| Project/Area Number |
08555029
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| Research Category |
Grant-in-Aid for Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Section | 展開研究 |
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| Research Field |
Materials/Mechanics of materials
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| Research Institution | Osaka Institute of Technology |
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Principal Investigator |
NAKAMACHI Eiji Osaka Institute of Technology, Faculty of Engineering, Professor, 工学部, 教授 (60099893)
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| Co-Investigator(Kenkyū-buntansha) |
TANAKA Masao Osaka University, Faculty of Senior Engineering, Professor, 基礎工学部, 教授 (40163571)
HIRANO Yoshiaki Osaka Institute of Technology, Faculty of Engineering, Associate Professor, 工学部, 助教授 (80247874)
HASHIMOTO Shigehiro Osaka Institute of Technology, Faculty of Engineering, Associate Professor, 工学部, 助教授 (00146515)
NAKAYASU Hidetoshi Konan University, Faculty of Science, Professor, 理学部, 教授 (80142553)
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| Project Period (FY) |
1996 – 1998
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| Project Status |
Completed (Fiscal Year 1998)
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| Budget Amount *help |
¥6,400,000 (Direct Cost: ¥6,400,000)
Fiscal Year 1998: ¥500,000 (Direct Cost: ¥500,000)
Fiscal Year 1997: ¥500,000 (Direct Cost: ¥500,000)
Fiscal Year 1996: ¥5,400,000 (Direct Cost: ¥5,400,000)
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| Keywords | biomimeticsmaterial / biomaterial / remodeling / self-recovering function / bio-tissue / molecular mechanics analysis / molecular dynamics analysis / muscle and bone tissues / 筋・骨細胞 / バイオミメティックス / 筋細胞 / 骨細胞 |
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| Research Abstract |
In this research, the evaluation system by analyzing molecular mechanical adaptation function of the bioimmetics material has been developed. The main results of this research is the development of analytical tool to evaluate the mechanical function of muscle and bone tissue, by employing the molecular mechanics(MM) and molecular dynainics(MD) simulations. We investigate the conformations -3-D atom coordinates - at the minimum potential energy of the acto-rnyosin hyper-molecular system and the collagen-hydroxyapatite(HAP) complex molecule. From the comparison between the actomyosin(normal model) and off-peptidebonding of actomyosin both with ATP , the role of ATP was confirmed for the structure stability and activation to motivate the relative sliding motion, which generate the muscle contraction in case of the normal model. The values of isothermal compressibility obtained by the molecular structure analysis shows good agreement with the experimental one.
MM and MD analyses of the collagen-HAP complex molecule, by employing the cross-linking and off-bonding of collagen fibrils, shows that the cross-link of the collagen fiber cause the higher mode fluctuation at the molecular level and might activate the formation of the bone tissue in the remodeling cycle.
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