2012 Fiscal Year Final Research Report
Analysis of amyloid fibril formation mechanism and cell toxicity of lysozyme
| Project/Area Number |
22580336
|
|---|
| Research Category |
Grant-in-Aid for Scientific Research (C)
|
| Allocation Type | Single-year Grants |
|---|
| Section | 一般 |
|---|
| Research Field |
Basic veterinary science/Basic zootechnical science
|
|---|
| Research Institution | Kagoshima University |
|---|
Principal Investigator |
|
|---|
| Co-Investigator(Kenkyū-buntansha) |
MATSUMOTO Mitsuharu 鹿児島大学, 共同獣医学部, 教授 (30157383)
KUSAKABE Takahiro 九州大学, 農学研究院, 教授 (30253595)
|
|---|
| Co-Investigator(Renkei-kenkyūsha) |
WATANABE Keiichi 佐賀大学, 農学部, 教授 (40191754)
|
|---|
| Project Period (FY) |
2010 – 2012
|
| Keywords | リゾチーム / アミロイド線維 / コアペプチド / トリプトファン62 / 細胞毒性 / ヒトリゾチーム変異体 / アミロイドーシス |
|---|
| Research Abstract |
It was confirmed that W62 of lysozyme is a crucial amino acid on amyloid fibrils formation by analysis of core peptide It is speculated that the fibrillation of lysozyme would occur by exposure to molecular surface of the region containing the W62, resulting in causing molecular association by mainly W62, and being formed the aligned structure. The cytotoxicity of lysozyme fibrils showed the cell death like necrosis. On the other hand, on the case of expression intracellular of the human mutant, cells cause impaired secretion, as a result, lysozyme cloud be accumulated as an insoluble fraction in cells.
|
