| Project/Area Number |
22570164
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Biophysics
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| Research Institution | Kinki University |
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Principal Investigator |
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| Co-Investigator(Kenkyū-buntansha) |
KATO Minoru 立命館大学, 薬学部, 教授 (00241258)
FUJISAWA Masao 近畿大学, 生物理工学部, 准教授 (20258065)
KONO Ryohei 和歌山県立医科大学, 医学部, 助教 (70569110)
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| Project Period (FY) |
2010 – 2012
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| Project Status |
Completed (Fiscal Year 2012)
|
| Budget Amount *help |
¥4,420,000 (Direct Cost: ¥3,400,000、Indirect Cost: ¥1,020,000)
Fiscal Year 2012: ¥910,000 (Direct Cost: ¥700,000、Indirect Cost: ¥210,000)
Fiscal Year 2011: ¥1,170,000 (Direct Cost: ¥900,000、Indirect Cost: ¥270,000)
Fiscal Year 2010: ¥2,340,000 (Direct Cost: ¥1,800,000、Indirect Cost: ¥540,000)
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| Keywords | フォールディング / リゾチーム / アミロイド / 線維形成 / ジスルフィド結合 / 疎水コア / シーディング / クロスシーディング |
|---|
| Research Abstract |
Lysozyme is one of the amyloidogenic proteins. Here, by using hen lysozyme disulfide-deficient variants and synthetic peptides covering specific residue positions, we investigated the mechanism of the core formation of lysozyme amyloid fibrils. Peptide regions involved in the core formation in normal monomolecular folding are also involved in misfolding and core formation of lysozyme amyloid fibrils. Specifically, absence of a structure which could interact and successfully accept a highly beta-aggregating structure in normal folding reaction leads to misfolding and fibrillogenesis through intermolecular beta-aggregation.
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