Phase Separation and Aggregation of α-Synuclein Diverge at Different Salt Conditions.

ABSTRACT: The coacervation of alpha-synuclein (αSyn) into cytotoxic oligomers and amyloid fibrils are considered pathological hallmarks of Parkinson's disease. While aggregation is central to amyloid diseases, liquid-liquid phase separation (LLPS) and its interplay with aggregation have gained increasing interest. Previous work shows that factors promoting or inhibiting aggregation have similar effects on LLPS. This study provides a detailed scanning of a wide range of parameters, including protein, salt and crowding concentrations at multiple pH values, revealing different salt dependencies of aggregation and LLPS. The influence of salt on aggregation under crowding conditions follows a non-monotonic pattern, showing increased effects at medium salt concentrations. This behavior can be elucidated t

SUBMITTER: Sternke-Hoffmann R 

PROVIDER: S-EPMC11425899 | biostudies-literature | 2024 Sep

REPOSITORIES: biostudies-literature