Amyloid-β fibrils assembled on ganglioside-enriched membranes contain both parallel β-sheets and turns.

ABSTRACT: Some protein and peptide aggregates, such as those of amyloid-β protein (Aβ), are neurotoxic and have been implicated in several neurodegenerative diseases. Aβ accumulates at nanoclusters enriched in neuronal lipids called gangliosides in the presynaptic neuronal membrane, and the resulting oligomeric and/or fibrous forms accelerate the development of Alzheimer's disease. Although the presence of Aβ deposits at such nanoclusters is known, the mechanism of their assembly and the relationship between Aβ secondary structure and topography are still unclear. Here, we first confirmed by atomic force microscopy that Aβ₄₀ fibrils can be obtained by incubating seed-free Aβ₄₀ monomers with a membrane composed of sphingomyelin, cholesterol, and the ganglioside GM1. Using Fourie

SUBMITTER: Matsubara T 

PROVIDER: S-EPMC6130953 | biostudies-literature | 2018 Sep

REPOSITORIES: biostudies-literature