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

被引：67

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

页码：1130 / 1137

页数：8

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