Changes in Adsorption, Aggregation, and Diffusion Nature of Amyloid β on a Lipid Membrane in an Open System.

The aggregation and accumulation of amyloid β 42 (Aβ42) peptides on the surface of brain cells is associated with Alzheimer's disease (AD); however, the underlying molecular mechanisms remain unclear. Herein, we used a unique brain-mimetic open system that continuously flows Aβ42 solution to analyze the initial aggregation and adsorptive nature of Aβ42 at physiological concentrations on the lipid membrane. The open system accelerated the adsorption and dimerization kinetics. Upon the addition of Aβ42, monomeric Aβ42 was dominant on the lipid bilayer surface in the closed system with no flow, whereas dimers and high-order oligomers were dominant in the open system. Closed and open systems exhibited different oligomerization kinetics, lipid-Aβ42 interactions, and diffusive properties of monomers and oligomers. These results indicate the specific adsorptive and diffusive nature of Aβ42 on the cell membrane. The open system may help in elucidating the molecular mechanisms underlying AD progression.