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The investigation of the interaction between edaravone and bovine serum albumin by spectroscopic approaches

Journal Article:

Abstract

The fluorescence and ultraviolet spectroscopies were explored to study the interaction between edaravone (EDA) and bovine serum albumin (BSA) under imitated physiological condition. The experimental results show that the fluorescence quenching mechanism between EDA and BSA is a combined quenching (dynamic and static quenching). The binding constants, binding sites, and the corresponding thermodynamic parameters ({Delta}G, {Delta}H, and {Delta}S) of the interaction system were calculated at different temperatures. According to Foerster non-radiation energy transfer theory, the binding distance between EDA and BSA was calculated to be 3.10 nm. The effect of EDA on the conformation of BSA was analyzed using synchronous fluorescence spectroscopy. In addition, the effects of some common metal ions Mg{sup 2+}, Ca{sup 2+}, Cu{sup 2+}, and Ni{sup 2+} on the binding constant between EDA and BSA were examined. - Highlights: {yields} We explored the interaction of BSA and EDA using spectroscopic methods. {yields} The fluorescence quenching mechanism is combined quenching. {yields} Hydrophobic interaction force plays a major role in stabilizing the complex. {yields} The binding constants, binding sites, and thermodynamic parameters were calculated. {yields} EDA affects the conformation of tryptophan residue's microregion.
Authors:
Xianyong, Yu; Ying, Yang; Ronghua, Liu; Haowen, Huang; Jian, Chen; Danhong, Ji; [1]  Li Xiaofang, E-mail: fine_chem@163.co; [1]  Fengxian, Yang; [1]  Yi Pinggui, E-mail: pgyi@hnust.c [1] 
  1. Key Laboratory of Theoretical Chemistry and Molecular Simulation of Ministry of Education, Hunan Province College Key Laboratory of QSAR/QSPR, School of Chemistry and Chemical Engineering, Hunan University of Science and Technology, Xiangtan 411201 (China)
Publication Date:
Jul 15, 2011
Product Type:
Journal Article
Resource Relation:
Journal Name: Journal of Luminescence; Journal Volume: 131; Journal Issue: 7; Other Information: DOI: 10.1016/j.jlumin.2011.03.051; PII: S0022-2313(11)00159-1; Copyright (c) 2011 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved.
Subject:
37 INORGANIC, ORGANIC, PHYSICAL AND ANALYTICAL CHEMISTRY; ALBUMINS; CALCIUM IONS; CATTLE; COPPER IONS; ENERGY TRANSFER; FLUORESCENCE; FLUORESCENCE SPECTROSCOPY; INTERACTIONS; MAGNESIUM IONS; NICKEL IONS; QUENCHING; TRYPTOPHAN; ULTRAVIOLET RADIATION; AMINO ACIDS; ANIMALS; AROMATICS; AZAARENES; AZOLES; CARBOXYLIC ACIDS; CHARGED PARTICLES; DOMESTIC ANIMALS; ELECTROMAGNETIC RADIATION; EMISSION; EMISSION SPECTROSCOPY; HETEROCYCLIC ACIDS; HETEROCYCLIC COMPOUNDS; INDOLES; IONS; LUMINESCENCE; MAMMALS; ORGANIC ACIDS; ORGANIC COMPOUNDS; ORGANIC NITROGEN COMPOUNDS; PHOTON EMISSION; PROTEINS; PYRROLES; RADIATIONS; RUMINANTS; SPECTROSCOPY; VERTEBRATES
OSTI ID:
21493911
Country of Origin:
Netherlands
Language:
English
Other Identifying Numbers:
Journal ID: ISSN 0022-2313; JLUMA8; TRN: NL11R2624085643
Availability:
Available from http://dx.doi.org/10.1016/j.jlumin.2011.03.051
Submitting Site:
NLN
Size:
page(s) 1510-1514
Announcement Date:
Nov 07, 2011

Journal Article:

Citation Formats

Xianyong, Yu, Ying, Yang, Ronghua, Liu, Haowen, Huang, Jian, Chen, Danhong, Ji, Li Xiaofang, E-mail: fine_chem@163.co, Fengxian, Yang, and Yi Pinggui, E-mail: pgyi@hnust.c. The investigation of the interaction between edaravone and bovine serum albumin by spectroscopic approaches. Netherlands: N. p., 2011. Web.
Xianyong, Yu, Ying, Yang, Ronghua, Liu, Haowen, Huang, Jian, Chen, Danhong, Ji, Li Xiaofang, E-mail: fine_chem@163.co, Fengxian, Yang, & Yi Pinggui, E-mail: pgyi@hnust.c. The investigation of the interaction between edaravone and bovine serum albumin by spectroscopic approaches. Netherlands.
Xianyong, Yu, Ying, Yang, Ronghua, Liu, Haowen, Huang, Jian, Chen, Danhong, Ji, Li Xiaofang, E-mail: fine_chem@163.co, Fengxian, Yang, and Yi Pinggui, E-mail: pgyi@hnust.c. 2011. "The investigation of the interaction between edaravone and bovine serum albumin by spectroscopic approaches." Netherlands.
@misc{etde_21493911,
title = {The investigation of the interaction between edaravone and bovine serum albumin by spectroscopic approaches}
author = {Xianyong, Yu, Ying, Yang, Ronghua, Liu, Haowen, Huang, Jian, Chen, Danhong, Ji, Li Xiaofang, E-mail: fine_chem@163.co, Fengxian, Yang, and Yi Pinggui, E-mail: pgyi@hnust.c}
abstractNote = {The fluorescence and ultraviolet spectroscopies were explored to study the interaction between edaravone (EDA) and bovine serum albumin (BSA) under imitated physiological condition. The experimental results show that the fluorescence quenching mechanism between EDA and BSA is a combined quenching (dynamic and static quenching). The binding constants, binding sites, and the corresponding thermodynamic parameters ({Delta}G, {Delta}H, and {Delta}S) of the interaction system were calculated at different temperatures. According to Foerster non-radiation energy transfer theory, the binding distance between EDA and BSA was calculated to be 3.10 nm. The effect of EDA on the conformation of BSA was analyzed using synchronous fluorescence spectroscopy. In addition, the effects of some common metal ions Mg{sup 2+}, Ca{sup 2+}, Cu{sup 2+}, and Ni{sup 2+} on the binding constant between EDA and BSA were examined. - Highlights: {yields} We explored the interaction of BSA and EDA using spectroscopic methods. {yields} The fluorescence quenching mechanism is combined quenching. {yields} Hydrophobic interaction force plays a major role in stabilizing the complex. {yields} The binding constants, binding sites, and thermodynamic parameters were calculated. {yields} EDA affects the conformation of tryptophan residue's microregion.}
journal = {Journal of Luminescence}
issue = {7}
volume = {131}
place = {Netherlands}
year = {2011}
month = {Jul}
}