期刊
JOURNAL OF PHOTOCHEMISTRY AND PHOTOBIOLOGY B-BIOLOGY
卷 94, 期 3, 页码 183-190出版社
ELSEVIER SCIENCE SA
DOI: 10.1016/j.jphotobiol.2008.11.013
关键词
Imidacloprid; Human serum albumin; Fluorescence spectroscopy; Thermodynamic parameter
资金
- Natural Science Foundation of Education Department of Jiangsu Province [07KJA18017]
- Educational Bureau [07KJD150235]
- Jiangsu Fundament
- Scientific Foundation of Yancheng Teachers University
The interaction between imidacloprid (IMI) and human serum albumin (HSA) was investigated using fluorescence and UV/vis absorption spectroscopy. The experimental results showed that the fluorescence quenching of HSA by IMI was a result of the formation of IMI-HSA complex; static quenching was confirmed to result in the fluorescence quenching. The apparent binding constant K-A between IMI and HSA at three differences were obtained to be 1.51 x 10(4), 1.58 x 10(4), and 2.19 x 10(4) L mol(-1), respectively. The thermodynamic parameters, Delta H degrees and Delta S degrees were estimated to be 28.44 kJ mol(-1), 174.76 J mol(-1) K-1 according to the van't Hoff equation. Hydrophobic interactions played a major role in stabilizing the complex. The distance r between donor (HSA) and acceptor (IMI) was obtained according to fluorescence resonance energy transfer. The effect of IMI on the conformation of HSA was analyzed using synchronous fluorescence spectroscopy CD and three-dimensional fluorescence spectra, the environment around Trp and Tyr residues were altered. (C) 2008 Elsevier B.V. All rights reserved.
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