High-speed atomic force microscopy reveals structural dynamics of amyloid β1-42 aggregates.

ABSTRACT: Aggregation of amyloidogenic proteins into insoluble amyloid fibrils is implicated in various neurodegenerative diseases. This process involves protein assembly into oligomeric intermediates and fibrils with highly polymorphic molecular structures. These structural differences may be responsible for different disease presentations. For this reason, elucidation of the structural features and assembly kinetics of amyloidogenic proteins has been an area of intense study. We report here the results of high-speed atomic force microscopy (HS-AFM) studies of fibril formation and elongation by the 42-residue form of the amyloid β-protein (Aβ1-42), a key pathogenetic agent of Alzheimer's disease. Our data demonstrate two different growth modes of Aβ1-42, one producing straight fibrils and the other

SUBMITTER: Watanabe-Nakayama T 

PROVIDER: S-EPMC4889376 | biostudies-literature | 2016 May

REPOSITORIES: biostudies-literature