Direct observation of secondary nucleation along the fibril surface of the amyloid β 42 peptide.

ABSTRACT: Alzheimer's disease is a neurodegenerative condition which involves heavy neuronal cell death linked to oligomers formed during the aggregation process of the amyloid β peptide 42 (Aβ42). The aggregation of Aβ42 involves both primary and secondary nucleation. Secondary nucleation dominates the generation of oligomers and involves the formation of new aggregates from monomers on catalytic fibril surfaces. Understanding the molecular mechanism of secondary nucleation may be crucial in developing a targeted cure. Here, the self-seeded aggregation of WT Aβ42 is studied using direct stochastic optical reconstruction microscopy (dSTORM) with separate fluorophores in seed fibrils and monomers. Seeded aggregation proceeds faster than nonseeded reactions because the fibr

SUBMITTER: Thacker D 

PROVIDER: S-EPMC10288637 | biostudies-literature | 2023 Jun

REPOSITORIES: biostudies-literature