Ultrafast propagation of β-amyloid fibrils in oligomeric cloud

Ogi, Hirotsugu; Fukukshima, Masahiko; Hamada, Hiroki; Noi, Kentaro; Hirao, Masahiko; Yagi, Hisashi; Goto, Yuji

doi:https://doi.org/10.1038/srep06960

Ultrafast propagation of β-amyloid fibrils in oligomeric cloud

Ogi, Hirotsugu; Fukukshima, Masahiko; Hamada, Hiroki et al.

Scientific Reports, 2014, 4, 6960

Number of Access:476（2025-10-09 11:46 Counts）

Identifier to cite or link to this item: https://hdl.handle.net/11094/71270

Link to primary information

File	Format	Terms of use	Size	Views	Date.Available	Description	information
SR_4_6960	pdf	None	2.20 MB	252	2019.02.26

Creative Commons : Attribution - NonCommercial - ShareAlike

Item Information

Output File Export EndNote Basic Export Mendeley

Title	Ultrafast propagation of β-amyloid fibrils in oligomeric cloud
Creator	NRID 1000090252626 1000090252626 researchmap permalink read0042771 read0042771 Scopus Author ID 35563683500 35563683500 CreatorName Ogi, Hirotsugu
	CreatorName Fukukshima, Masahiko
	CreatorName Hamada, Hiroki
	NRID 1000030588405 1000030588405 CreatorName Noi, Kentaro
	NRID 1000080112027 1000080112027 CreatorName Hirao, Masahiko
	NRID 1000010432494 1000010432494 CreatorName Yagi, Hisashi
	NRID 1000040153770 1000040153770 researchmap permalink read0014440 read0014440 CreatorName Goto, Yuji
Description	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
Abstract	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.
Publisher	Springer Nature
Source Title	Scientific Reports
Volume (Issue)	4
Page	6960
Date of Issued	2014-11
Language	English
Handle URL	https://hdl.handle.net/11094/71270
eISSN	20452322
Relation.isIdenticalTo	DOI (Publisher Version) https://doi.org/10.1038/srep06960
Access Rights	open access
CopyRight	© 2014 The Author(s). This article is licensed under a Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International License.
oaire:version	Version of Record
Category	学術雑誌論文 Journal Article

Resource Type	journal article
Local Type	Journal Article
DCMI Type	Text
DCTERMS.bibliographicCitation	Scientific Reports. 2014, 4, p. 6960
DC.title	Ultrafast propagation of β-amyloid fibrils in oligomeric cloud
DC.creator	Ogi, Hirotsugu
	Fukukshima, Masahiko
	Hamada, Hiroki
	Noi, Kentaro
	Hirao, Masahiko
	Yagi, Hisashi
	Goto, Yuji
DC.publisher	Springer Nature
DC.language' scheme='DCTERMS.RFC1766	English
DC.type' scheme='DCTERMS.DCMIType	Text
DCTERMS.issued' scheme='DCTERMS.W3CDTF	2014-11
DC.identifier	https://doi.org/10.1038/srep06960
DC.description	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
DCTERMS.abstract	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.
DC.rights	© 2014 The Author(s). This article is licensed under a Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International License.
DC.format	71270
citation_title	Ultrafast propagation of β-amyloid fibrils in oligomeric cloud
citation_author	Ogi, Hirotsugu
	Fukukshima, Masahiko
	Hamada, Hiroki
	Noi, Kentaro
	Hirao, Masahiko
	Yagi, Hisashi
	Goto, Yuji
citation_publisher	Springer Nature
citation_language	English
citation_date	2014-11
citation_journal_title	Scientific Reports
citation_volume	4
citation_firstpage	6960
citation_doi	https://doi.org/10.1038/srep06960
citation_public_url	https://hdl.handle.net/11094/71270

Ultrafast propagation of β-amyloid fibrils in oligomeric cloud

Link to primary information

Item Information

Show details