Investigation of the binding sites and orientation of caffeine on human serum albumin by surface-enhanced Raman scattering and molecular docking

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• 作者：Weinan Wang ; Wei Zhang ; Yaokai Duan ; Yong Jiang ; Liangren Zhang ; Bing Zhao ; Pengfei Tu
• 关键词：Caffeine ; Human serum albumin ; Surface-enhanced Raman scattering ; Molecular docking
• 刊名：Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy
• 出版年：2013
• 出版时间：November, 2013
• 年：2013
• 卷：115
• 期：Complete
• 页码：57-63
• 全文大小：1959 K

文摘

Fluorescence, normal Raman and surface-enhanced Raman scattering (SERS) were introduced to explore the absorptive geometry of caffeine on Human Serum Albumin (HSA) at physiological condition. The molecular docking was also employed to make a better understanding of the interaction between caffeine and HSA as well as to elucidate the detailed information of the major binding site. The results showed that caffeine could bind to HSA via the hydrophobic force of aromatic stacking and the main binding group on caffeine could be the pyrimidine ring. In addition, a consecutive set of changes in the orientation of caffeine molecule had been demonstrated during the process of caffeine binding to HSA, and the primary binding site was considered to be a hydrophobic cavity formed by Leu198, Lys199, Ser202, Phe211, Trp214, Val344, Ser454 and Leu481 in domain II.