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

Number of Access:827（2025-08-30 01:46 Counts）

Identifier to cite or link to this item: https://hdl.handle.net/11094/71291

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Title	Real-time and Single Fibril Observation of the Formation of Amyloid β Spherulitic Structures
Creator	NRID 1000000579667 1000000579667 CreatorName Ban, Tadato
	CreatorName Morigaki, Kenichi
	NRID 1000010432494 1000010432494 CreatorName Yagi, Hisashi
	NRID 1000060356839 1000060356839 CreatorName Kawasaki, Takashi
	CreatorName Kobayashi, Atsuko
	NRID 1000040263248 1000040263248 CreatorName Yuba, Shunsuke
	NRID 1000010227704 1000010227704 CreatorName Naiki, Hironobu
	NRID 1000040153770 1000040153770 researchmap permalink read0014440 read0014440 CreatorName Goto, Yuji
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
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.
Publisher	American Society for Biochemistry and Molecular Biology
Source Title	Journal of Biological Chemistry
Volume (Issue)	281(44)
Page	33677-33683
Date of Issued	2006-11
Language	English
Handle URL	https://hdl.handle.net/11094/71291
eISSN	1083351X
NCID	AA1202460X
Relation.isIdenticalTo	DOI (Publisher Version) https://doi.org/10.1074/jbc.M606072200
Access Rights	open access
oaire:version	Version of Record
Category	学術雑誌論文 Journal Article

Resource Type	journal article
Local Type	Journal Article
DCMI Type	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	English
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	English
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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