Molecular mechanism of the self-propagation of amyloid fibrils explored by structural analysis of prefibrillar intermediates
| Project/Area Number |
23770188
|
|---|
| Research Category |
Grant-in-Aid for Young Scientists (B)
|
| Allocation Type | Multi-year Fund |
|---|
| Research Field |
Biophysics
|
|---|
| Research Institution | Kobe University |
|---|
Principal Investigator |
CHATANI Eri 神戸大学, 大学院・理学研究科, 准教授 (00432493)
|
|---|
| Project Period (FY) |
2011 – 2012
|
| Project Status |
Completed (Fiscal Year 2012)
|
| Budget Amount *help |
¥4,550,000 (Direct Cost: ¥3,500,000、Indirect Cost: ¥1,050,000)
Fiscal Year 2012: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2011: ¥3,250,000 (Direct Cost: ¥2,500,000、Indirect Cost: ¥750,000)
|
|---|
| Keywords | タンパク質 / フォールディング / ミスフォールディング / アミロイド線維 / 線維前駆中間体 / NMR / インスリン / アミロイド / 伝播 / 中間体 |
|---|
| Research Abstract |
Protein misfolding occasionally leads to the formation of supramolecular assemblies known as amyloid fibrils, the deposition of which is associated with numerous diseases. One of the most unique and essential properties of amyloid fibrils is their template-dependent growth, which underlies the propagation of pathology of amyloidoses. In this study, we trapped a prefibrillar intermediate of insulin formed transiently in the early stage of fibrillation reaction and from detailed structural properties analyzed by using AFM, FTIR, and proteolytic digestion, several regions have proved to be essential for the amyloid propagation
|
Report
(3 results)
Research Products
(42 results)
