The binding of the small heat-shock protein αB-crystallin to fibrils of α-synuclein is driven by entropic forces.

ABSTRACT: Molecular chaperones are key components of the cellular proteostasis network whose role includes the suppression of the formation and proliferation of pathogenic aggregates associated with neurodegenerative diseases. The molecular principles that allow chaperones to recognize misfolded and aggregated proteins remain, however, incompletely understood. To address this challenge, here we probe the thermodynamics and kinetics of the interactions between chaperones and protein aggregates under native solution conditions using a microfluidic platform. We focus on the binding between amyloid fibrils of α-synuclein, associated with Parkinson's disease, to the small heat-shock protein αB-crystallin, a chaperone widely involved in the cellular stress response. We find that αB-crystallin binds to α-s

SUBMITTER: Scheidt T 

PROVIDER: S-EPMC8463877 | biostudies-literature | 2021 Sep

REPOSITORIES: biostudies-literature