Effect of temperature on the conformation of lysozyme adsorbed to silica particles

被引：87

作者：

Czeslik, C ^{[1
]}

Winter, R ^{[1
]}

机构：

[1] Univ Dortmund, Fachbereich Chem, D-44227 Dortmund, Germany

来源：

PHYSICAL CHEMISTRY CHEMICAL PHYSICS | 2001年 / 3卷 / 02期

关键词：

D O I：

10.1039/b005900p

中图分类号：

O64 [物理化学（理论化学）、化学物理学];

学科分类号：

070304 ; 081704 ;

摘要：

Steady-state and lifetime fluorescence spectroscopy was used to study the conformation of hen egg white lysozyme adsorbed to differently charged colloidal silica particles as a function of temperature. While electrostatic interactions appear to be the driving force for adsorption, a decreased charge density of the substrate was found to enhance attractive protein-silica interactions. In the adsorbed state the temperature of unfolding is lowered by about 12-20 degreesC, reflecting a decreased thermal protein stability. Applying a two-state thermodynamic model significantly smaller enthalpy and entropy changes have been found for the temperature-induced unfolding of lysozyme when it is adsorbed to the silica particles. From intrinsic fluorescence lifetime measurements a characteristic change of the lifetime distribution of lysozyme due to adsorption has been observed over a wide temperature range. These results were found to be consistent with an adsorption-induced modification of the lysozyme structure and a spreading of lysozyme on the silica particles in the process of unfolding.

引用

页码：235 / 239

页数：5

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