NDLI: Study of in vitro interaction between tetrabromobisphenol A and bovine serum albumin by fluorescence spectroscopy.

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Study of in vitro interaction between tetrabromobisphenol A and bovine serum albumin by fluorescence spectroscopy.

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Study of in vitro interaction between tetrabromobisphenol A and bovine serum albumin by fluorescence spectroscopy.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Wu, Yingxin Qian, Yan Cui, Hao Lai, Xiaomin Xie, Xianchuan Wang, Xiaorong
Description	Author Affiliation: Wu Y ( State Key Laboratory of Pollution Control and Resource Reuse, Nanjing University, Nanjing, People's Republic of China.)
Abstract	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 310 K were obtained as 4.75 × 10(5) L/mol, 5.63 × 10(5) L/mol, and 6.66 × 10(5) L/mol, respectively. There may be two binding sites of TBBPA on BSA. The enthalpy change (ΔH), free energy change (ΔG), and entropy change (ΔS) 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.
File Format	HTM / HTML
ISSN	07307268
Issue Number	12
Volume Number	30
e-ISSN	15528618
Journal	Environmental Toxicology and Chemistry
Language	English
Publisher	Wiley
Publisher Date	2011-12-01
Publisher Place	United States
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Research Support, Non-u.s. Gov't Environmental Monitoring Environmental Pollutants Discipline Environmental Health Molecular Conformation Fluorescence Spectrometry, Fluorescence Discipline Toxicology Entropy Journal Article Thermodynamics Chemistry Animals Serum Albumin, Bovine Cattle Analysis Hydrophobic And Hydrophilic Interactions Protein Binding Discipline Chemistry Polybrominated Biphenyls Binding Sites
Content Type	Text
Resource Type	Article
Subject	Environmental Chemistry Health, Toxicology and Mutagenesis

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