Journal
JOURNAL OF MOLECULAR STRUCTURE
Volume 881, Issue 1-3, Pages 132-138Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.molstruc.2007.09.002
Keywords
icariin; human serum albumin; fluorescence spectroscopy; thermodynamic parameters; energy transfer
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The interaction between icariin and human serum albumin (HSA) in physiological buffer (pH 7.4) was investigated by fluorescence and UV-Vis absorption spectroscopy. Results obtained from analysis of fluorescence spectrum and fluorescence intensity indicated that icariin has a strong ability to quench the intrinsic fluorescence of HSA through a static quenching procedure. The thermodynamic parameters, Delta H-0 and Delta S-0 were calculated to be 12.29 kJ mol(-1) > 0, and 47.08 J mol(-1) K-1 > 0, respectively, which suggested that hydrophobic force plays a major role in the reaction of icariin with HSA. The binding constants of icariin with HSA were determined at different temperatures by fluorescence quenching method. The distance r between donor (HSA) and acceptor (icariin) was calculated to be 4.18 nm based on Forster's non-radiative energy transfer theory. The results of synchronous fluorescence spectra and three-dimensional fluorescence spectra showed that binding of icariin to HSA can induce conformational changes in HSA. (C) 2007 Elsevier B.V. All rights reserved.
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