期刊
JOURNAL OF PHOTOCHEMISTRY AND PHOTOBIOLOGY B-BIOLOGY
卷 162, 期 -, 页码 332-339出版社
ELSEVIER SCIENCE SA
DOI: 10.1016/j.jphotobiol.2016.07.005
关键词
Interaction; Butachlor; Herbicide; Pesticide; Bovine serum albumin (BSA); Spectroscopic method
资金
- Project of Science and Technology Department of Zhejiang Province [2012C37058]
- Key Innovation Team of Science and Technology in Zhejiang Province [2010R50018]
Butachlor is an effective herbicide to deal with undesired weeds selectively and is used at high levels in Asian countries. However, its interaction and impairment effect on BSA was still not clear. In this study, we investigated the interaction between butachlor and bovine serum albumin (BSA) by multi-spectroscopic methods including UV absorption, circular dichroism (CD) spectra, Fourier transform infrared (FTIR) spectra and fluorescence spectra under physiological conditions (pH = 7.4). The results revealed that there was a static quenching of BSA induced by butachlor stemmed from the formation of complex. Based on thermodynamic data, the interaction of butachlor with BSA was due to happen, and van der Waals force as well as hydrogen bond were the major forces contributed to the interaction. The binding constant K-b and number of binding site of butachlor with BSA were 5.158 x 10(5) and 1.372 at 303 K, respectively. The distance r between donor (BSA) and acceptor (butachlor) was 0.113 nm, obtained according to the Forster theory. The results revealed that butachlor induced conformational changes in BSA but the secondary structure of BSA was still retained. In addition, the microenvironment around chromophore residues of BSA, for example, tryptophan, changed as well, resulting from the formation of more hydrogen bonds. (C) 2016 Elsevier B.V. All rights reserved.
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