引用本文:
吕茜茜, 高苏亚, 夏冬辉, 李华. 荧光光谱法研究双醋瑞因与人血清白蛋白的相互作用[J]. 应用化学,
2011, 28(7): 836-841.
doi:
10.3724/SP.J.1095.2011.00497
Citation: LV Qianqian, GAO Suya, XIA Donghui, LI Hua. Fluorescence Spectroscopy on the Interaction of Diacerein and Human Serum Albumin[J]. Chinese Journal of Applied Chemistry, 2011, 28(7): 836-841. doi: 10.3724/SP.J.1095.2011.00497
Citation: LV Qianqian, GAO Suya, XIA Donghui, LI Hua. Fluorescence Spectroscopy on the Interaction of Diacerein and Human Serum Albumin[J]. Chinese Journal of Applied Chemistry, 2011, 28(7): 836-841. doi: 10.3724/SP.J.1095.2011.00497
荧光光谱法研究双醋瑞因与人血清白蛋白的相互作用
摘要:
在模拟人体生理条件下(pH=7.40),采用荧光光谱法研究双醋瑞因与人血清白蛋白的相互作用。采用2种方法计算不同温度下其结合常数KA、结合位点数n,同时对2种计算方法进行了比较;并根据热力学参数确定了双醋瑞因与人血清白蛋白之间的作用力类型。根据Förster非辐射能量转移原理,确定了双醋瑞因与人血清白蛋白相互结合时供能体-受能体间的作用距离和能量转移效率,并用同步荧光光谱研究了双醋瑞因对人血清白蛋白构象的影响。结果表明,双醋瑞因与人血清白蛋白之间主要是以静态猝灭为主;结合距离r=2.88 nm,能量转移效率E=0.2738,二者主要凭借氢键和范德华力进行结合。
English
Fluorescence Spectroscopy on the Interaction of Diacerein and Human Serum Albumin
Abstract:
The interaction of diacerein with human serum albumin(HSA) in physiological solution was studied by fluorescence spectroscopy.The result shows that diacerein quenches the fluorescence of HSA in a static quenching mode.The binding equilibrium constant KA and numbers of binding site n at different temperatures were calculated using two methods,which were compared in the work.The thermodynamic parameters obtained from measured data showed that the binding of diacerein to HSA involved hydrogen bonding and van der Waals interactions.According to the theory of energy transfer,the binding distance(r=2.88 nm) and transfer efficiency of energy(E=0.273 8) between diacerein and HSA were determined.The effect of diacerein on the conformation of HSA was also analyzed by synchronous fluorescence spectrometry.
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Key words:
- diacerein
- / human serum albumin
- / fluorescence spectroscopy
- / interaction
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