Amyloid-β aggregation with gold nanoparticles on brain lipid bilayer

Understanding and manipulating amyloid-β (Aβ) aggregation provide key knowledge and means for the diagnosis and cure of Alzheimer's disease (AD) and the applications of Aβ-based aggregation systems. Here, we studied the formation of various Aβ aggregate structures with gold nanoparticles (AuNPs) and brain total lipid extract-based supported lipid bilayer (brain SLB). The roles of AuNPs and brain SLB in forming Aβ aggregates were studied in real time, and the structural details of Aβ aggregates were monitored and analyzed with the dark-field imaging of plasmonic AuNPs that allows for long-term in situ imaging of Aβ aggregates with great structural details without further labeling. It was shown that the fluid brain SLB platform provides the binding sites for Aβ and drives the fast and efficient formation of Aβ aggregate structures and, importantly, large Aβ plaque structures (>15 μm in diameter), a hallmark for AD, were formed without going through fibril structures when Aβ peptides were co-incubated with AuNPs on the brain SLB. The dark-field scattering and circular dichroism-correlation data suggest that AuNPs were heavily involved with Aβ aggregation on the brain SLB and less α-helix, less β-sheet and more random coil structures were found in large plaque-like Aβ aggregates.