Trusova V. Protein-lipid interactions as a modulator of protein aggregation behavior

The object of study: complexes of model lipid membranes with protein assemblies of different oligomerization degree and ordering. Aim of work: elucidating the role of protein-lipid interactions in protein aggregation behavior. Methods: fluorescence spectroscopy, spectrophotometry, microscopy, computer simulation and molecular dynamics. Scientific novelty: structural characteristics of amyloid fibrils have been determined. The structural model of membrane-bound lysozyme has been proposed. The effect of amyloid fibril morphology on its interaction with lipid membranes was investigated. The complexation of lysozyme, N-terminal fragment of apolipoprotein A-I and cytochrome c with lipid bilayers of different composition was analyzed using molecular dynamics. Practical meaning: application in molecular biophysics, pharmacology, molecular biology and medicine.