A novel pathway for amyloids self-assembly in aggregates at nanomolar concentration mediated by the interaction with surfaces.

ABSTRACT: A limitation of the amyloid hypothesis in explaining the development of neurodegenerative diseases is that the level of amyloidogenic polypeptide in vivo is below the critical concentration required to form the aggregates observed in post-mortem brains. We discovered a novel, on-surface aggregation pathway of amyloidogenic polypeptide that eliminates this long-standing controversy. We applied atomic force microscope (AFM) to demonstrate directly that on-surface aggregation takes place at a concentration at which no aggregation in solution is observed. The experiments were performed with the full-size Aβ protein (Aβ42), a decapeptide Aβ(14-23) and α-synuclein; all three systems demonstrate a dramatic preference of the on-surface aggregation pathway compared to the aggregation in the bulk so

SUBMITTER: Banerjee S 

PROVIDER: S-EPMC5372363 | biostudies-literature | 2017 Mar

REPOSITORIES: biostudies-literature