The cyclic neuropeptide somatostatin binds to human Aβ1-42 through an interface that critically relies on a specific tryptophan, thereby blocking the propensity of Aβ to aggregate, a critical step in the pathobiology of Alzheimer's disease.

Novel designed alpha-sheet peptides inhibit amyloidosis in two different systems and preferentially bind the toxic oligomer.

An optogenetic approach has been developed to model Alzheimer's disease allowing light-induced Amyloid-β aggregation and tested in three model organisms, Drosophila, C. elegans and D. rerio.

Soluble amyloid-β precursor peptide has no functional effects at recombinant and native GABA_B receptors.

Inhibitors of seeded propagation of alpha-synuclein may be developed into diagnostics and therapeutics for Parkinson's disease.

Monitoring the formation of two distinct arrangements in early amyloid-ß aggregation by mass spectrometry and ion mobility allows determination of the effect of potential drug candidates.

Biochemical studies in combination with computational modeling and molecular dynamics simulations reveal that the lipid bilayer promotes intramembrane proteolysis by stabilizing the enzyme-substrate complex and the protease active site.

The protease γ-secretase generates amyloid-beta peptides using a mechanism that is driven by the stabilization of an enzyme-substrate scisson complex.

Further evidence in support of a new amyloid-independent hypothesis for the pathogenesis of Alzheimer's disease is provided, with an expanded set of Alzheimer-causing mutations in the protease that produces amyloid.

A massively parallel analysis of the effects of mutations on amyloid beta nucleation provide the first comprehensive atlas of how mutations alter the formation of amyloid fibrils.