Destruction of Amyloid Fibrils of a β2-Microglobulin Fragment by Laser Beam Irradiation

Ozawa, Daisaku; Yagi, Hisashi; Ban, Tadato; Kameda, Atsushi; Kawakami, Toru; Naiki, Hironobu; Goto, Yuji

doi:https://doi.org/10.1074/jbc.M805118200

Destruction of Amyloid Fibrils of a β2-Microglobulin Fragment by Laser Beam Irradiation

Ozawa, Daisaku; Yagi, Hisashi; Ban, Tadato et al.

Journal of Biological Chemistry, 2009, 284(2), 1009-1017

アクセス数:649件（2025-07-11 21:40 集計）

固定URL: https://hdl.handle.net/11094/71288

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タイトル	Destruction of Amyloid Fibrils of a β2-Microglobulin Fragment by Laser Beam Irradiation
著者	NRID 1000060554524 1000060554524 著者名 Ozawa, Daisaku
	NRID 1000010432494 1000010432494 著者名 Yagi, Hisashi
	NRID 1000000579667 1000000579667 著者名 Ban, Tadato
	著者名 Kameda, Atsushi
	NRID 1000070273711 1000070273711 著者名 Kawakami, Toru
	NRID 1000010227704 1000010227704 著者名 Naiki, Hironobu
	NRID 1000040153770 1000040153770 researchmap permalink read0014440 read0014440 著者名 Goto, Yuji
内容	This research was originally published in the Journal of Biological Chemistry. Daisaku Ozawa, Hisashi Yagi, Tadato Ban, Atsushi Kameda, Toru Kawakami, Hironobu Naiki and Yuji Goto. Destruction of Amyloid Fibrils of a β2-Microglobulin Fragment by Laser Beam Irradiation. J. Biol. Chem. 2009; 284, 1009-1017. © the American Society for Biochemistry and Molecular Biology
抄録	To understand the mechanism by which amyloid fibrils form, we have been making real-time observations of the growth of individual fibrils, using total internal fluorescence microscopy combined with an amyloid-specific fluorescence dye, thioflavin T (ThT). At neutral pH, irradiation at 442 nm with a laser beam to excite ThT inhibited the fibril growth of β2-microglobulin (β2-m), a major component of amyloid fibrils deposited in patients with dialysis-related amyloidosis. Examination with a 22-residue K3 fragment of β2-m showed that the inhibition of fibril growth and moreover the destruction of preformed fibrils were coupled with the excitation of ThT. Several pieces of evidence suggest that the excited ThT transfers energy to ground state molecular oxygen, producing active oxygen, which causes various types of chemical modifications. The results imply a novel strategy for preventing the deposition of amyloid fibrils and for destroying preformed amyloid deposits.
出版者	American Society for Biochemistry and Molecular Biology
収録物名	Journal of Biological Chemistry
巻(号)	284(2)
ページ	1009-1017
刊行年月	2009-01
言語	英語
ハンドルURL	https://hdl.handle.net/11094/71288
eISSN	1083351X
NCID	AA1202457X
関連情報 (isIdenticalTo)	DOI (出版社版) https://doi.org/10.1074/jbc.M805118200
アクセス権	open access
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	Journal of Biological Chemistry. 2009, 284(2), p. 1009-1017
DC.title	Destruction of Amyloid Fibrils of a β2-Microglobulin Fragment by Laser Beam Irradiation
DC.creator	Ozawa, Daisaku
	Yagi, Hisashi
	Ban, Tadato
	Kameda, Atsushi
	Kawakami, Toru
	Naiki, Hironobu
	Goto, Yuji
DC.publisher	American Society for Biochemistry and Molecular Biology
DC.language' scheme='DCTERMS.RFC1766	英語
DC.type' scheme='DCTERMS.DCMIType	text
DCTERMS.issued' scheme='DCTERMS.W3CDTF	2009-01
DC.identifier	https://doi.org/10.1074/jbc.M805118200
DC.description	This research was originally published in the Journal of Biological Chemistry. Daisaku Ozawa, Hisashi Yagi, Tadato Ban, Atsushi Kameda, Toru Kawakami, Hironobu Naiki and Yuji Goto. Destruction of Amyloid Fibrils of a β2-Microglobulin Fragment by Laser Beam Irradiation. J. Biol. Chem. 2009; 284, 1009-1017. © the American Society for Biochemistry and Molecular Biology
DCTERMS.abstract	To understand the mechanism by which amyloid fibrils form, we have been making real-time observations of the growth of individual fibrils, using total internal fluorescence microscopy combined with an amyloid-specific fluorescence dye, thioflavin T (ThT). At neutral pH, irradiation at 442 nm with a laser beam to excite ThT inhibited the fibril growth of β2-microglobulin (β2-m), a major component of amyloid fibrils deposited in patients with dialysis-related amyloidosis. Examination with a 22-residue K3 fragment of β2-m showed that the inhibition of fibril growth and moreover the destruction of preformed fibrils were coupled with the excitation of ThT. Several pieces of evidence suggest that the excited ThT transfers energy to ground state molecular oxygen, producing active oxygen, which causes various types of chemical modifications. The results imply a novel strategy for preventing the deposition of amyloid fibrils and for destroying preformed amyloid deposits.
DC.format	71288
citation_title	Destruction of Amyloid Fibrils of a β2-Microglobulin Fragment by Laser Beam Irradiation
citation_author	Ozawa, Daisaku
	Yagi, Hisashi
	Ban, Tadato
	Kameda, Atsushi
	Kawakami, Toru
	Naiki, Hironobu
	Goto, Yuji
citation_publisher	American Society for Biochemistry and Molecular Biology
citation_language	英語
citation_date	2009-01
citation_journal_title	Journal of Biological Chemistry
citation_volume	284
citation_issue	2
citation_firstpage	1009
citation_lastpage	1017
citation_doi	https://doi.org/10.1074/jbc.M805118200
citation_public_url	https://hdl.handle.net/11094/71288

Destruction of Amyloid Fibrils of a β2-Microglobulin Fragment by Laser Beam Irradiation

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