Amyloid-β modulates the phase separation and aggregation of α-synuclein.

ABSTRACT: The aggregation of amyloid-β (Aβ) and α-synuclein (αSyn) into insoluble proteinaceous deposits is a hallmark of Alzheimer's and Parkinson's diseases. Recent evidence suggests that these amyloidogenic proteins act in synergy, with their coaggregation frequently observed in these disorders. In this study, we investigate the interaction of Aβ and αSyn using various biophysical tools. In particular, we explore the cocondensation of Aβ with αSyn, elucidating the pathways through which Aβ modulates αSyn phase separation. We studied different variants of Aβ, focusing on the most prominent species, namely Aβ42 and Aβ40. We found that Aβ42 and Aβ40 have fundamentally different mechanistic effects on the kinetics of αSyn condensation. Aβ42 initially forms large aggregates that act as heterogeneous n

SUBMITTER: Rontgen A 

PROVIDER: S-EPMC12305028 | biostudies-literature | 2025 Jul

REPOSITORIES: biostudies-literature