Disaggregation Behavior of Amyloid β Fibrils by Anthocyanins Studied by Total-Internal-Reflection-Fluorescence Microscopy Coupled with a Wireless Quartz-Crystal Microbalance Biosensor

Noi, Kentaro; Ikenaka, Kensuke; Mochizuki, Hideki; Goto, Yuji; Ogi, Hirotsugu

doi:https://doi.org/10.1021/acs.analchem.1c01720

Disaggregation Behavior of Amyloid β Fibrils by Anthocyanins Studied by Total-Internal-Reflection-Fluorescence Microscopy Coupled with a Wireless Quartz-Crystal Microbalance Biosensor

Noi, Kentaro; Ikenaka, Kensuke; Mochizuki, Hideki et al.

Analytical Chemistry, 2021, 93(32), 11176-11183

アクセス数:738件（2025-08-15 08:15 集計）

固定URL: https://hdl.handle.net/11094/93315

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タイトル	Disaggregation Behavior of Amyloid β Fibrils by Anthocyanins Studied by Total-Internal-Reflection-Fluorescence Microscopy Coupled with a Wireless Quartz-Crystal Microbalance Biosensor
著者	NRID 1000030588405 1000030588405 著者名 Noi, Kentaro
	NRID 1000070774058 1000070774058 researchmap permalink kensukeikenaka kensukeikenaka Scopus Author ID 8588484300 8588484300 著者名 Ikenaka, Kensuke
	NRID 1000090230044 1000090230044 ORCID 0000-0002-0874-7542 0000-0002-0874-7542 researchmap permalink read0207787 read0207787 Scopus Author ID 7202006099 7202006099 著者名 Mochizuki, Hideki
	NRID 1000040153770 1000040153770 著者名 Goto, Yuji
	NRID 1000090252626 1000090252626 researchmap permalink read0042771 read0042771 Scopus Author ID 35563683500 35563683500 著者名 Ogi, Hirotsugu
内容	Noi K., Ikenaka K., Mochizuki H., et al. Disaggregation Behavior of Amyloid β Fibrils by Anthocyanins Studied by Total-Internal-Reflection-Fluorescence Microscopy Coupled with a Wireless Quartz-Crystal Microbalance Biosensor. Analytical Chemistry, 93(32), 11176-11183, August 17, 2021. Copyright © 2021, American Chemical Society. https://doi.org/10.1021/acs.analchem.1c01720.
抄録	Amyloid fibrils are formed from various proteins, some of which cause the corresponding neurodegenerative disorders, such as Alzheimer's and Parkinson's diseases. It has been reported that many compounds inhibit the formation of amyloid fibrils. Anthocyanins are flavonoid pigments present in fruits and vegetables, which are known to suppress symptoms related with Alzheimer's disease. However, the influence of anthocyanins on the amyloid fibril remains unclear. Here, we succeeded in the direct monitoring of the disaggregation reaction of single amyloid β (Aβ) fibrils by anthocyanins using total-internal-reflection-fluorescence microscopy with a quartz-crystal microbalance (TIRFM-QCM). It is found that the disassembly activity to the Aβ fibrils depends on the number of hydroxyl groups in six-membered ring B of anthocyanin, and only delphinidin-3-galactoside, possessing three hydroxyl groups there, shows high disassembly activity. Our results show the importance of the number of hydroxyl groups and demonstrate the usefulness of TIRFM-QCM as a powerful tool in studying interactions between amyloid fibrils and compounds.
出版者	American Chemical Society
収録物名	Analytical Chemistry
巻(号)	93(32)
ページ	11176-11183
刊行年月	2021-08-17
言語	英語
ハンドルURL	https://hdl.handle.net/11094/93315
PISSN	00032700
eISSN	15206882
関連情報 (isIdenticalTo)	DOI (出版社版) https://doi.org/10.1021/acs.analchem.1c01720
アクセス権	open access
権利情報	This article is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License.
出版タイプ	Version of Record
カテゴリ	学術雑誌論文 Journal Article

資源タイプ	学術雑誌論文
ローカル資源タイプ	学術雑誌論文
DCMI資源タイプ	text
DCTERMS.bibliographicCitation	Analytical Chemistry. 2021, 93(32), p. 11176-11183
DC.title	Disaggregation Behavior of Amyloid β Fibrils by Anthocyanins Studied by Total-Internal-Reflection-Fluorescence Microscopy Coupled with a Wireless Quartz-Crystal Microbalance Biosensor
DC.creator	Noi, Kentaro
	Ikenaka, Kensuke
	Mochizuki, Hideki
	Goto, Yuji
	Ogi, Hirotsugu
DC.publisher	American Chemical Society
DC.language' scheme='DCTERMS.RFC1766	英語
DC.type' scheme='DCTERMS.DCMIType	text
DCTERMS.issued' scheme='DCTERMS.W3CDTF	2021-08-17
DC.identifier	https://doi.org/10.1021/acs.analchem.1c01720
DC.description	Noi K., Ikenaka K., Mochizuki H., et al. Disaggregation Behavior of Amyloid β Fibrils by Anthocyanins Studied by Total-Internal-Reflection-Fluorescence Microscopy Coupled with a Wireless Quartz-Crystal Microbalance Biosensor. Analytical Chemistry, 93(32), 11176-11183, August 17, 2021. Copyright © 2021, American Chemical Society. https://doi.org/10.1021/acs.analchem.1c01720.
DCTERMS.abstract	Amyloid fibrils are formed from various proteins, some of which cause the corresponding neurodegenerative disorders, such as Alzheimer's and Parkinson's diseases. It has been reported that many compounds inhibit the formation of amyloid fibrils. Anthocyanins are flavonoid pigments present in fruits and vegetables, which are known to suppress symptoms related with Alzheimer's disease. However, the influence of anthocyanins on the amyloid fibril remains unclear. Here, we succeeded in the direct monitoring of the disaggregation reaction of single amyloid β (Aβ) fibrils by anthocyanins using total-internal-reflection-fluorescence microscopy with a quartz-crystal microbalance (TIRFM-QCM). It is found that the disassembly activity to the Aβ fibrils depends on the number of hydroxyl groups in six-membered ring B of anthocyanin, and only delphinidin-3-galactoside, possessing three hydroxyl groups there, shows high disassembly activity. Our results show the importance of the number of hydroxyl groups and demonstrate the usefulness of TIRFM-QCM as a powerful tool in studying interactions between amyloid fibrils and compounds.
DC.rights	This article is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License.
DC.format	93315
citation_title	Disaggregation Behavior of Amyloid β Fibrils by Anthocyanins Studied by Total-Internal-Reflection-Fluorescence Microscopy Coupled with a Wireless Quartz-Crystal Microbalance Biosensor
citation_author	Noi, Kentaro
	Ikenaka, Kensuke
	Mochizuki, Hideki
	Goto, Yuji
	Ogi, Hirotsugu
citation_publisher	American Chemical Society
citation_language	英語
citation_date	2021-08-17
citation_journal_title	Analytical Chemistry
citation_volume	93
citation_issue	32
citation_firstpage	11176
citation_lastpage	11183
citation_doi	https://doi.org/10.1021/acs.analchem.1c01720
citation_public_url	https://hdl.handle.net/11094/93315

Disaggregation Behavior of Amyloid β Fibrils by Anthocyanins Studied by Total-Internal-Reflection-Fluorescence Microscopy Coupled with a Wireless Quartz-Crystal Microbalance Biosensor

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