Influence of oligomeric and fibrillar lysozyme on physical properties of model membranes
Keywords:
amyloid lysozyme, oligomers, fibrils, pyrene, Laurdan, membrane fluidity, dehydrationAbstract
A pathological hallmark of more than 20 human diseases including Alzheimer’s disease, Parkinson’s
disease, type II diabetes is the deposition in organs and tissues of insoluble highly ordered protein
aggregates, called amyloid fibrils. It is becoming widely recognized that toxicity of amyloid species is
related to their interactions with cell membranes. In the present study we focused our efforts on the
examination of the influence of amyloid fibrils and their precursors (oligomeric aggregates) of lysozyme
on the structural and physical properties of the model membranes composed of phosphatidylcholine and
its mixture with cholesterol. For evaluating the extent of lipid bilayer modifications, we used fluorescence
spectroscopy technique. The results of pyrene excimerization measurements showed that amyloid protein
reduces membrane fluidity. Analysis of Laurdan emission spectra revealed the ability of lysozyme
aggregates to produce bilayer dehydration. The most pronounced membrane-modifying effects were
observed in the case of oligomeric lysozyme. Significantly less influence of pathogenic protein
aggregates on the physical properties of cholesterol-containing vesicles confirmed the hypothesis on the
preventive role of cholesterol in amyloid-related diseases.
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