Investigation of the interactions of lysozyme and trypsin with biphenol A using spectroscopic methods

被引：66
作者：
Wang, Yan-Qing [1 ,2 ]
Chen, Ting-Ting [3 ]
Zhang, Hong-Mei [1 ,2 ]
机构：
[1] Yancheng Teachers Univ, Dept Chem, Inst Appl Chem & Environm Engn, Yancheng City 224002, Jiangsu Prov, Peoples R China
[2] Jiangsu Prov Key Lab Coastal Wetland Bioresources, Yancheng City 224002, Jiangsu Prov, Peoples R China
[3] Nantong Univ, Sch Chem & Chem Engn, Nantong 226019, Peoples R China
来源：
SPECTROCHIMICA ACTA PART A-MOLECULAR AND BIOMOLECULAR SPECTROSCOPY | 2010年 / 75卷 / 03期
基金：
中国国家自然科学基金;
关键词：
Biphenol A; Lysozyme; Trypsin; Fluorescence spectroscopy; HUMAN SERUM-ALBUMIN; BISPHENOL-A; IN-VITRO; FLUORESCENCE; BINDING; ESTROGENICITY; METHYL; PROBE; WATER;
D O I：
10.1016/j.saa.2009.12.071
中图分类号：
O433 [光谱学];
学科分类号：
0703 ; 070302 ;
摘要：
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.
引用
收藏
页码：1130 / 1137
页数：8
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