Viscoelasticity Response during Fibrillation of Amyloid β Peptides on a Quartz-Crystal-Microbalance Biosensor

Lai, Yen Ting; Ogi, Hirotsugu; Noi, Kentaro; Kato, Fumihito

doi:https://doi.org/10.1021/acs.langmuir.8b00639

Viscoelasticity Response during Fibrillation of Amyloid β Peptides on a Quartz-Crystal-Microbalance Biosensor

Lai, Yen Ting; Ogi, Hirotsugu; Noi, Kentaro et al.

Langmuir, 2018, 34(19), 5474-5479

Number of Access:457（2025-11-25 02:18 Counts）

Identifier to cite or link to this item: https://hdl.handle.net/11094/84143

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Title	Viscoelasticity Response during Fibrillation of Amyloid β Peptides on a Quartz-Crystal-Microbalance Biosensor
Creator	CreatorName Lai, Yen Ting
	NRID 1000090252626 1000090252626 researchmap permalink read0042771 read0042771 Scopus Author ID 35563683500 35563683500 ORCID 0000-0002-9602-5194 0000-0002-9602-5194 CreatorName Ogi, Hirotsugu
	NRID 1000030588405 1000030588405 CreatorName Noi, Kentaro
	NRID 1000070780170 1000070780170 CreatorName Kato, Fumihito
Description	Yen-Ting Lai, Hirotsugu Ogi, Kentaro Noi, and Fumihito Kato. Viscoelasticity Response during Fibrillation of Amyloid β Peptides on a Quartz-Crystal-Microbalance Biosensor. Langmuir, 2018, 34(19), 5474-5479. ©2018 American Chemical Society. https://doi.org/10.1021/acs.langmuir.8b00639.
Abstract	Unlike previous in vitro measurements where Amyloid β (Aβ) aggregation was studied in bulk solutions, we detect the structure change of the Aβ aggregate on the surface of a wireless quartz-crystal-microbalance biosensor, which resembles more closely the aggregation process on the cell membrane. Using a 58 MHz quartz crystal, we monitored changes in the viscoelastic properties of the aggregate formed on the quartz surface from monomers to oligomers and then to fibrils, involving up to the 7th overtone mode (406 MHz). With atomic-force microscopy observations, we found a significant stiffness increase as well as thinning of the protein layer during the structure change from oligomer to fibrils at 20 h, which indicates that the stiffness of the fibril is much higher. Viscoelasticity can provide a significant index of fibrillation and can be useful for evaluating inhibitory medicines in drug development.
Publisher	American Chemical Society
Source Title	Langmuir
Volume (Issue)	34(19)
Page	5474-5479
Date of Issued	2018-05-15
Language	English
Handle URL	https://hdl.handle.net/11094/84143
PISSN	07437463
eISSN	15205827
NCID	AA10461730
Relation.isVersionOf	DOI (Publisher Version) https://doi.org/10.1021/acs.langmuir.8b00639
Relation.isIdenticalTo	PMID 29697982
Access Rights	open access
CopyRight	This document is the Accepted Manuscript version of a Published Work that appeared in final form in Langmuir, © 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.langmuir.8b00639.
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	Langmuir. 2018, 34(19), p. 5474-5479
DC.title	Viscoelasticity Response during Fibrillation of Amyloid β Peptides on a Quartz-Crystal-Microbalance Biosensor
DC.creator	Lai, Yen Ting
	Ogi, Hirotsugu
	Noi, Kentaro
	Kato, Fumihito
DC.publisher	American Chemical Society
DC.language' scheme='DCTERMS.RFC1766	English
DC.type' scheme='DCTERMS.DCMIType	Text
DCTERMS.issued' scheme='DCTERMS.W3CDTF	2018-05-15
DC.identifier	https://doi.org/10.1021/acs.langmuir.8b00639
DC.description	Yen-Ting Lai, Hirotsugu Ogi, Kentaro Noi, and Fumihito Kato. Viscoelasticity Response during Fibrillation of Amyloid β Peptides on a Quartz-Crystal-Microbalance Biosensor. Langmuir, 2018, 34(19), 5474-5479. ©2018 American Chemical Society. https://doi.org/10.1021/acs.langmuir.8b00639.
DCTERMS.abstract	Unlike previous in vitro measurements where Amyloid β (Aβ) aggregation was studied in bulk solutions, we detect the structure change of the Aβ aggregate on the surface of a wireless quartz-crystal-microbalance biosensor, which resembles more closely the aggregation process on the cell membrane. Using a 58 MHz quartz crystal, we monitored changes in the viscoelastic properties of the aggregate formed on the quartz surface from monomers to oligomers and then to fibrils, involving up to the 7th overtone mode (406 MHz). With atomic-force microscopy observations, we found a significant stiffness increase as well as thinning of the protein layer during the structure change from oligomer to fibrils at 20 h, which indicates that the stiffness of the fibril is much higher. Viscoelasticity can provide a significant index of fibrillation and can be useful for evaluating inhibitory medicines in drug development.
DC.rights	This document is the Accepted Manuscript version of a Published Work that appeared in final form in Langmuir, © 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.langmuir.8b00639.
DC.format	84143
citation_title	Viscoelasticity Response during Fibrillation of Amyloid β Peptides on a Quartz-Crystal-Microbalance Biosensor
citation_author	Lai, Yen Ting
	Ogi, Hirotsugu
	Noi, Kentaro
	Kato, Fumihito
citation_publisher	American Chemical Society
citation_language	English
citation_date	2018-05-15
citation_journal_title	Langmuir
citation_volume	34
citation_issue	19
citation_firstpage	5474
citation_lastpage	5479
citation_doi	https://doi.org/10.1021/acs.langmuir.8b00639
citation_pmid	29697982
citation_public_url	https://hdl.handle.net/11094/84143

Viscoelasticity Response during Fibrillation of Amyloid β Peptides on a Quartz-Crystal-Microbalance Biosensor

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