NDLI: Study of the interaction between mercury (II) and bovine serum albumin by spectroscopic methods.

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Study of the interaction between mercury (II) and bovine serum albumin by spectroscopic methods.

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Study of the interaction between mercury (II) and bovine serum albumin by spectroscopic methods.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Chunmei, Dai Cunwei, Ji Huixiang, Lan Yuze, Song Wei, Yang Dan, Zheng
Description	Author Affiliation: Chunmei D ( Liaoning Medical University, Jinzhou 121001, PR China.); Cunwei J ( Key Laboratory of Environment and Health, Ministry of Education & Ministry of Environmental Protection, and State Key Laboratory of Environmental Health (Incubating) School of Public Health, Tongji Medical College, Huazhong University of Science and Technology, Wuhan 430030, PR China.); Huixiang L ( Key Laboratory of Environment and Health, Ministry of Education & Ministry of Environmental Protection, and State Key Laboratory of Environmental Health (Incubating) School of Public Health, Tongji Medical College, Huazhong University of Science and Technology, Wuhan 430030, PR China.); Yuze S ( Liaoning Medical University, Jinzhou 121001, PR China.); Wei Y ( Liaoning Medical University, Jinzhou 121001, PR China.); Dan Z ( Key Laboratory of Environment and Health, Ministry of Education & Ministry of Environmental Protection, and State Key Laboratory of Environmental Health (Incubating) School of Public Health, Tongji Medical College, Huazhong University of Science and Technology, Wuhan 430030, PR China. Electronic)
Abstract	Mercury is a significant environmental pollutant that originates from industry. Mercury will bind with albumin and destroy biological functions in humans if it enters the blood. In this paper, the interaction between mercury (II) and bovine serum albumin (BSA) was investigated in vitro by fluorescence, UV-Vis absorption and circular dichroism (CD) under simulated physiological conditions. This study proves that the probable quenching mechanism of BSA by mercury (II) was mainly static quenching due to the formation of a mercury (II)-BSA complex. The quenching constant K(a) and the corresponding thermodynamic parameters (ΔH, ΔS and ΔG) at four different temperatures were calculated by a modified Stern-Volmer equation and the van't Hoff equation, respectively. The results revealed that the interaction between mercury (II) and BSA was mainly enthalpy-driven and that hydrogen bonding and van der Waals forces played a major role in the reaction. The obtained data for binding sites of n approximately equal to 1 indicated that there was a single class of binding site for the BSA with mercury (II). The value of the distance r (3.55 nm), determined by Föster's non-radioactive energy transfer theory, suggested that the energy transfer from BSA to mercury (II) occurred with a high probability. The conformational investigation from synchronous fluorescence, CD spectroscopy and three-dimensional fluorescence showed that the presence of mercury (II) resulted in micro-environmental and conformational changes of the BSA molecules, which may be responsible for the toxicity of mercury (II) in vivo.
File Format	HTM / HTML
ISSN	13826689
Issue Number	2
Volume Number	37
e-ISSN	18727077
Journal	Environmental Toxicology and Pharmacology
Language	English
Publisher	Elsevier
Publisher Date	2014-03-01
Publisher Place	Netherlands
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Discipline Environmental Health Discipline Pharmacology Environmental Pollutants Metabolism Mercury Serum Albumin, Bovine Binding Sites Circular Dichroism Protein Binding Protein Conformation Spectrometry, Fluorescence Spectrophotometry, Ultraviolet Thermodynamics Journal Article Research Support, Non-u.s. Gov't
Content Type	Text
Resource Type	Article
Subject	Health, Toxicology and Mutagenesis Medicine Toxicology Pharmacology

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