Heterotypic Seeding Generates Mixed Amyloid Polymorphs.

ABSTRACT: Aggregation of the amyloid β (Aβ) peptide into fibrils represents one of the major biochemical pathways underlying the development of Alzheimer's disease (AD). Extensive studies have been carried out to understand the role of fibrillar seeds on the overall kinetics of amyloid aggregation. However, the precise effect of seeds that are structurally or sequentially different from Aβ on the structure of the resulting amyloid aggregates is yet to be fully understood. Herein, nanoscale infrared spectroscopy is used to probe the spectral facets of individual aggregates formed by aggregating Aβ42 with antiparallel fibrillar seeds of Aβ(16-22) and E22Q Aβ(1-40) Dutch mutant and it is demonstrated that Aβ can form heterotypic or mixed polymorphs that deviate significantly from its expected parallel

SUBMITTER: Banerjee S 

PROVIDER: S-EPMC11709449 | biostudies-literature | 2024 Sep

REPOSITORIES: biostudies-literature