Fluorescence Spectroscopic Studies of Interaction between 4-Aminobenzenesulfonic Acid and Bovine Serum Albumin

Abstract:

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The interaction between 4-aminobenzenesulfonic acid and bovine serum albumin (BSA) had been studied by fluorescence spectroscopy. The binding constant (K=2.51×104) and binding points (n=0.998) of 4-aminobenzenesulfonic acid with BSA 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 4-aminobenzenesulfonic acid-BSA complexes showed that van der Waals interactions and hydrogen bonds might play a major role in the binding of 4-aminobenzenesulfonic acid to BSA. The distance, r, between donor (BSA) and acceptor (4-aminobenzenesulfonic acid) was obtained according to the Förster’s theory of non-radiation energy transfer. The results of synchronous fluorescence spectra revealed that 4-aminobenzenesulfonic acid induced conformational change of BSA.

Info:

Periodical:

Advanced Materials Research (Volumes 233-235)

Edited by:

Zhong Cao, Lixian Sun, Xueqiang Cao, Yinghe He

Pages:

2619-2623

DOI:

10.4028/www.scientific.net/AMR.233-235.2619

Citation:

J. L. Liu et al., "Fluorescence Spectroscopic Studies of Interaction between 4-Aminobenzenesulfonic Acid and Bovine Serum Albumin", Advanced Materials Research, Vols. 233-235, pp. 2619-2623, 2011

Online since:

May 2011

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Price:

$35.00

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