Axel Abelein

TL;DR: The results show that, under near-physiological conditions, substoichiometric amounts of Zn2+ effectively retard the generation of amyloid fibrils and propose that zinc adopts the role of a minimal antiaggregation chaperone for Aβ40.

TL;DR: This review focuses on biophysical studies of the Aβ peptides of the aggregation pathways and intermediates observed during aggregation, of the molecular structures observed along these pathways, and of the interactions of Aβ with Cu and Zn ions and with small molecules that modify the aggregation processes.

TL;DR: It is concluded that a hairpin-like conformation constitutes a common motif for the Aβ peptides in most of the described structures, which could be one reason for the molecular heterogeneity observed in the aggregated systems.

TL;DR: A model is suggested where salt decreases the free-energy barrier for Aβ40 folding to the Fβ state, favoring the buildup of the mature fibril morphology while omitting competing, energetically less favorable structural states.

TL;DR: It is shown that Bri2 BRICHOS monomers potently prevent neuronal network toxicity of Aβ, while dimers strongly suppress Aβ fibril formation, suggesting a means to generate molecular chaperone diversity.