Modulation of physiological and pathological activities of lysozyme by biological membranes

Cellular & Molecular Biology Letters

Valeriya Trusova¹ 

[1]Department of Biological and Medical Physics, V. N. Karazin Kharkov National University, Kharkov, Ukraine$$Kharkov, Ukraine$$

关键词: Amyloid toxicity;    Antimicrobial activity;    “Carpet” mechanism;    Fluorescence spectroscopy;    Lipid membranes;    Lipid domain formation;    Lysozyme;    Membrane free volume;    Membrane destabilization;    Protein aggregation;   

DOI  :  10.2478/s11658-012-0015-6

学科分类：分子生物学，细胞生物学和基因

来源: Uniwersytet Wroclawski * Wydzial Biotechnologii / University of Wroclaw, Faculty of Biotechnology

【 摘 要 】

The molecular details of interactions between lipid membranes and lysozyme (Lz), a small polycationic protein with a wide range of biological activities, have long been the focus of numerous studies. The biological consequences of this process are considered to embrace at least two aspects: i) correlation between antimicrobial and membranotropic properties of this protein, and ii) lipid-mediated Lz amyloidogenesis. The mechanisms underlying the lipid-assisted protein fibrillogenesis and membrane disruption exerted by Lz in bacterial cells are believed to be similar. The present investigation was undertaken to gain further insight into Lz-lipid interactions and explore the routes by which Lz exerts its antimicrobial and amyloidogenic actions. Binding and Förster resonance energy transfer studies revealed that upon increasing the content of anionic lipids in lipid vesicles, Lz forms aggregates in a membrane environment. Total internal reflection fluorescence microscopy and pyrene excimerization reaction were employed to study the effect of Lz on the structural and dynamic properties of lipid bilayers. It was found that Lz induces lipid demixing and reduction of bilayer free volume, the magnitude of this effect being much more pronounced for oligomeric protein.

【 授权许可】

Unknown