Studies on the interaction between imidacloprid and human serum albumin: Spectroscopic approach

被引:143
|
作者
Wang Yan-qing [1 ,2 ]
Tang Bo-ping [1 ]
Zhang Hong-mei [2 ]
Zhou Qiu-hua [2 ]
Zhang Gen-cheng [2 ]
机构
[1] Jiangsu Prov Key Lab Coastal Werland Bioresources, Yancheng City 224002, Jiangsu Prov, Peoples R China
[2] Yancheng Teachers Coll, Inst Appl Chem & Environm Engn, Yancheng City 224002, Jiangsu Prov, Peoples R China
关键词
Imidacloprid; Human serum albumin; Fluorescence spectroscopy; Thermodynamic parameter; TRAZODONE HYDROCHLORIDE; BINDING; FLUORESCENCE; ACID; THERMODYNAMICS; DERIVATIVES; ABSORPTION; COLCHICINE;
D O I
10.1016/j.jphotobiol.2008.11.013
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
收藏
页码:183 / 190
页数:8
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