Fluorescence spectroscopic investigation of the interaction between chloramphenicol and lysozyme

被引：111

作者：

Ding, Fei ^{[1
]}

Zhao, Guangyu ^{[1
]}

Huang, Jinli ^{[1
]}

Sun, Ying ^{[1
]}

Zhang, Li ^{[1
]}

机构：

[1] China Agr Univ, Dept Chem, Beijing 100193, Peoples R China

来源：

EUROPEAN JOURNAL OF MEDICINAL CHEMISTRY | 2009年 / 44卷 / 10期

关键词：

Chloramphenicol; Lysozyme; Fluorescence spectroscopy; Circular dichroism; Fluorescence resonance energy transfer; HUMAN SERUM-ALBUMIN; EGG-WHITE LYSOZYME; CIRCULAR-DICHROISM; BINDING; COMPLEXATION; COMPONENTS; MECHANISM; SPECTRA; OXYGEN;

D O I：

10.1016/j.ejmech.2009.04.047

中图分类号：

R914 [药物化学];

学科分类号：

100701 ;

摘要：

The interactions between chloramphenicol and lysozyme were studied using fluorescence, UV/vis and circular dichroism spectra. The results proved the mechanism of fluorescence quenching of lysozyme by chloramphenicol is due to the formation of lysozyme-chloramphenicol complex. The thermodynamic parameters, enthalpy change (Delta H) and entropy change (AS) for the reaction, were calculated to be -12.41 kJ mol(-1) and 37.99 J mol(-1) K-1, which indicated that hydrophobic force and hydrogen bond were the dominant intermolecular forces in stabilizing the complex. The distance r = 3.99 nm between donor and acceptor was obtained according to Forster's theory. In addition, the alterations of lysozyme secondary structure in the presence of chloramphenicol were confirmed by the evidences from circular dichroism, synchronous and three-dimensional fluorescence spectroscopy. (C) 2009 Elsevier Masson SAS. All rights reserved.

引用

页码：4083 / 4089

页数：7

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