Nucleation-fibrillation dynamics of Aβ₁₋₄₀ peptides on liquid-solid surface studied by total-internal-reflection fluorescence microscopy coupled with quartz-crystal microbalance biosensor

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

doi:https://doi.org/10.7567/JJAP.54.07HE01

Nucleation-fibrillation dynamics of Aβ₁₋₄₀ peptides on liquid-solid surface studied by total-internal-reflection fluorescence microscopy coupled with quartz-crystal microbalance biosensor

Hamada, Hiroki; Ogi, Hirotsugu; Noi, Kentaro et al.

Japanese Journal of Applied Physics, 2015, 54, 07HE01

Number of Access:461（2025-08-14 09:01 Counts）

Identifier to cite or link to this item: https://hdl.handle.net/11094/84171

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Title	Nucleation-fibrillation dynamics of Aβ₁₋₄₀ peptides on liquid-solid surface studied by total-internal-reflection fluorescence microscopy coupled with quartz-crystal microbalance biosensor
Creator	CreatorName Hamada, Hiroki
	NRID 1000090252626 1000090252626 researchmap permalink read0042771 read0042771 Scopus Author ID 35563683500 35563683500 CreatorName Ogi, Hirotsugu
	NRID 1000030588405 1000030588405 CreatorName Noi, Kentaro
	NRID 1000010432494 1000010432494 CreatorName Yagi, Hisashi
	NRID 1000040153770 1000040153770 researchmap permalink read0014440 read0014440 CreatorName Goto, Yuji
	NRID 1000080112027 1000080112027 CreatorName Hirao, Masahiko
Description	Hiroki Hamada, Hirotsugu Ogi, Kentaro Noi, Hisashi Yagi, Yuji Goto and Masahiko Hirao. Nucleation-fibrillation dynamics of Aβ₁₋₄₀ peptides on liquid-solid surface studied by total-internal-reflection fluorescence microscopy coupled with quartz-crystal microbalance biosensor. Japanese Journal of Applied Physics, 2015, 54(7S1), 07HE01. https://doi.org/10.7567/JJAP.54.07HE01.
Abstract	We have successfully developed the total-internal-reflection-fluorescence microscopy combined with a quartz-crystal microbalance (TIRFM-QCM) biosensor, and monitored the nucleation-fibrillation phenomenon of amyloid β₁₋₄₀ peptide on the naked quartz surface. The cross-β-sheet structures were visualized with the TIRFM using the thioflavin-T (Th-T) label, and other unlabeled aggregates were detected through the frequency change of the 58-MHz wireless-electrodeless QCM throughout the aggregation reaction. The QCM response indicates significant adsorption of the peptides on the quartz surface at the early stage, which is followed by fibrillation. The non-cross-β-sheet oligomers are first formed, and nuclei appear in the oligomer region, from which fibrils originate and elongate. The two-color TIRFM observation was performed after the aggregation reaction with the Nile-red label as well as the ThT label for identifying nucleation from non-β-sheet regions. An aggregation model is proposed.
Publisher	The Japan Society of Applied Physics
Source Title	Japanese Journal of Applied Physics
Volume (Issue)	54
Page	07HE01
Date of Issued	2015-05-12
Language	English
Handle URL	https://hdl.handle.net/11094/84171
PISSN	00214922
eISSN	13474065
NCID	AA12295836
Relation.isVersionOf	DOI (Publisher Version) https://doi.org/10.7567/JJAP.54.07HE01
Access Rights	open access
oaire:version	Accepted Manuscript
Category	学術雑誌論文 Journal Article

Resource Type	journal article
Local Type	Journal Article
DCMI Type	Text
DCTERMS.bibliographicCitation	Japanese Journal of Applied Physics. 2015, 54, p. 07HE01
DC.title	Nucleation-fibrillation dynamics of Aβ₁₋₄₀ peptides on liquid-solid surface studied by total-internal-reflection fluorescence microscopy coupled with quartz-crystal microbalance biosensor
DC.creator	Hamada, Hiroki
	Ogi, Hirotsugu
	Noi, Kentaro
	Yagi, Hisashi
	Goto, Yuji
	Hirao, Masahiko
DC.publisher	The Japan Society of Applied Physics
DC.language' scheme='DCTERMS.RFC1766	English
DC.type' scheme='DCTERMS.DCMIType	Text
DCTERMS.issued' scheme='DCTERMS.W3CDTF	2015-05-12
DC.identifier	https://doi.org/10.7567/JJAP.54.07HE01
DC.description	Hiroki Hamada, Hirotsugu Ogi, Kentaro Noi, Hisashi Yagi, Yuji Goto and Masahiko Hirao. Nucleation-fibrillation dynamics of Aβ₁₋₄₀ peptides on liquid-solid surface studied by total-internal-reflection fluorescence microscopy coupled with quartz-crystal microbalance biosensor. Japanese Journal of Applied Physics, 2015, 54(7S1), 07HE01. https://doi.org/10.7567/JJAP.54.07HE01.
DCTERMS.abstract	We have successfully developed the total-internal-reflection-fluorescence microscopy combined with a quartz-crystal microbalance (TIRFM-QCM) biosensor, and monitored the nucleation-fibrillation phenomenon of amyloid β₁₋₄₀ peptide on the naked quartz surface. The cross-β-sheet structures were visualized with the TIRFM using the thioflavin-T (Th-T) label, and other unlabeled aggregates were detected through the frequency change of the 58-MHz wireless-electrodeless QCM throughout the aggregation reaction. The QCM response indicates significant adsorption of the peptides on the quartz surface at the early stage, which is followed by fibrillation. The non-cross-β-sheet oligomers are first formed, and nuclei appear in the oligomer region, from which fibrils originate and elongate. The two-color TIRFM observation was performed after the aggregation reaction with the Nile-red label as well as the ThT label for identifying nucleation from non-β-sheet regions. An aggregation model is proposed.
DC.format	84171
citation_title	Nucleation-fibrillation dynamics of Aβ₁₋₄₀ peptides on liquid-solid surface studied by total-internal-reflection fluorescence microscopy coupled with quartz-crystal microbalance biosensor
citation_author	Hamada, Hiroki
	Ogi, Hirotsugu
	Noi, Kentaro
	Yagi, Hisashi
	Goto, Yuji
	Hirao, Masahiko
citation_publisher	The Japan Society of Applied Physics
citation_language	English
citation_date	2015-05-12
citation_journal_title	Japanese Journal of Applied Physics
citation_volume	54
citation_firstpage	07HE01
citation_doi	https://doi.org/10.7567/JJAP.54.07HE01
citation_public_url	https://hdl.handle.net/11094/84171

Nucleation-fibrillation dynamics of Aβ₁₋₄₀ peptides on liquid-solid surface studied by total-internal-reflection fluorescence microscopy coupled with quartz-crystal microbalance biosensor

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