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Ultrafast propagation of ?-amyloid fibrils in oligomeric cloud.

ABSTRACT: Interaction between monomer peptides and seeds is essential for clarifying the fibrillation mechanism of amyloid ? (A?) peptides. We monitored the deposition reaction of A?(1-40) peptides on immobilized seeds grown from A?(1-42), which caused formation of oligomers in the early stage. The deposition reaction and fibrillation procedure were monitored throughout by novel total-internal-reflection-fluorescence microscopy with a quartz-crystal microbalance (TIRFM-QCM) system. This system allows simultaneous evaluation of the amount of deposited peptides on the surface seeds by QCM and fibril nucleation and elongation by TIRFM. Most fibrils reached other nuclei, forming the fibril network across the nucleus hubs in a short time. We found a fibril-elongation rate two-orders-of-magnitude higher in an oligomeric cloud than reported values, indicating ultrafast transition of oligomers into fibrils.

SUBMITTER: Ogi H

PROVIDER: S-EPMC4223663 | biostudies-literature | 2014 Nov

REPOSITORIES: biostudies-literature

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Ultrafast propagation of β-amyloid fibrils in oligomeric cloud.

Ogi Hirotsugu H Fukukshima Masahiko M Hamada Hiroki H Noi Kentaro K Hirao Masahiko M Yagi Hisashi H Goto Yuji Y

Scientific reports 20141107

Interaction between monomer peptides and seeds is essential for clarifying the fibrillation mechanism of amyloid β (Aβ) peptides. We monitored the deposition reaction of Aβ(1-40) peptides on immobilized seeds grown from Aβ(1-42), which caused formation of oligomers in the early stage. The deposition reaction and fibrillation procedure were monitored throughout by novel total-internal-reflection-fluorescence microscopy with a quartz-crystal microbalance (TIRFM-QCM) system. This system allows simu ...[more]

PMID: 25376301

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