Characterization of conformational dynamics of the active end of amyloid fibril to elucidate mechanisms underlying the fibril elongation
Project/Area Number |
23870043
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Research Category |
Grant-in-Aid for Research Activity Start-up
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Allocation Type | Single-year Grants |
Research Field |
Biophysics
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Research Institution | 大学共同利用機関法人自然科学研究機構(岡崎共通研究施設) (2012) National Institutes of Natural Sciences Okazaki Research Facilities (2011) |
Principal Investigator |
YAGI Maho 大学共同利用機関法人自然科学研究機構(岡崎共通研究施設), 岡崎統合バイオサイエンスセンター, 特任助教 (40608999)
|
Project Period (FY) |
2011 – 2012
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Project Status |
Completed (Fiscal Year 2012)
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Budget Amount *help |
¥3,250,000 (Direct Cost: ¥2,500,000、Indirect Cost: ¥750,000)
Fiscal Year 2012: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2011: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
|
Keywords | アミロイド / アルツハイマー病 / 抗体 / NMR / X線結晶構造解析 |
Research Abstract |
To characterize the conformational dynamics of the active end of amyloid fibril, we attempted to design small-sized amyloid fibril models. We successfully prepared tandem repeats of amyloid β (Aβ) molecules as minimal models of the amyloid fibrils by genetic manipulation. It was revealed that the tandem-repeat Aβ was recognized by the specific antibody directed against the end point of Aβ amyloid fibrils and served as nucleus which promoted the amyloid fibrillization. Furthermore, we found that bacterial molecular chaperones and ganglioside-embedding bicelles could suppress formation of Aβ fibrils.
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Report
(3 results)
Research Products
(40 results)
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[Journal Article] Protein encapsulation within synthetic molecular hosts2012
Author(s)
D. Fujita, K. Suzuki, S. Sato, M. Yagi-Utsumi, Y. Yamaguchi, N. Mizuno, T. Kumasaka, M. Takata, M. Noda, S. Uchiyama, K. Kato, and M. Fujita
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Journal Title
Nature Communications
Volume: 3
Issue: 1
Pages: 1093-1093
DOI
Related Report
Peer Reviewed
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[Journal Article] NMR and mutational identification of the collagen-binding site of the chaperone Hsp47.2012
Author(s)
Maho Yagi-Utsumi, Sumi Yoshikawa, Yoshiki Yamaguchi, Yohei Nishi, Eiji Kurimoto, Yoshihito Ishida, Takayuki Homma, Jun Hoseki, Yoshimi Nishikawa, Takaki Koide, Kazuhiro Nagata, Koichi Kato.
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Journal Title
PLoS One
Volume: 7
Issue: 9
Pages: e45930-e45930
DOI
Related Report
Peer Reviewed
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[Journal Article] A non-canonical UBA-UBL interaction forms the linear-ubiquitin-chain assembly complex.2012
Author(s)
H.Yagi, K.Ishimoto, T.Hiromoto, H.Fujita, T.Mizushima, Y.Uekusa, M.Yagi-Utsumi, E.Kurimoto, M.Noda, S.Uchiyama, F.Tokunaga, K. Iwai, and K.Kato
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Journal Title
EMBO Rep.
Volume: 13
Issue: 5
Pages: 462-468
DOI
Related Report
Peer Reviewed
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