Optimized sonoreactor for accelerative amyloid-fibril assays through enhancement of primary nucleation and fragmentation

Nakajima, Kichitaro; Noi, Kentaro; Yamaguchi, Keiichi; So, Masatomo; Ikenaka, Kensuke; Mochizuki, Hideki; Ogi, Hirotsugu; Goto, Yuji

doi:https://doi.org/10.1016/j.ultsonch.2021.105508

Optimized sonoreactor for accelerative amyloid-fibril assays through enhancement of primary nucleation and fragmentation

Nakajima, Kichitaro; Noi, Kentaro; Yamaguchi, Keiichi et al.

Ultrasonics Sonochemistry, 2021, 73, 105508

Number of Access:1,347（2025-08-14 12:04 Counts）

Identifier to cite or link to this item: https://hdl.handle.net/11094/84201

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Title	Optimized sonoreactor for accelerative amyloid-fibril assays through enhancement of primary nucleation and fragmentation
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 1000030588405 1000030588405 CreatorName Noi, Kentaro
	NRID 1000090432187 1000090432187 researchmap permalink read0105908 read0105908 Scopus Author ID 8731908100 8731908100 CreatorName Yamaguchi, Keiichi
	NRID 1000040746335 1000040746335 CreatorName So, Masatomo
	NRID 1000070774058 1000070774058 researchmap permalink kensukeikenaka kensukeikenaka Scopus Author ID 8588484300 8588484300 CreatorName Ikenaka, Kensuke
	NRID 1000090230044 1000090230044 ORCID 0000-0002-0874-7542 0000-0002-0874-7542 researchmap permalink read0207787 read0207787 Scopus Author ID 7202006099 7202006099 CreatorName Mochizuki, Hideki
	NRID 1000090252626 1000090252626 researchmap permalink read0042771 read0042771 Scopus Author ID 35563683500 35563683500 CreatorName Ogi, Hirotsugu
	NRID 1000040153770 1000040153770 researchmap permalink read0014440 read0014440 CreatorName Goto, Yuji
Subject	Amyloid fibril
	Fragmentation
	Nucleation
	Sonocrystallization
	Sonoreactor
	Supersaturation
Description	Nakajima K., Noi K., Yamaguchi K., et al. Optimized sonoreactor for accelerative amyloid-fibril assays through enhancement of primary nucleation and fragmentation. Ultrasonics Sonochemistry, 73, 105508, 2021. https://doi.org/10.1016/j.ultsonch.2021.105508.
Abstract	Ultrasonication to supersaturated protein solutions forcibly forms amyloid fibrils, thereby allowing the early-stage diagnosis for amyloidoses. Previously, we constructed a high-throughput sonoreactor to investigate features of the amyloid-fibril nucleation. Although the instrument substantiated the ultrasonication efficacy, several challenges remain; the key is the precise control of the acoustic field in the reactor, which directly affects the fibril-formation reaction. In the present study, we develop the optimized sonoreactor for the amyloid-fibril assay, which improves the reproducibility and controllability of the fibril formation. Using β2-microglobulin, we experimentally demonstrate that achieving identical acoustic conditions by controlling oscillation amplitude and frequency of each transducer results in identical fibril-formation behavior across 36 solutions. Moreover, we succeed in detecting the 100-fM seeds using the developed sonoreactor at an accelerated rate. Finally, we reveal that the acceleration of the fibril-formation reaction with the seeds is achieved by enhancing the primary nucleation and the fibril fragmentation through the analysis of the fibril-formation kinetics. These results demonstrate the efficacy of the developed sonoreactor for the diagnosis of amyloidoses owing to the accelerative seed detection and the possibility for further early-stage diagnosis even without seeds through the accelerated primary nucleation.
Publisher	Elsevier B.V.
Source Title	Ultrasonics Sonochemistry
Volume (Issue)	73
Page	105508
Date of Issued	2021-03-03
Language	English
