Optimized Ultrasonic Irradiation Finds Out Ultrastable Aβ₁₋₄₀ Oligomers

Nakajima, Kichitaro; So, Masatomo; Takahashi, Kazuma; Tagawa, Yoh-ichi; Hirao, Masahiko; Goto, Yuji; Ogi, Hirotsugu

doi:https://doi.org/10.1021/acs.jpcb.7b01409

Optimized Ultrasonic Irradiation Finds Out Ultrastable Aβ₁₋₄₀ Oligomers

Nakajima, Kichitaro; So, Masatomo; Takahashi, Kazuma et al.

Journal of Physical Chemistry B, 2017, 121(12), 2603-2613

Number of Access:712（2025-08-16 00:38 Counts）

Identifier to cite or link to this item: https://hdl.handle.net/11094/84142

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Title	Optimized Ultrasonic Irradiation Finds Out Ultrastable Aβ₁₋₄₀ Oligomers
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 1000040746335 1000040746335 CreatorName So, Masatomo
	CreatorName Takahashi, Kazuma
	NRID 1000070262079 1000070262079 CreatorName Tagawa, Yoh-ichi
	NRID 1000080112027 1000080112027 CreatorName Hirao, Masahiko
	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	Kichitaro Nakajima, Masatomo So, Kazuma Takahashi, Yoh-ichi Tagawa, Masahiko Hirao, Yuji Goto, and Hirotsugu Ogi. Optimized Ultrasonic Irradiation Finds Out Ultrastable Aβ₁₋₄₀ Oligomers. Journal of Physical Chemistry B, 2017, 121(12), 2603-2613. ©2017 American Chemical Society. https://doi.org/10.1021/acs.jpcb.7b01409.
Abstract	Oligomer species of amyloid β (Aβ) peptides are intensively investigated because of their relevance to Alzheimer's disease (AD), and a stable oligomer will be a cause of AD. In this article, we investigate the structural stability of two representative Aβ₁₋₄₀ oligomers, which are with and without the β-sheet structure, denoted by β and non-β oligomers, respectively, using optimized ultrasonic irradiation (OUI). Recent studies reveal that OUI significantly accelerates the fibril formation in Aβ₁₋₄₀ monomers; it is capable of transforming any unstable oligomers into fibrils (the dead-end products) in a short time. First, we find that β oligomers can be produced under high-speed stirring agitation; their β-sheet structures are evaluated by the circular-dichroism spectrum measurement, by the immunoassay using the fibril-specific OC antibody, and by the seeding experiment, showing identical characteristics to those formed in previous reports. Second, we form non-β oligomers in a high-concentration NaCl solution and confirm that they include no β-sheet structure, and they are recognized by the oligomer-specific A11 antibody. Furthermore, we confirm the neurotoxicity of the two types of oligomers using the neural tissue derived from mouse embryonic stem cells. We apply the OUI agitation to the β and non-β oligomers. The non-β oligomers are transformed into the fibrils, indicating that they are intermediate species in the fibrillation pathway. However, the β oligomers are surprisingly unaffected by OUI, indicating their high thermodynamic stability. We conclude that the β oligomers should be the independent dead-end products of another pathway, different from the fibrillation pathway.
Publisher	American Chemical Society
Source Title	Journal of Physical Chemistry B
Volume (Issue)	121(12)
Page	2603-2613
Date of Issued	2017-03-30
Language	English
Handle URL	https://hdl.handle.net/11094/84142
PISSN	15206106
eISSN	15205207
NCID	AA11114073
Relation.isVersionOf	DOI (Publisher Version) https://doi.org/10.1021/acs.jpcb.7b01409
Relation.isIdenticalTo	PMID 28260388
Access Rights	open access
CopyRight	This document is the Accepted Manuscript version of a Published Work that appeared in final form in The Journal of Physical Chemistry B, © 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.jpcb.7b01409.
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 B. 2017, 121(12), p. 2603-2613
DC.title	Optimized Ultrasonic Irradiation Finds Out Ultrastable Aβ₁₋₄₀ Oligomers
DC.creator	Nakajima, Kichitaro
	So, Masatomo
	Takahashi, Kazuma
	Tagawa, Yoh-ichi
	Hirao, Masahiko
	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	2017-03-30
DC.identifier	https://doi.org/10.1021/acs.jpcb.7b01409
DC.description	Kichitaro Nakajima, Masatomo So, Kazuma Takahashi, Yoh-ichi Tagawa, Masahiko Hirao, Yuji Goto, and Hirotsugu Ogi. Optimized Ultrasonic Irradiation Finds Out Ultrastable Aβ₁₋₄₀ Oligomers. Journal of Physical Chemistry B, 2017, 121(12), 2603-2613. ©2017 American Chemical Society. https://doi.org/10.1021/acs.jpcb.7b01409.
DCTERMS.abstract	Oligomer species of amyloid β (Aβ) peptides are intensively investigated because of their relevance to Alzheimer's disease (AD), and a stable oligomer will be a cause of AD. In this article, we investigate the structural stability of two representative Aβ₁₋₄₀ oligomers, which are with and without the β-sheet structure, denoted by β and non-β oligomers, respectively, using optimized ultrasonic irradiation (OUI). Recent studies reveal that OUI significantly accelerates the fibril formation in Aβ₁₋₄₀ monomers; it is capable of transforming any unstable oligomers into fibrils (the dead-end products) in a short time. First, we find that β oligomers can be produced under high-speed stirring agitation; their β-sheet structures are evaluated by the circular-dichroism spectrum measurement, by the immunoassay using the fibril-specific OC antibody, and by the seeding experiment, showing identical characteristics to those formed in previous reports. Second, we form non-β oligomers in a high-concentration NaCl solution and confirm that they include no β-sheet structure, and they are recognized by the oligomer-specific A11 antibody. Furthermore, we confirm the neurotoxicity of the two types of oligomers using the neural tissue derived from mouse embryonic stem cells. We apply the OUI agitation to the β and non-β oligomers. The non-β oligomers are transformed into the fibrils, indicating that they are intermediate species in the fibrillation pathway. However, the β oligomers are surprisingly unaffected by OUI, indicating their high thermodynamic stability. We conclude that the β oligomers should be the independent dead-end products of another pathway, different from the fibrillation pathway.
DC.rights	This document is the Accepted Manuscript version of a Published Work that appeared in final form in The Journal of Physical Chemistry B, © 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.jpcb.7b01409.
DC.format	84142
citation_title	Optimized Ultrasonic Irradiation Finds Out Ultrastable Aβ₁₋₄₀ Oligomers
citation_author	Nakajima, Kichitaro
	So, Masatomo
	Takahashi, Kazuma
	Tagawa, Yoh-ichi
	Hirao, Masahiko
	Goto, Yuji
	Ogi, Hirotsugu
citation_publisher	American Chemical Society
citation_language	English
citation_date	2017-03-30
citation_journal_title	Journal of Physical Chemistry B
citation_volume	121
citation_issue	12
citation_firstpage	2603
citation_lastpage	2613
citation_doi	https://doi.org/10.1021/acs.jpcb.7b01409
citation_pmid	28260388
citation_public_url	https://hdl.handle.net/11094/84142

Optimized Ultrasonic Irradiation Finds Out Ultrastable Aβ₁₋₄₀ Oligomers

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