Oligomerization of amyloid beta-peptides studies by computer simulations
| Project/Area Number |
24740296
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| Research Category |
Grant-in-Aid for Young Scientists (B)
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| Allocation Type | Multi-year Fund |
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| Research Field |
Biophysics/Chemical physics
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| Research Institution | Institute for Molecular Science |
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Principal Investigator |
ITOH Satoru 分子科学研究所, 理論・計算分子科学研究領域, 助教 (90595381)
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| Project Period (FY) |
2012-04-01 – 2015-03-31
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| Project Status |
Completed (Fiscal Year 2014)
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| Budget Amount *help |
¥2,340,000 (Direct Cost: ¥1,800,000、Indirect Cost: ¥540,000)
Fiscal Year 2014: ¥520,000 (Direct Cost: ¥400,000、Indirect Cost: ¥120,000)
Fiscal Year 2013: ¥520,000 (Direct Cost: ¥400,000、Indirect Cost: ¥120,000)
Fiscal Year 2012: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
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| Keywords | アミロイド線維形成 / 分子シミュレーション / アミロイド形成 / 国際情報交換 |
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| Outline of Final Research Achievements |
I had developed new simulation methods, the replica-permutation method and the Hamiltonian replica-permutation method. By using these methods, efficient conformational sampling for biomolecules can be realized in comparison with existing simulation methods. I had studied the oligomerization process of amyloid-beta peptides by these new methods. As a result, it was shown that beta-hairpin structures were increased when the amyloid-beta peptides came close. When the amyloid-beta peptides got close sufficiently, intermolecular beta-sheet structures as seen in amyloid fibrils were readily created in the presence of intramolecular beta-sheet structures.
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Report
(4 results)
Research Products
(32 results)
