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Affiliation |
Faculty of Science Department of Chemistry and Biological Science |
ITOH Satoru G.
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Research Areas 【 display / non-display 】
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Natural Science / Biophysics, chemical physics and soft matter physics
From Graduate School 【 display / non-display 】
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The Graduate University for Advanced Studies Graduate School, Division of Physics Doctor's Course Completed
- 2005.03
External Career 【 display / non-display 】
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分子科学研究所 助教
2010.06 - 2026.03
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National Institutes of Health 研究員
2008.03 - 2010.05
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Nagoya University Researcher
2005.04 - 2008.03
Professional Memberships 【 display / non-display 】
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分子シミュレーション学会
2016
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日本蛋白質科学会
2011
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日本生物物理学会
2004
Papers 【 display / non-display 】
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Computational analysis and molecular dynamics simulation of metformin derivatives as potential α-glucosidase inhibitors for type 2 diabetes Reviewed
Nor Akmalyati Sulong, Hisashi Okumura, Satoru G. Itoh, Chin Fei Chee, Mohd Rafie Johan, Vannajan Sanghiran Lee
RESULTS IN CHEMISTRY 18 2025.11
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Oligomerization Mechanism of Amyloid β Peptides at Hydrophobic Interfaces Revealed by Molecular Dynamics Simulations Reviewed
Taiga Saito, Tatsuya Ishiyama, Masafumi Sakono, Satoru G. Itoh, Hisashi Okumura
JOURNAL OF PHYSICAL CHEMISTRY B 129 6794 2025.07
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Why do histone monomethylation and dimethylation cause a significant difference in binding to LEDGF? Reviewed
Hinako X. Suzuki, Hisashi Okumura, Satoru G. Itoh
JOURNAL OF CHEMICAL PHYSICS 162 2025.05
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Molecular dynamics simulations of amyloid-β(29-42) aggregation in bulk water and at the air-water interface Reviewed
Anne-Idil Farah, Satoru G. Itoh, Hisashi Okumura
BIOPHYSICS AND PHYSICOBIOLOGY 20 2025
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Nonequilibrium Molecular Dynamics Method to Generate Poiseuille-Like Flow between Lipid Bilayers Reviewed
Masaki Otawa, Satoru G. Itoh, Hisashi Okumura
JOURNAL OF CHEMICAL THEORY AND COMPUTATION 20 10199 2024.11
Awards 【 display / non-display 】
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2023年度日本シミュレーション学会 ベストオーサー賞
2023
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The 3rd International Symposium “Dynamical ordering of biomolecular systems for creation of integrated functions,” Poster Presentation Award
2015
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平成二十五年度日本生物物理学会中部支部講演会 優秀発表賞
2014
Scientific Research Funds Acquisition Results 【 display / non-display 】
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Aggregation process of amyloid-beta peptides on a membrane on a lipid membrane studied by computer simulation
Grant number：21K06040 2021.04 - 2024.03
Japan Society for the Promotion of Science Grants-in-Aid for Scientific Research Grant-in-Aid for Scientific Research (C)
Grant amount：\2730000 （ Direct Cost: \2100000 、 Indirect Cost：\630000 ）
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Oligomer formation of amyloid-beta studied by new constant pH simulations
Grant number：16K18531 2016.04 - 2019.03
Japan Society for the Promotion of Science Grants-in-Aid for Scientific Research Grant-in-Aid for Young Scientists (B) Grant-in-Aid for Young Scientists (B)
Itoh Satoru
Grant amount：\2990000 （ Direct Cost: \2300000 、 Indirect Cost：\690000 ）
The oligomer formation process of Abeta(29-42), which is a fragment of the amyloid beta (Abeta) peptide, was studied by Coulomb replica-permutation molecular dynamics simulations. It was found that an oligomer increased in size by addition of a monomer to the oligomer sequentially.
We also performed Coulomb replica-permutation molecular dynamics simulations to clarify the dimer formation process of the full-length Abeta peptides. As a result, it was found that the intramolecular beta-sheet structure accelerated the formation of an intermolecular beta-sheet structure. -
Oligomerization of amyloid beta-peptides studies by computer simulations
Grant number：24740296 2012.04 - 2015.03
Japan Society for the Promotion of Science Grants-in-Aid for Scientific Research Grant-in-Aid for Young Scientists (B) Grant-in-Aid for Young Scientists (B)
ITOH Satoru
Grant amount：\2340000 （ Direct Cost: \1800000 、 Indirect Cost：\540000 ）
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.
Teaching Experience 【 display / non-display 】
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Basic statistical mechanics
2025.02
Level：Postgraduate
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情報科学
2024.04 - 2026.03 Institution：Chukyo University
Level：Undergraduate (liberal arts)
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情報と技術
2023.09 - 2026.03 Institution：Chukyo University
Level：Postgraduate
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生体分子シミュレーション
2023.04 - 2026.03 Institution：The Graduate University for Advanced Studies
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構造化学特論III
2020.01 Institution：Kyushu University
Level：Postgraduate