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

T Watanabe-Nakayama, K Ono… - Proceedings of the …, 2016 - National Acad Sciences
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 …

High-speed atomic force microscopy reveals structural dynamics of amyloid Β1-42 aggregates

K Ono, T Nakayama, M Itami, R Takahashi… - Journal of the …, 2017 - jns-journal.com
Background: Alzheimer's disease (AD) is characterized by the accumulation of amyloid
plaques and neurofibrillary tangles. 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. Objective: The objective is to elucidate the structural features and assembly …
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