期刊
JOURNAL OF LUMINESCENCE
卷 130, 期 11, 页码 2013-2021出版社
ELSEVIER
DOI: 10.1016/j.jlumin.2010.05.019
关键词
Bensulfuron-methyl; Human serum albumin; Fluorescence spectroscopy; Circular dichroism; Molecular modeling; Ligand binding
类别
资金
- China Agricultural University
Bensulfuron-methyl (BM) is a highly active sulfonylurea herbicide for use on paddy rice. Steady state fluorescence, UV/vis absorption, circular dichroism (CD), time-resolved fluorescence and molecular modeling methods have been exploited to determine the binding affinity and binding site of BM to human serum albumin (HSA). From the synchronous fluorescence, UV/vis, CD and three-dimensional fluorescence spectra, it was evident that the interaction between BM and HSA induced a conformational change in the protein. Steady state and time-resolved fluorescence data illustrates that the fluorescence quenching of HSA by BM was the formation of HSA-BM complex at 1:1 molar ratio. Site marker competitive experiments demonstrated that the binding of BM to HSA primarily took place in subdomain IIIA (Sudlow's site II), this corroborates the hydrophobic probe ANS displacement and molecular modeling results. Thermodynamic analysis displays hydrophobic, electrostatic and hydrogen bonds interactions are the major acting forces in stabilizing the HSA-BM complex. (C) 2010 Elsevier B.V. All rights reserved.
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