Imaging the Morphology and Structure of Apolipoprotein Amyloid Fibrils

Abstract

Several plasma apolipoproteins are able to self-assemble into amyloid fibrils or influence amyloid fibril formation by other proteins. For instance, oxidation of methionine residues induces amyloid fibril formation by full-length apoA-I. ApoE is widely distributed in all types of amyloid plaques and forms amyloid-like fibrils. Specific isoforms of apoE are also genetically linked to the incidence of Alzheimer's disease. ApoC-II forms fibrils under lipid-free conditions with a twisted ribbon-like morphology, and multiple physical techniques applied to the analysis of these fibrils have led to a structural model of individual subunits in a 'G-like' conformation, stacked in a linear array withi..