期刊
SPECTROCHIMICA ACTA PART A-MOLECULAR AND BIOMOLECULAR SPECTROSCOPY
卷 75, 期 3, 页码 1130-1137出版社
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.saa.2009.12.071
关键词
Biphenol A; Lysozyme; Trypsin; Fluorescence spectroscopy
类别
资金
- Fund for Excellent Innovation Team of Jiangsu Provincial Department of Education [2009-23]
- National Natural Science Foundation of China [30570218]
- Natural Science Foundation of Education Department of Jiangsu Province [07KJA18017]
- Educational Bureau [09KJD150007]
- Qilan Project
- 333 Project
- Scientific Foundation of Yancheng Teachers University
The interaction between bisphenol A (BPA) and lysozyme (or trypsin) was investigated by UV-vis absorption, fluorescence. synchronous fluorescence, and three-dimensional fluorescence spectra techniques under physiological pH 7.40. BPA effectively quenched the intrinsic fluorescence of lysozyme and trypsin via static quenching. H-bonds and van der Waals interactions played a major role in stabilizing the BPA-protemase complex. The distance r between donor and acceptor was obtained to be 1.65 and 2.26 nm for BPA-lysozyme and BPA-trypsin complexes, respectively. The effect of BPA on the conformation of lysozyme and trypsin was analyzed using synchronous fluorescence and three-dimensional fluorescence spectra. (C) 2010 Elsevier B.V. All rights reserved.
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