学術雑誌論文

学術雑誌論文

text

Scientific Reports. 2014, 4, p. 6960

Ultrafast propagation of β-amyloid fibrils in oligomeric cloud

Springer Nature

英語

text

2014-11

https://doi.org/10.1038/srep06960

Hirotsugu Ogi, Masahiko Fukukshima, Hiroki Hamada, Kentaro Noi, Masahiko Hirao, Hisashi Yagi & Yuji Goto "Ultrafast propagation of β-amyloid fibrils in oligomeric cloud", Scientific Reports, volume 4, Article number: 6960, Springer Nature, 2014

Interaction between monomer peptides and seeds is essential for clarifying the fibrillation mechanism of amyloid β (Aβ) peptides. We monitored the deposition reaction of Aβ1–40 peptides on immobilized seeds grown from Aβ1–42, 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.

© 2014 The Author(s). This article is licensed under a Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International License.

application/pdf

Ultrafast propagation of β-amyloid fibrils in oligomeric cloud

Springer Nature

英語

2014-11

Scientific Reports

4

6960

https://doi.org/10.1038/srep06960

https://hdl.handle.net/11094/71270