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Significance Two unresolved problems in Alzheimer’s disease (AD) are its onset and propagation, linked to Aβ peptide aggregation. Fibrils of Aβ42 may grow by monomer addition at their ends. Additionally, through so-called secondary nucleation, fibrils can catalyse the formation of new aggregates from monomer on their surface, thereby generating oligomeric species that are toxic to brain tissue. Insights into the structural transitions occurring during secondary nucleation will facilitate the design of therapies to limit the neurotoxicity in AD, but such information is currently lacking. This study identifies conditions that allow the capture of reaction intermediates of secondary nucleation for the purpose of ultrastructural characterization. These reaction intermediates are morphologically distinct from mature fibrils and cover the sides of fibrils during an on-going aggregation reaction.

Ultrastructural evidence for self-replication of Alzheimer-associated Aβ42 amyloid along the sides of fibrils