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Investigation of the interaction between chlorophenols and lysozyme in solution

Paper ID Volume ID Publish Year Pages File Format Full-Text
30846 44508 2011 9 PDF Available
Title
Investigation of the interaction between chlorophenols and lysozyme in solution
Abstract

The binding interactions of lysozyme with 2-chlorophenol, 2,4-dichlorophenol, 2,4,6-trichlorophenol and pentachlorophenol were investigated by UV–vis absorption, CD, fluorescence, synchronous fluorescence, and three-dimensional fluorescence spectra techniques under physiological pH 7.40. The binding constants, quenching mechanism, and the number of binding sites were determined by the quenching of lysozyme fluorescence in presence of chlorophenols. H-bonds and hydrophobic interactions played major roles in stabilizing the chlorophenols–lysozyme complex. The distances r between chlorophenols and lysozyme were calculated to be 1.94 nm, 2.75 nm, 3.54 nm, and 3.76 nm for 2-CP, 2,4-DCP, 2,4,6-TCP, and PCP, respectively. The effects of chlorophenols on the conformation of lysozyme were analyzed using CD, synchronous fluorescence and three-dimensional fluorescence spectra.

► This is the first report on the interaction of chlorophenols with lysozyme by fluorescence spectra techniques. ► The number of –Cl partly effected the binding ability of chlorophenols with lysozyme. ► The H-bonds and hydrophobic interactions played major roles in stabilizing the chlorophenols–lysozyme complex. ► The calculated distance r of chlorophenols–lysozyme system may place chlorophenols at the interface of protein.

Keywords
Chlorophenols; Lysozyme; Fluorescence; Interaction
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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Photochemistry and Photobiology B: Biology - Volume 104, Issue 3, 2 September 2011, Pages 405–413
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
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Price was $35.95
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