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

共 45 条

[21] Interactions between hen egg-white lysozyme, PEG2,000, and PLA50 at the air-water interface [J].

Malzert-Fréon, A ;

Abillon, O ;

Proust, JE ;

Gref, R ;

Benoît, JP ;

Boury, F .

COLLOIDS AND SURFACES B-BIOINTERFACES, 2005, 42 (02) :97-106

[22] Metabolic barrier against bisphenol a in rat uterine endometrium [J].

Matsumoto, Junya ;

Iwano, Hidetomo ;

Inoue, Hiroki ;

Iwano, Naomi ;

Yamashiki, Naoko ;

Yokota, Hiroshi .

TOXICOLOGICAL SCIENCES, 2007, 99 (01) :118-125

[23] Surface plasmon resonance sensor for lysozyme based on molecularly imprinted thin films [J].

Matsunaga, Takateru ;

Hishiya, Takayuki ;

Takeuchi, Toshifumi .

ANALYTICA CHIMICA ACTA, 2007, 591 (01) :63-67

[24] Binding of the Promen fluorescent probe to human serum albumin -: A fluorescence spectroscopic study [J].

Moreno, F ;

González-Jiménez, J .

CHEMICO-BIOLOGICAL INTERACTIONS, 1999, 121 (03) :237-252

[25] Internal motion of lysozyme studied by time-resolved fluorescence depolarization of tryptophan residues [J].

Nishimoto, E ;

Yamashita, S ;

Szabo, AG ;

Imoto, T .

BIOCHEMISTRY, 1998, 37 (16) :5599-5607

[26] H-1 AND N-15 NMR-STUDY OF HUMAN LYSOZYME [J].

OHKUBO, T ;

TANIYAMA, Y ;

KIKUCHI, M .

JOURNAL OF BIOCHEMISTRY, 1991, 110 (06) :1022-1029

[27] Estrogenicity of resin-based composites and sealants used in dentistry [J].

Olea, N ;

Pulgar, R ;

Perez, P ;

OleaSerrano, F ;

Rivas, A ;

NovilloFertrell, A ;

Pedraza, V ;

Soto, AM ;

Sonnenschein, C .

ENVIRONMENTAL HEALTH PERSPECTIVES, 1996, 104 (03) :298-305

[28] H-1-NMR STUDIES OF HUMAN LYSOZYME - SPECTRAL ASSIGNMENT AND COMPARISON WITH HEN LYSOZYME [J].

REDFIELD, C ;

DOBSON, CM .

BIOCHEMISTRY, 1990, 29 (31) :7201-7214

[29] THERMODYNAMICS OF PROTEIN ASSOCIATION REACTIONS - FORCES CONTRIBUTING TO STABILITY [J].

ROSS, PD ;

SUBRAMANIAN, S .

BIOCHEMISTRY, 1981, 20 (11) :3096-3102

[30] Fluorescence resonance energy transfer (FRET) in chemistry and biology: Non-Forster distance dependence of the FRET rate [J].

Saini, S ;

Singh, H ;

Bagchi, B .

JOURNAL OF CHEMICAL SCIENCES, 2006, 118 (01) :23-35

← 1 2 3 4 5 →