caa a22 4500 445328576 CHVBK 20180317142729.0 cr unu---uuuuu 170323e20110501xx s 000 0 eng 10.1007/s10953-011-9684-4 doi (NATIONALLICENCE)springer-10.1007/s10953-011-9684-4 Study of the Binding of Herbacetin to Bovine Serum Albumin by Fluorescence Spectroscopy [Elektronische Daten] [Shuya Cui, Xiaoli Hu, Jiaqin Liu] In this paper, the interaction between herbacetin and BSA was investigated by fluorescence and three-dimensional fluorescence spectroscopy under simulated physiological conditions. It was proved that the fluorescence quenching of BSA by herbacetin was mainly the result of the formation of a herbacetin-BSA complex. The modified Stern-Volmer quenching constant and the corresponding thermodynamic parameters ΔH 0, ΔG 0 and ΔS 0 were calculated at different temperatures. The results indicated that electrostatic interactions were the predominant intermolecular forces in stabilizing the complex. The distance r=3.23nm between the donor (BSA) and acceptor (herbacetin) was obtained according to Förster's nonradioactive energy transfer theory. The synchronous fluorescence and three-dimensional fluorescence spectra results showed that the hydrophobity of amino acid residues increased in the presence of herbacetin. These results revealed that the microenvironment and conformation of BSA changed during the binding reaction. Springer Science+Business Media, LLC, 2011 Herbacetin nationallicence Binding nationallicence Bovine serum albumin nationallicence Fluorescence nationallicence Cui Shuya College of Chemistry and Chemical Engineering, Mianyang Normal University, 621000, Mianyang, P.R. China aut Hu Xiaoli College of Chemistry and Chemical Engineering, Mianyang Normal University, 621000, Mianyang, P.R. China aut Liu Jiaqin School of Physics and Chemistry, Xihua University, 6100039, Chengdu, P.R. China aut Journal of Solution Chemistry Springer US; http://www.springer-ny.com 40/5(2011-05-01), 764-774 0095-9782 40:5<764 2011 40 10953 https://doi.org/10.1007/s10953-011-9684-4 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s10953-011-9684-4 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Cui Shuya College of Chemistry and Chemical Engineering, Mianyang Normal University, 621000, Mianyang, P.R. China aut NATIONALLICENCE 700 1- Hu Xiaoli College of Chemistry and Chemical Engineering, Mianyang Normal University, 621000, Mianyang, P.R. China aut NATIONALLICENCE 700 1- Liu Jiaqin School of Physics and Chemistry, Xihua University, 6100039, Chengdu, P.R. China aut NATIONALLICENCE 773 0- Journal of Solution Chemistry Springer US; http://www.springer-ny.com 40/5(2011-05-01), 764-774 0095-9782 40:5<764 2011 40 10953 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer