期刊
ANALYTICAL SCIENCES
卷 27, 期 1, 页码 79-84出版社
JAPAN SOC ANALYTICAL CHEMISTRY
DOI: 10.2116/analsci.27.79
关键词
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资金
- National Natural Science Foundation of China [31060044]
- Foundation of Yunnan Province [2009ZC046M]
- National Foundation of Innovative Experiment for College Student of China [091067444]
The binding properties on alizarin to human serum albumin (HSA) have been studied for the first time using fluorescence spectroscopy in combination with UV-visible absorbance spectroscopy. The results showed that alizarin strongly quenched the intrinsic fluorescence of HSA through a static quenching procedure, and non-radiation energy transfer occurred within the molecules. The number of binding sites was I, and the efficiency of Forster energy transfer provided a distance of 1.83 nm between tryptophan and alizarin binding site. Delta H-theta, Delta S-theta and Delta G(theta) were obtained based on the quenching constants and thermodynamic theory (Delta H-theta < 0, Delta S-theta > 0 and Delta G(theta) < 0). These results indicated that hydrophobic and electrostatic interactions are the main binding forces in the alizarin-HSA system. In addition, the results obtained from synchronous fluorescence spectra and three-dimensional fluorescence spectra showed that the binding of alizarin with HSA could induce conformational changes in HSA.
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