The Role of α-Synuclein-DNAJB6b Coaggregation in Amyloid Suppression.

ABSTRACT: Chaperones may retard the aggregation of other proteins and increase their solubility. An important goal is a thermodynamic understanding of such an action. Here, the chaperone DNAJB6b (JB6) is found to suppress amyloid formation of the protein α-synuclein (α-syn) leading to a reduced rate of fibril formation and an increase in apparent solubility of α-syn. These findings were reached at mildly acidic pH and with light seeding under conditions where the effect on secondary nucleation is visible. Cryo-transmission electron microscopy (cryo-TEM) imaging reveals that coaggregates of α-syn and JB6 are formed with significantly altered ultrastructure compared to both pure protein fibrils and pure chaperone aggregates. This is further supported by the formation of ThT-negative aggregates and by

SUBMITTER: Palmadottir T 

PROVIDER: S-EPMC12100659 | biostudies-literature | 2025 May

REPOSITORIES: biostudies-literature