期刊
SPECTROCHIMICA ACTA PART A-MOLECULAR AND BIOMOLECULAR SPECTROSCOPY
卷 115, 期 -, 页码 57-63出版社
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.saa.2013.05.036
关键词
Caffeine; Human serum albumin; Surface-enhanced Raman scattering; Molecular docking
类别
资金
- National Natural Science Foundation of China [81172944]
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, Va1344, Ser454 and Leu481 in domain II. (C) 2013 Elsevier B.V. All rights reserved.
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