用热力学参数检测奥硝唑与白蛋白的相互作用

Esra Maltaş Çağıl
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引用次数: 0

摘要

采用荧光光谱和紫外可见光谱研究了1-氯-3-(2-甲基-5-硝基- 1h -咪唑-1-基)丙烯-2-醇(奥硝唑)与人血清白蛋白(HSA)的结合。利用Stern-Volmer方程和Van 't Hoff方程确定了奥硝唑(ornidazole, OR)与HSA的相互作用。通过几个方程计算不同温度下的结合常数Kb和热力学参数∆H、∆S、∆G。结果表明,奥硝唑对HSA的荧光猝灭机制可能是静态猝灭。热力学参数表明,范德华相互作用和氢键是奥硝唑与HSA相互作用的主要作用力。同步荧光光谱的变化表明,在结合过程中,OR的微环境和HSA的浓度构象都发生了变化。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Detection of interaction between ornidazole and albumin by using thermodynamic parameters
The binding of 1-chloro-3-(2-methyl-5-nitro-1H-imidazole-1-yl) propan-2-ol (Ornidazole) to human serum albumin (HSA) was studied by fluorescence and UV-visible spectroscopy. Interaction of ornidazole (OR) with HSA was identified by Stern-Volmer and Van’t Hoff equations. The binding constant, Kb and the thermodynamic parameters, ∆H, ∆S, and ∆G at different temperatures were calculated by several equations. Data shows that the fluorescence quenching mechanism of HSA with ornidazole may occur via static quenching. The thermodynamic parameters showed that van der Waals interactions and hydrogen bonds are the major forces for the interaction of ornidazole with HSA. The spectral changes of synchronous fluorescence suggested that both the microenvironment of OR and the conformation of HSA concerning their concentrations have changed during binding.   
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