Heterotypic Amyloid β interactions facilitate amyloid assembly and modify amyloid structure.

ABSTRACT: It is still unclear why pathological amyloid deposition initiates in specific brain regions or why some cells or tissues are more susceptible than others. Amyloid deposition is determined by the self-assembly of short protein segments called aggregation-prone regions (APRs) that favour cross-β structure. Here, we investigated whether Aβ amyloid assembly can be modified by heterotypic interactions between Aβ APRs and short homologous segments in otherwise unrelated human proteins. Mining existing proteomics data of Aβ plaques from AD patients revealed an enrichment in proteins that harbour such homologous sequences to the Aβ APRs, suggesting heterotypic amyloid interactions may occur in patients. We identified homologous APRs from such proteins and show that they can modify Aβ assembly kine

SUBMITTER: Konstantoulea K 

PROVIDER: S-EPMC8762568 | biostudies-literature | 2022 Dec

REPOSITORIES: biostudies-literature