Competing chaperone pathways in α-synuclein disaggregation and aggregation dynamics.

ABSTRACT: The aggregation of the protein α-synuclein into amyloid fibrils and their subsequent deposition into large proteinaceous inclusions is a pathological hallmark of several neurodegenerative diseases, including Parkinson's disease. Molecular chaperones, including the small heat-shock proteins (sHsps) and the Hsp70 chaperone system, are known to interact with α-synuclein fibrils, preventing further aggregation and disaggregating fibrillar species, respectively. However, it remains unclear if sHsps co-operate with the Hsp70 chaperones to potentially improve the kinetics or effectiveness of Hsp70-mediated disaggregation and how disaggregation kinetics are influenced by aggregation-prone α-synuclein monomers. Using thioflavin-T assays, we demonstrate that the sHsps Hsp27 (HSPB1) and αB-crystallin

SUBMITTER: Auld NK 

PROVIDER: S-EPMC12432404 | biostudies-literature | 2025 Oct

REPOSITORIES: biostudies-literature