Preparation of fibril nuclei of beta-amyloid peptides in reverse micelles.

We report the preparation of protofibrils from oligomeric Aβ40 aggregates, which have been incubated under spatially constrained conditions. The molecular structure of the resultant protofibrils is highly homogeneous, suggesting that the phenomenon of structural polymorphism commonly observed in Aβ40 fibrils may be largely due to multiple nucleation events.

Zinc ion rapidly induces toxic, off-pathway amyloid-β oligomers distinct from amyloid-β derived diffusible ligands in Alzheimer's disease.

Alzheimer's disease (AD) is the most prevalent neurodegenerative disease in the elderly. Zinc (Zn) ion interacts with the pathogenic hallmark, amyloid-β (Aβ), and is enriched in senile plaques in brain of AD patients. To understand Zn-chelated Aβ (ZnAβ) species, here we systematically characterized ZnAβ aggregates by incubating equimolar Aβ with Zn.

Fibrillization of β-Amyloid Peptides via Chemically Modulated Pathway.

The aggregation of β-amyloid peptides is closely associated with Alzheimer's disease. We have used liposomes to modulate the early aggregation events of 40-residue β-amyloid peptides. The spatial confinement provided by liposomes leads to the formation of nonfibrillar aggregates of β-amyloid peptides.