Study on crystallization and polymorphism of amyloidgenic proteins on biomembranes
| Project/Area Number |
20760539
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| Research Category |
Grant-in-Aid for Young Scientists (B)
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| Allocation Type | Single-year Grants |
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| Research Field |
Biofunction/Bioprocess
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| Research Institution | Osaka University |
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Principal Investigator |
SHIMANOUCHI Toshinori Osaka University, 大学院・基礎工学研究科, 助教 (10335383)
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| Research Collaborator |
GOTO Yuji 大阪大学, 蛋白質研究所, 教授 (40153770)
NODA Minoru 京都工芸繊維大学, 工芸学部, 教授 (20294168)
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| Project Period (FY) |
2008 – 2009
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| Project Status |
Completed (Fiscal Year 2009)
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| Budget Amount *help |
¥4,290,000 (Direct Cost: ¥3,300,000、Indirect Cost: ¥990,000)
Fiscal Year 2009: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2008: ¥2,730,000 (Direct Cost: ¥2,100,000、Indirect Cost: ¥630,000)
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| Keywords | メンブレン・ストレスバイオテクノロジー / 生体膜 / アミロイド / 多形 / スフェルライト / 品質管理 / 核形成 / 線維伸長 |
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| Research Abstract |
Amyloid firbril formation is similar to a crystallization. The amyloid fibrils fragmented in advance has been reported to play a role for a seeds. The seeds showed the variety of their growth behavior in the presence of the model biomembranes (liposomes). The addition of oxidative stress could lead to the formation of radiated amyloid fibrils (spherulite) and as well as the oxidized liposome could. It is, therefore, suggested that the liposome membranes determined the polymorphism of the amyloid.
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Report
(3 results)
Research Products
(72 results)
