| Project/Area Number |
17K18365
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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 |
Bio-related chemistry
Biophysics
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| Research Institution | Institute of Physical and Chemical Research |
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Principal Investigator |
Niitsu Ai 国立研究開発法人理化学研究所, 開拓研究本部, 基礎科学特別研究員 (10791064)
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| Project Period (FY) |
2017-04-01 – 2021-03-31
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| Project Status |
Completed (Fiscal Year 2020)
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| Budget Amount *help |
¥4,290,000 (Direct Cost: ¥3,300,000、Indirect Cost: ¥990,000)
Fiscal Year 2018: ¥2,730,000 (Direct Cost: ¥2,100,000、Indirect Cost: ¥630,000)
Fiscal Year 2017: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
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| Keywords | 膜ペプチド / 分子動力学 / 膜タンパク質設計 / タンパク質設計 / 膜貫通ペプチド / 合成生物学 / タンパク質フォールディング / タンパク質デザイン |
|---|
| Outline of Final Research Achievements |
This study focuses on the association mechanism of transmembrane α-helices, the most fundamental phenomenon in membrane protein folding. The assembling process of rationally designed α-helix peptides in lipid bilayers was analysed by using structural modelling and molecular dynamics simulations. Based on the simulation results, peptides with redesigned amino acid sequences were synthesised, and their experimental conditions for structural and functional analyses were optimised. The obtained results provide new insights into the interaction of the highly stable designed peptide assemblies with lipid bilayers.
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| Academic Significance and Societal Importance of the Research Achievements |
本研究で得られた人工設計αヘリックスペプチド会合体と脂質二重膜の相互作用に関する新たな知見は、タンパク質の折り畳みを理解することに加えて未だ黎明期にある人工膜タンパク質の実現に寄与する。また新たに設計したペプチドは新規生体分子材料として利用可能であり、工学的応用を通して研究成果を社会に還元できると期待される。
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