Real-time and Single Fibril Observation of the Formation of Amyloid β Spherulitic Structures
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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
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.
収録刊行物
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- Journal of Biological Chemistry
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Journal of Biological Chemistry 281 (44), 33677-33683, 2006-11
American Society for Biochemistry and Molecular Biology
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詳細情報 詳細情報について
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- CRID
- 1050862643879053824
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- NII論文ID
- 120006557651
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- NII書誌ID
- AA1202460X
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- ISSN
- 1083351X
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- HANDLE
- 11094/71291
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- 本文言語コード
- en
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- 資料種別
- journal article
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- データソース種別
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- IRDB
- CiNii Articles