期刊
JOURNAL OF PHARMACEUTICAL AND BIOMEDICAL ANALYSIS
卷 49, 期 3, 页码 753-759出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.jpba.2008.12.017
关键词
Mangiferin; Human serum albumin; CD spectroscopy; FT-IR spectroscopy; Molecular modeling
The interactions between mangiferin and human serum albumin (HSA) were investigated by spectroscopy and molecular modeling. The results proved the formation of complex between mangiferin and HSA. Hydrophobic interaction dominated in the association reaction. Mangiferin statically quenched the fluorescence of HSA in a concentration dependent manner positively deviating from the linear Scatchard equation. The binding of mangiferin to HSA lead to changes in the conformation of HSA according to synchronous fluorescence spectra, FT-IR, UV-vis and CID data. The presence of amino acids and metal ion affected the binding constant of mangiferin-HSA complex. Computational mapping of the possible binding sites of mangiferin revealed the molecule to be bound in the large hydrophobic cavity of subdomain IIA. (C) 2008 Elsevier B.V. All rights reserved.
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