Real-time and Single Fibril Observation of the Formation of Amyloid β Spherulitic Structures

Ban, Tadato; Morigaki, Kenichi; Yagi, Hisashi; Kawasaki, Takashi; Kobayashi, Atsuko; Yuba, Shunsuke; Naiki, Hironobu; Goto, Yuji

doi:https://doi.org/10.1074/jbc.M606072200

Real-time and Single Fibril Observation of the Formation of Amyloid β Spherulitic Structures

Ban, Tadato; Morigaki, Kenichi; Yagi, Hisashi et al.

Journal of Biological Chemistry, 2006, 281(44), 33677-33683

アクセス数:769件（2025-07-06 09:30 集計）

固定URL: https://hdl.handle.net/11094/71291

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タイトル	Real-time and Single Fibril Observation of the Formation of Amyloid β Spherulitic Structures
著者	NRID 1000000579667 1000000579667 著者名 Ban, Tadato
	著者名 Morigaki, Kenichi
	NRID 1000010432494 1000010432494 著者名 Yagi, Hisashi
	NRID 1000060356839 1000060356839 著者名 Kawasaki, Takashi
	著者名 Kobayashi, Atsuko
	NRID 1000040263248 1000040263248 著者名 Yuba, Shunsuke
	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. Tadato Ban, Kenichi Morigaki, Hisashi Yagi, Takashi Kawasaki, Atsuko Kobayashi, Shunsuke Yuba, Hironobu Naiki and Yuji Goto. Real-time and Single Fibril Observation of the Formation of Amyloid β Spherulitic Structures. J. Biol. Chem. 2006; 281, 33677–33683. © the American Society for Biochemistry and Molecular Biology
抄録	In Alzheimer disease, amyloid β, a 39-43-residue peptide produced by cleavage from a large amyloid precursor protein, undergoes conformational change to form amyloid fibrils and deposits as senile amyloid plaques in the extracellular cerebral cortices of the brain. However, the mechanism of how the intrinsically linear amyloid fibrils form spherical senile plaques is unknown. With total internal reflection fluorescence microscopy combined with the use of thioflavin T, an amyloid-specific fluorescence dye, we succeeded in observing the formation of the senile plaque-like spherulitic structures with diameters of around 15 μm on the chemically modified quartz surface. Real-time observation at a single fibrillar level revealed that, in the absence of tight contact with the surface, the cooperative and radial growth of amyloid fibrils from the core leads to a huge spherulitic structure. The results suggest the underlying physicochemical mechanism of senile plaque formation, essential for obtaining insight into prevention of Alzheimer disease.
出版者	American Society for Biochemistry and Molecular Biology
収録物名	Journal of Biological Chemistry
巻(号)	281(44)
ページ	33677-33683
刊行年月	2006-11
言語	英語
ハンドルURL	https://hdl.handle.net/11094/71291
eISSN	1083351X
NCID	AA1202460X
関連情報 (isIdenticalTo)	DOI (出版社版) https://doi.org/10.1074/jbc.M606072200
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. 2006, 281(44), p. 33677-33683
DC.title	Real-time and Single Fibril Observation of the Formation of Amyloid β Spherulitic Structures
DC.creator	Ban, Tadato
	Morigaki, Kenichi
	Yagi, Hisashi
	Kawasaki, Takashi
	Kobayashi, Atsuko
	Yuba, Shunsuke
	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	2006-11
DC.identifier	https://doi.org/10.1074/jbc.M606072200
DC.description	This research was originally published in the Journal of Biological Chemistry. Tadato Ban, Kenichi Morigaki, Hisashi Yagi, Takashi Kawasaki, Atsuko Kobayashi, Shunsuke Yuba, Hironobu Naiki and Yuji Goto. Real-time and Single Fibril Observation of the Formation of Amyloid β Spherulitic Structures. J. Biol. Chem. 2006; 281, 33677–33683. © the American Society for Biochemistry and Molecular Biology
DCTERMS.abstract	In Alzheimer disease, amyloid β, a 39-43-residue peptide produced by cleavage from a large amyloid precursor protein, undergoes conformational change to form amyloid fibrils and deposits as senile amyloid plaques in the extracellular cerebral cortices of the brain. However, the mechanism of how the intrinsically linear amyloid fibrils form spherical senile plaques is unknown. With total internal reflection fluorescence microscopy combined with the use of thioflavin T, an amyloid-specific fluorescence dye, we succeeded in observing the formation of the senile plaque-like spherulitic structures with diameters of around 15 μm on the chemically modified quartz surface. Real-time observation at a single fibrillar level revealed that, in the absence of tight contact with the surface, the cooperative and radial growth of amyloid fibrils from the core leads to a huge spherulitic structure. The results suggest the underlying physicochemical mechanism of senile plaque formation, essential for obtaining insight into prevention of Alzheimer disease.
DC.format	71291
citation_title	Real-time and Single Fibril Observation of the Formation of Amyloid β Spherulitic Structures
citation_author	Ban, Tadato
	Morigaki, Kenichi
	Yagi, Hisashi
	Kawasaki, Takashi
	Kobayashi, Atsuko
	Yuba, Shunsuke
	Naiki, Hironobu
	Goto, Yuji
citation_publisher	American Society for Biochemistry and Molecular Biology
citation_language	英語
citation_date	2006-11
citation_journal_title	Journal of Biological Chemistry
citation_volume	281
citation_issue	44
citation_firstpage	33677
citation_lastpage	33683
citation_doi	https://doi.org/10.1074/jbc.M606072200
citation_public_url	https://hdl.handle.net/11094/71291

Real-time and Single Fibril Observation of the Formation of Amyloid β Spherulitic Structures

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