative energy transfer theory. We also confirmed that the main sorts of binding force between Fenbufen and BSA is electrostatic force. Meanwhile
synchronous fluorescence and three-dimensional fluorescence spectra were used to investigate the structure change of BSA before and after the introduction of Fenbufen.Furthermore
the effect of coexistence metal ions on the binding constants of Fenbufen with BSA was also discussed.
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