Flow-induced Alignment of Amyloid Protofilaments Revealed by Linear Dichroism

Adachi, Rumi; Yamaguchi, Kei-ichi; Yagi, Hisashi; Sakurai, Kazumasa; Naiki, Hironobu; Goto, Yuji

doi:https://doi.org/10.1074/jbc.M611738200

Flow-induced Alignment of Amyloid Protofilaments Revealed by Linear Dichroism

Adachi, Rumi; Yamaguchi, Kei-ichi; Yagi, Hisashi et al.

Journal of Biological Chemistry, 2007, 282(12), 8978-8983

アクセス数:645件（2025-07-11 16:37 集計）

固定URL: https://hdl.handle.net/11094/71289

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タイトル	Flow-induced Alignment of Amyloid Protofilaments Revealed by Linear Dichroism
著者	著者名 Adachi, Rumi
	NRID 1000090432187 1000090432187 researchmap permalink read0105908 read0105908 Scopus Author ID 8731908100 8731908100 著者名 Yamaguchi, Kei-ichi
	NRID 1000010432494 1000010432494 著者名 Yagi, Hisashi
	NRID 1000010403015 1000010403015 著者名 Sakurai, Kazumasa
	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. Rumi Adachi, Kei-ichi Yamaguchi, Hisashi Yagi, Kazumasa Sakurai, Hironobu Naiki and Yuji Goto. Flow-induced Alignment of Amyloid Protofilaments Revealed by Linear Dichroism. J. Biol. Chem. 2007; 282, 8978-8983. © the American Society for Biochemistry and Molecular Biology
抄録	Amyloid fibrils underlying various serious amyloidoses including Alzheimer and prion diseases form characteristic deposits in which linear fibrils with an unbranched and rigid morphology associate laterally or radially, e.g. radial senile amyloid plaques of amyloid β. To clarify the formation of these high order amyloid deposits, studying the rheology is important. A 22-residue K3 peptide fragment of β2-microglobulin, a protein responsible for dialysis-related amyloidosis, forms long and homogeneous protofilament-like fibrils in 20% (v/v) 2,2,2-trifluoroethanol and 10 mm HCl (pH ∼2). Here, using circular dichroism and linear dichroism, we observed the flow-induced alignment of fibrils. Analysis of far- and near-UV linear dichroism spectra suggested that both the net π-π* transition moment of the backbone carbonyl group and Lb transition moment of the Tyr26 side chain are oriented in parallel to the fibril axis, revealing the structural details of amyloid protofilaments. Moreover, the intensities of flow-induced circular dichroism or linear dichroism signals depended critically on the length and type of fibrils, suggesting that they are useful for detecting and characterizing amyloid fibrils.
出版者	American Society for Biochemistry and Molecular Biology
収録物名	Journal of Biological Chemistry
巻(号)	282(12)
ページ	8978-8983
刊行年月	2007-03
言語	英語
ハンドルURL	https://hdl.handle.net/11094/71289
eISSN	1083351X
NCID	AA1202458X
関連情報 (isIdenticalTo)	DOI (出版社版) https://doi.org/10.1074/jbc.M611738200
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. 2007, 282(12), p. 8978-8983
DC.title	Flow-induced Alignment of Amyloid Protofilaments Revealed by Linear Dichroism
DC.creator	Adachi, Rumi
	Yamaguchi, Kei-ichi
	Yagi, Hisashi
	Sakurai, Kazumasa
	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	2007-03
DC.identifier	https://doi.org/10.1074/jbc.M611738200
DC.description	This research was originally published in the Journal of Biological Chemistry. Rumi Adachi, Kei-ichi Yamaguchi, Hisashi Yagi, Kazumasa Sakurai, Hironobu Naiki and Yuji Goto. Flow-induced Alignment of Amyloid Protofilaments Revealed by Linear Dichroism. J. Biol. Chem. 2007; 282, 8978-8983. © the American Society for Biochemistry and Molecular Biology
DCTERMS.abstract	Amyloid fibrils underlying various serious amyloidoses including Alzheimer and prion diseases form characteristic deposits in which linear fibrils with an unbranched and rigid morphology associate laterally or radially, e.g. radial senile amyloid plaques of amyloid β. To clarify the formation of these high order amyloid deposits, studying the rheology is important. A 22-residue K3 peptide fragment of β2-microglobulin, a protein responsible for dialysis-related amyloidosis, forms long and homogeneous protofilament-like fibrils in 20% (v/v) 2,2,2-trifluoroethanol and 10 mm HCl (pH ∼2). Here, using circular dichroism and linear dichroism, we observed the flow-induced alignment of fibrils. Analysis of far- and near-UV linear dichroism spectra suggested that both the net π-π* transition moment of the backbone carbonyl group and Lb transition moment of the Tyr26 side chain are oriented in parallel to the fibril axis, revealing the structural details of amyloid protofilaments. Moreover, the intensities of flow-induced circular dichroism or linear dichroism signals depended critically on the length and type of fibrils, suggesting that they are useful for detecting and characterizing amyloid fibrils.
DC.format	71289
citation_title	Flow-induced Alignment of Amyloid Protofilaments Revealed by Linear Dichroism
citation_author	Adachi, Rumi
	Yamaguchi, Kei-ichi
	Yagi, Hisashi
	Sakurai, Kazumasa
	Naiki, Hironobu
	Goto, Yuji
citation_publisher	American Society for Biochemistry and Molecular Biology
citation_language	英語
citation_date	2007-03
citation_journal_title	Journal of Biological Chemistry
citation_volume	282
citation_issue	12
citation_firstpage	8978
citation_lastpage	8983
citation_doi	https://doi.org/10.1074/jbc.M611738200
citation_public_url	https://hdl.handle.net/11094/71289

Flow-induced Alignment of Amyloid Protofilaments Revealed by Linear Dichroism

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