S100B chaperone multimers suppress the formation of oligomers during Aβ42 aggregation.

ABSTRACT: Extracellular aggregation of the amyloid-β 1-42 (Aβ42) peptide is a major hallmark of Alzheimer's disease (AD), with recent data suggesting that Aβ intermediate oligomers (AβO) are more cytotoxic than mature amyloid fibrils. Understanding how chaperones harness such amyloid oligomers is critical toward establishing the mechanisms underlying regulation of proteostasis in the diseased brain. This includes S100B, an extracellular signaling Ca²⁺-binding protein which is increased in AD as a response to neuronal damage and whose holdase-type chaperone activity was recently unveiled. Driven by this evidence, we here investigate how different S100B chaperone multimers influence the formation of oligomers during Aβ42 fibrillation. Resorting to kinetic analysis coupled with simulation of

SUBMITTER: Figueira AJ 

PROVIDER: S-EPMC10070764 | biostudies-literature | 2023

REPOSITORIES: biostudies-literature