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首页> 外文期刊>Spectrochimica acta, Part A. Molecular and biomolecular spectroscopy >Binding analysis of farrerol to lysozyme by spectroscopic methods
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Binding analysis of farrerol to lysozyme by spectroscopic methods

机译：光谱法分析法瑞洛尔与溶菌酶的结合

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Binding of farrerol to lysozyme (LYSO) was investigated at 302, 313 and 318 K at pH 7.4 using spectrophotometric techniques such as fluorescence emission, circular dichroism (CD) and UV absorption. The data obtained from fluorescence quenching experiments showed that farrerol was bound to LYSO and the affinity was enhanced by the addition of farrerol. When the concentration ratio of farrerol to LYSO was higher than 5.4, both the binding constant and the binding stoichiometry went up. Based on the thermodynamic parameters evaluated from the van't Hoff equation, the enthalpy change (Delta H degrees) and entropy change (Delta S degrees) were derived to be negative values. They indicated that both van der Waals forces and hydrogen bonds are the major interactions between farrerol and LYSO. A value of 2.67 nm for the average distance r between farrerol (acceptor) and tryptophan residues (Trp) of LYSO (donor) was derived from the fluorescence resonance energy transfer. Besides, the change in the conformation of LYSO was observed, being caused by the interaction with farrerol. (C) 2007 Elsevier B.V. All rights reserved.
机译：使用分光光度法，例如荧光发射，圆二色性（CD）和UV吸收，在pH 7.4的302、313和318 K下研究了farrerol与溶菌酶（LYSO）的结合。从荧光猝灭实验获得的数据表明，法雷洛尔与LYSO结合，并且通过添加法雷洛尔增强了亲和力。当法瑞罗尔与LYSO的浓度比高于5.4时，结合常数和结合化学计量均升高。基于从van't Hoff方程评估的热力学参数，将焓变（ΔH度）和熵变（ΔS度）推导为负值。他们指出范德华力和氢键都是法雷洛尔与LYSO之间的主要相互作用。从荧光共振能量转移得出法雷洛尔（受体）与LYSO（供体）色氨酸残基（Trp）之间的平均距离r为2.67 nm。此外，观察到LYSO的构象变化是由于与法瑞罗的相互作用引起的。 （C）2007 Elsevier B.V.保留所有权利。

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