Handle URL	https://hdl.handle.net/11094/84201
PISSN	13504177
eISSN	18732828
NCID	AA11024447
NCID	AA11541041
Relation.isIdenticalTo	DOI (Publisher Version) https://doi.org/10.1016/j.ultsonch.2021.105508
Relation.isIdenticalTo	PMID 33770746
Access Rights	open access
CopyRight	© 2021 The Author(s). Published by Elsevier B.V. This article is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 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	Ultrasonics Sonochemistry. 2021, 73, p. 105508
DC.title	Optimized sonoreactor for accelerative amyloid-fibril assays through enhancement of primary nucleation and fragmentation
DC.creator	Nakajima, Kichitaro
	Noi, Kentaro
	Yamaguchi, Keiichi
	So, Masatomo
	Ikenaka, Kensuke
	Mochizuki, Hideki
	Ogi, Hirotsugu
	Goto, Yuji
DC.publisher	Elsevier B.V.
DC.language' scheme='DCTERMS.RFC1766	English
DC.type' scheme='DCTERMS.DCMIType	Text
DCTERMS.issued' scheme='DCTERMS.W3CDTF	2021-03-03
DC.identifier	https://doi.org/10.1016/j.ultsonch.2021.105508
DC.subject	Amyloid fibril
	Fragmentation
	Nucleation
	Sonocrystallization
	Sonoreactor
	Supersaturation
DC.description	Nakajima K., Noi K., Yamaguchi K., et al. Optimized sonoreactor for accelerative amyloid-fibril assays through enhancement of primary nucleation and fragmentation. Ultrasonics Sonochemistry, 73, 105508, 2021. https://doi.org/10.1016/j.ultsonch.2021.105508.
DCTERMS.abstract	Ultrasonication to supersaturated protein solutions forcibly forms amyloid fibrils, thereby allowing the early-stage diagnosis for amyloidoses. Previously, we constructed a high-throughput sonoreactor to investigate features of the amyloid-fibril nucleation. Although the instrument substantiated the ultrasonication efficacy, several challenges remain; the key is the precise control of the acoustic field in the reactor, which directly affects the fibril-formation reaction. In the present study, we develop the optimized sonoreactor for the amyloid-fibril assay, which improves the reproducibility and controllability of the fibril formation. Using β2-microglobulin, we experimentally demonstrate that achieving identical acoustic conditions by controlling oscillation amplitude and frequency of each transducer results in identical fibril-formation behavior across 36 solutions. Moreover, we succeed in detecting the 100-fM seeds using the developed sonoreactor at an accelerated rate. Finally, we reveal that the acceleration of the fibril-formation reaction with the seeds is achieved by enhancing the primary nucleation and the fibril fragmentation through the analysis of the fibril-formation kinetics. These results demonstrate the efficacy of the developed sonoreactor for the diagnosis of amyloidoses owing to the accelerative seed detection and the possibility for further early-stage diagnosis even without seeds through the accelerated primary nucleation.
DC.rights	© 2021 The Author(s). Published by Elsevier B.V. This article is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License.
DC.format	84201
citation_title	Optimized sonoreactor for accelerative amyloid-fibril assays through enhancement of primary nucleation and fragmentation
citation_author	Nakajima, Kichitaro
	Noi, Kentaro
	Yamaguchi, Keiichi
	So, Masatomo
	Ikenaka, Kensuke
	Mochizuki, Hideki
	Ogi, Hirotsugu
	Goto, Yuji
citation_publisher	Elsevier B.V.
citation_language	English
citation_date	2021-03-03
citation_journal_title	Ultrasonics Sonochemistry
citation_volume	73
citation_firstpage	105508
citation_doi	https://doi.org/10.1016/j.ultsonch.2021.105508
citation_pmid	33770746
citation_public_url	https://hdl.handle.net/11094/84201

Optimized sonoreactor for accelerative amyloid-fibril assays through enhancement of primary nucleation and fragmentation

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