Self-assembly
of amyloid-β (Aβ) peptides in nonequilibrium,
flowing conditions is associated with pathogenesis of Alzheimer’s
disease. We examined the role of biologically relevant, nonequilibrium,
flowing conditions in the desorption, diffusion, and integration of
Aβ-lipid assemblies at the membrane surface using a microchannel
connected with microsyringes. A 1,2-dimyristoyl-sn-glycero-3-phosphocholine (DMPC) bilayer was formed on a glass substrate
and incubated in Aβ solution under either a quiescent condition
(no flow) or flowing condition for 24 h. Although dot-like aggregates
(<1 μm) comprising Aβ fibrils formed on the DMPC membrane
under the quiescent condition, larger plaque-like aggregates formed
under the flowing condition, suggesting that nonequilibrium continuous
flow governs the cytotoxicity of Aβ species. We propose that
Aβ adsorption on the membrane surface involves spontaneous desorption
of Aβ-lipid to form self-assembling aggregates, with this accelerated
by surface shear forces. These findings suggest that nonequilibrium,
flowing conditions influence inter/intra-molecular Aβ-fibril
formation to trigger formation of amyloid plaques.