Controlling interfacial protein adsorption, desorption and aggregation in biomolecular condensates.

ABSTRACT: Aggregation of amyloidogenic proteins is linked to age-related diseases. The presence of interfaces can affect their aggregation mechanism, often speeding up aggregation. α-Synuclein (αSyn) can adsorb to biomolecular condensates, leading to heterogenous nucleation and faster aggregation. Understanding the mechanism underlying localization of amyloidogenic proteins at condensate interfaces is crucial for developing strategies to prevent or reverse their binding. We show that αSyn localization to the surface of peptide-based heterotypic condensates is an adsorption process governed by the protein's condensate-amphiphilic nature, and the condensate surface charge. Adsorption occurs reversibly in multiple layers and plateaus at micromolar concentrations. Based on these findings, we rationally

SUBMITTER: Visser BS 

PROVIDER: S-EPMC12630862 | biostudies-literature | 2025 Nov

REPOSITORIES: biostudies-literature