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生物活性咪唑与牛血清白蛋白结合相互作用的荧光研究-静态猝灭机制。

Luminescent study on the binding interaction of bioactive imidazole with bovine serum albumin-A static quenching mechanism.

机构信息

Department of Chemistry, Annamalai University, Annamalainagar 608 002, India.

出版信息

Spectrochim Acta A Mol Biomol Spectrosc. 2011 Dec 15;84(1):233-7. doi: 10.1016/j.saa.2011.09.033. Epub 2011 Sep 20.

DOI:10.1016/j.saa.2011.09.033
PMID:21993253
Abstract

Novel bioactive imidazole derivatives were synthesized and characterized by NMR spectra, mass and CHN analysis. The interaction between the imidazole derivative and bovine serum albumin (BSA) was investigated by fluorescence and UV-vis absorption spectroscopy. The fluorescence quenching of BSA by the imidazole derivatives may be due to the formation of imidazole-BSA complex. The fluorescence quenching mechanism of BSA by imidazole was analyzed and the binding constant has been calculated. The binding distance between imidazole and BSA was obtained based on Forester's non-radiation energy transfer (FRET). The effect of some common ions on the binding constant between imidazole and BSA was also examined.

摘要

新型生物活性咪唑衍生物通过 NMR 光谱、质谱和 CHN 分析进行了合成和表征。通过荧光和紫外-可见吸收光谱研究了咪唑衍生物与牛血清白蛋白(BSA)的相互作用。BSA 被咪唑衍生物的荧光猝灭可能是由于形成了咪唑-BSA 复合物。分析了咪唑对 BSA 的荧光猝灭机制,并计算了结合常数。基于福斯特的非辐射能量转移(FRET)获得了咪唑与 BSA 之间的结合距离。还研究了一些常见离子对咪唑与 BSA 之间结合常数的影响。

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