Sequestration within biomolecular condensates inhibits Aβ-42 amyloid formation.

ABSTRACT: Biomolecular condensates are emerging as an efficient strategy developed by cells to control biochemical reactions in space and time by locally modifying composition and environment. Yet, local increase in protein concentration within these compartments could promote aberrant aggregation events, including the nucleation and growth of amyloid fibrils. Understanding protein stability within the crowded and heterogeneous environment of biological condensates is therefore crucial, not only when the aggregation-prone protein is the scaffold element of the condensates but also when proteins are recruited as client molecules within the compartments. Here, we investigate the partitioning and aggregation kinetics of the amyloidogenic peptide Abeta42 (Aβ-42), the peptide strongly associated with Alz

SUBMITTER: Kuffner AM 

PROVIDER: S-EPMC8179469 | biostudies-literature | 2021 Feb

REPOSITORIES: biostudies-literature