Time-Resolved Observation of Evolution of Amyloid-β Oligomer with Temporary Salt Crystals

Nakajima, Kichitaro; Yamazaki, Tomoya; Kimura, Yuki; So, Masatomo; Goto, Yuji; Ogi, Hirotsugu

doi:https://doi.org/10.1021/acs.jpclett.0c01487

Time-Resolved Observation of Evolution of Amyloid-β Oligomer with Temporary Salt Crystals

Nakajima, Kichitaro; Yamazaki, Tomoya; Kimura, Yuki et al.

Journal of Physical Chemistry Letters, 2020, 11(15), 6176-6184

Number of Access:940（2025-08-14 15:06 Counts）

Identifier to cite or link to this item: https://hdl.handle.net/11094/84186

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Title	Time-Resolved Observation of Evolution of Amyloid-β Oligomer with Temporary Salt Crystals
Creator	NRID 1000020867337 1000020867337 ORCID 0000-0003-2644-741X 0000-0003-2644-741X researchmap permalink sonochem sonochem Scopus Author ID 57145904700 57145904700 CreatorName Nakajima, Kichitaro
	NRID 1000050735032 1000050735032 CreatorName Yamazaki, Tomoya
	NRID 1000050449542 1000050449542 CreatorName Kimura, Yuki
	NRID 1000040746335 1000040746335 CreatorName So, Masatomo
	NRID 1000040153770 1000040153770 researchmap permalink read0014440 read0014440 CreatorName Goto, Yuji
	NRID 1000090252626 1000090252626 researchmap permalink read0042771 read0042771 Scopus Author ID 35563683500 35563683500 CreatorName Ogi, Hirotsugu
Description	Nakajima K., Yamazaki T., Kimura Y., et al. "Time-Resolved Observation of Evolution of Amyloid-β Oligomer with Temporary Salt Crystals", Journal of Physical Chemistry Letters, 11(15), 6176-6184, July 20, 2020. Copyright © 2020 American Chemical Society. https://doi.org/10.1021/acs.jpclett.0c01487.
Abstract	The aggregation behavior of amyloid-β (Aβ) peptides remains unclarified despite the fact that it is closely related to the pathogenic mechanism of Alzheimer's disease. Aβ peptides form diverse oligomers with various diameters before nucleation, making clarification of the mechanism involved a complex problem with conventional macroscopic analysis methods. Time-resolved single-molecule level analysis in bulk solution is thus required to fully understand their early stage aggregation behavior. Here, we perform time-resolved observation of the aggregation dynamics of Aβ oligomers in bulk solution using liquid-state transmission electron microscopy. Our observations reveal previously unknown behaviors. The most important discovery is that a salt crystal can precipitate even with a concentration much lower than its solubility, and it then dissolves in a short time, during which the aggregation reaction of Aβ peptides is significantly accelerated. These findings will provide new insights in the evolution of the Aβ oligomer.
Publisher	American Chemical Society
Source Title	Journal of Physical Chemistry Letters
Volume (Issue)	11(15)
Page	6176-6184
Date of Issued	2020-07-20
Language	English
Handle URL	https://hdl.handle.net/11094/84186
eISSN	19487185
NCID	AA1260018X
Relation.isVersionOf	DOI (Publisher Version) https://doi.org/10.1021/acs.jpclett.0c01487
Relation.isIdenticalTo	PMID 32687370
Access Rights	open access
CopyRight	This document is the Accepted Manuscript version of a Published Work that appeared in final form in Journal of Physical Chemistry Letters, © American Chemical Society after peer review and technical editing by the publisher. To access the final edited and published work see https://doi.org/10.1021/acs.jpclett.0c01487.
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	Journal of Physical Chemistry Letters. 2020, 11(15), p. 6176-6184
DC.title	Time-Resolved Observation of Evolution of Amyloid-β Oligomer with Temporary Salt Crystals
DC.creator	Nakajima, Kichitaro
	Yamazaki, Tomoya
	Kimura, Yuki
	So, Masatomo
	Goto, Yuji
	Ogi, Hirotsugu
DC.publisher	American Chemical Society
DC.language' scheme='DCTERMS.RFC1766	English
DC.type' scheme='DCTERMS.DCMIType	Text
DCTERMS.issued' scheme='DCTERMS.W3CDTF	2020-07-20
DC.identifier	https://doi.org/10.1021/acs.jpclett.0c01487
DC.description	Nakajima K., Yamazaki T., Kimura Y., et al. "Time-Resolved Observation of Evolution of Amyloid-β Oligomer with Temporary Salt Crystals", Journal of Physical Chemistry Letters, 11(15), 6176-6184, July 20, 2020. Copyright © 2020 American Chemical Society. https://doi.org/10.1021/acs.jpclett.0c01487.
DCTERMS.abstract	The aggregation behavior of amyloid-β (Aβ) peptides remains unclarified despite the fact that it is closely related to the pathogenic mechanism of Alzheimer's disease. Aβ peptides form diverse oligomers with various diameters before nucleation, making clarification of the mechanism involved a complex problem with conventional macroscopic analysis methods. Time-resolved single-molecule level analysis in bulk solution is thus required to fully understand their early stage aggregation behavior. Here, we perform time-resolved observation of the aggregation dynamics of Aβ oligomers in bulk solution using liquid-state transmission electron microscopy. Our observations reveal previously unknown behaviors. The most important discovery is that a salt crystal can precipitate even with a concentration much lower than its solubility, and it then dissolves in a short time, during which the aggregation reaction of Aβ peptides is significantly accelerated. These findings will provide new insights in the evolution of the Aβ oligomer.
DC.rights	This document is the Accepted Manuscript version of a Published Work that appeared in final form in Journal of Physical Chemistry Letters, © American Chemical Society after peer review and technical editing by the publisher. To access the final edited and published work see https://doi.org/10.1021/acs.jpclett.0c01487.
DC.format	84186
citation_title	Time-Resolved Observation of Evolution of Amyloid-β Oligomer with Temporary Salt Crystals
citation_author	Nakajima, Kichitaro
	Yamazaki, Tomoya
	Kimura, Yuki
	So, Masatomo
	Goto, Yuji
	Ogi, Hirotsugu
citation_publisher	American Chemical Society
citation_language	English
citation_date	2020-07-20
citation_journal_title	Journal of Physical Chemistry Letters
citation_volume	11
citation_issue	15
citation_firstpage	6176
citation_lastpage	6184
citation_doi	https://doi.org/10.1021/acs.jpclett.0c01487
citation_pmid	32687370
citation_public_url	https://hdl.handle.net/11094/84186

Time-Resolved Observation of Evolution of Amyloid-β Oligomer with Temporary Salt Crystals

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