Oligomerization of amyloid beta-peptides studies by computer simulations

2014 Fiscal Year Final Research Report

• Project/Area Number: 24740296
• Research Category: Grant-in-Aid for Young Scientists (B)
• Allocation Type: Multi-year Fund
• Research Field: Biophysics/Chemical physics
• Research Institution: Institute for Molecular Science
• 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)
• Project Period (FY): 2012-04-01 – 2015-03-31
• Keywords: アミロイド線維形成 / 分子シミュレーション

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.

Free Research Field

生物物理