The mechanism of pathological or functional amyloid-assembly is unknown. It is thought that the interaction of proteins with interfaces composed of lipids and/or polysaccharides is essential to amyloid-assembly. In vivo this occurs in overcrowded compartments in which molecular interactions are very different from bulk solution where in-vitro studies are conducted. Herein we will develop a method to entrap proteins and polysaccharides within liposomes to investigate the role of confinement and overcrowding in amyloid-assembly. Biophysical and advanced cryo-electron microscopy techniques will be used to study the mechanism and structure of functional (hormone vasopressin) and pathological (lysozyme) amyloids formed inside the liposomes.
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