NDLI: Investigation on the interaction between 3, 5-dihydroxytoluene and bovine serum albumin by fluorescence spectroscopy

Content Provider	IEEE Xplore Digital Library
Author	Xiang-Yu Cao Jian-Li Liu Tie-Min Li Jiang-Bei Yuan Cheng-Bin Xu Xiu-Juan Hui Dian-Bo Dong Meng Zeng
Copyright Year	2011
Description	Author affiliation: Liaoning Academy of Environmental Sciences, China (Dian-Bo Dong) \|\| School of Environment science, Liaoning University, Shenyang, China (Cheng-Bin Xu; Xiu-Juan Hui) \|\| School of life science, Liaoning University, Shenyang, China (Xiang-Yu Cao; Jian-Li Liu; Tie-Min Li; Jiang-Bei Yuan) \|\| Tianjin Academy of Environmental Sciences, China (Meng Zeng)
Abstract	The interaction between 3, 5-dihydroxytoluene and bovine serum albumin (BSA) had been investigated by fluorescence spectroscopy. By the analysis of fluorescence spectrum and fluorescence intensity, it was observed that the 3, 5-dihydroxytoluene had a strong ability to quench the intrinsic fluorescence of BSA through a static quenching procedure. The binding constant and the number of binding sites were determined at 298 K based on fluorescence quenching results. The thermodynamic parameters such as enthalpy change (ΔH), entropy change (ΔS) and Gibbs free-energy change (ΔG) for the reactions were also calculated according to the thermodynamic equations. The negative ΔH and ΔS values in case of 3, 5-dihydroxytoluene-BSA complexes showed that van der Waals interactions and hydrogen bonds might play a major role in the binding of 3, 5-dihydroxytoluene to BSA. The distance, r, between donor (BSA) and acceptor (3, 5-dihydroxytoluene) was obtained according to the Förster's theory of non-radiation energy transfer. The experimental results of synchronous fluorescence spectroscopy showed that the binding of 3, 5-dihydroxytoluene to BSA induced conformational changes in BSA.
Starting Page	679
Ending Page	683
File Size	106097
Page Count	5
File Format	PDF
ISBN	9781612847016
e-ISBN	9781612847047
DOI	10.1109/ITiME.2011.6130752
Language	English
Publisher	Institute of Electrical and Electronics Engineers, Inc. (IEEE)
Publisher Date	2011-12-09
Publisher Place	China
Access Restriction	Subscribed
Rights Holder	Institute of Electrical and Electronics Engineers, Inc. (IEEE)
Subject Keyword	Proteins Fluorescence spectroscopy Spectroscopy Thermodynamics Absorption Bovine Energy exchange Interaction Fluorescence 3, 5-dihydroxytoluene Bovine serum albumin (BSA)
Content Type	Text
Resource Type	Article

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