Abstract
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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