Ultrafast propagation of β-amyloid fibrils in oligomeric cloud

摘要: Interaction between monomer peptides and seeds is essential for clarifying the fibrillation mechanism of amyloid β (Aβ) peptides. We monitored deposition reaction Aβ1–40 on immobilized grown from Aβ1–42, which caused formation oligomers in early stage. The procedure were throughout by novel total-internal-reflection-fluorescence microscopy with a quartz-crystal microbalance (TIRFM-QCM) system. This system allows simultaneous evaluation amount deposited surface QCM fibril nucleation elongation TIRFM. Most fibrils reached other nuclei, forming network across nucleus hubs short time. found fibril-elongation rate two-orders-of-magnitude higher an oligomeric cloud than reported values, indicating ultrafast transition into fibrils.