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

ABSTRACT: The coacervation and structural rearrangement of the protein alpha-synuclein (αSyn) into cytotoxic oligomers and amyloid fibrils are considered pathological hallmarks of Parkinson's disease. While aggregation is recognized as the key element of amyloid diseases, liquid-liquid phase separation (LLPS) and its interplay with aggregation have gained increasing interest. Previous work showed that factors promoting or inhibiting amyloid formation have similar effects on phase separation. Here, we provide 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 phase separation. The influence of salt on aggregation under crowded conditions follows a non-monotonic pattern, s

SUBMITTER: Sternke-Hoffmann R 

PROVIDER: S-EPMC10925286 | biostudies-literature | 2024 Mar

REPOSITORIES: biostudies-literature