STUDY OF IN VITRO INTERACTION BETWEEN TETRABROMOBISPHENOL A AND BOVINE SERUM ALBUMIN BY FLUORESCENCE SPECTROSCOPY

被引：10

作者：

Wu, Yingxin ^{[1
,2
]}

Qian, Yan ^{[1
]}

Cui, Hao ^{[1
]}

Lai, Xiaomin ^{[1
]}

Xie, Xianchuan ^{[1
,3
]}

Wang, Xiaorong ^{[1
]}

机构：

[1] Nanjing Univ, State Key Lab Pollut Control & Resource Reuse, Nanjing 210008, Peoples R China

[2] Sun Yat Sen Univ, Sch Environm Sci & Engn, Guangzhou 510275, Guangdong, Peoples R China

[3] Chinese Acad Sci, Key Lab Soil Environm & Pollut Remediat, Nanjing, Peoples R China

来源：

ENVIRONMENTAL TOXICOLOGY AND CHEMISTRY | 2011年 / 30卷 / 12期

关键词：

Tetrabromobisphenol A; Bovine serum albumin; Fluorescence spectroscopy; BROMINATED FLAME RETARDANTS; POLYBROMINATED DIPHENYL ETHERS; BINDING; TOXICOKINETICS; EXPOSURE;

D O I：

10.1002/etc.676

中图分类号：

X [环境科学、安全科学];

学科分类号：

08 ; 0830 ;

摘要：

The interaction between tetrabromobisphenol A (TBBPA) and bovine serum albumin (BSA) in simulated physiological conditions (pH 7.4) was investigated by fluorescence spectroscopy. The results revealed that TBBPA caused the fluorescence quenching of BSA through a static quenching procedure. The binding constants (K) of TBBPA with BSA at 277, 298, and 310K were obtained as 4.75 x 10(5) L/mol, 5.63 x 10(5) L/mol, and 6.66 x 10(5) L/mol, respectively. There may be two binding sites of TBBPA on BSA. The enthalpy change (Delta H), free energy change (Delta G), and entropy change (Delta S) of thermodynamic parameters indicated that the interaction between TBBPA and BSA was driven mainly by hydrophobic and electrostatic forces. Synchronous fluorescence spectra showed TBBPA binding slightly changed the conformation of BSA by decreasing its polarity and increasing its hydrophobicity. The results of the present study may provide valuable information for studying the distribution and toxicity mechanisms of TBBPA in vivo. Environ. Toxicol. Chem. 2011;30:2697-2700. (C) 2011 SETAC

引用

页码：2697 / 2700

页数：4

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