| Project/Area Number |
14580837
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Biomedical engineering/Biological material science
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| Research Institution | Osaka Prefecture University |
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Principal Investigator |
OKA Masahito Osaka Prefecture University, Research Institute for Advanced Science and Technology, Associate Professor, 先端科学研究所, 助教授 (70203966)
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| Co-Investigator(Kenkyū-buntansha) |
HIRANO Yoshiaki Osaka Institute of Technology, Department of Applied Chemistry, Associate Professor, 工学部, 助教授 (80247874)
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| Project Period (FY) |
2002 – 2003
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| Project Status |
Completed (Fiscal Year 2003)
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| Budget Amount *help |
¥3,400,000 (Direct Cost: ¥3,400,000)
Fiscal Year 2003: ¥1,500,000 (Direct Cost: ¥1,500,000)
Fiscal Year 2002: ¥1,900,000 (Direct Cost: ¥1,900,000)
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| Keywords | cell-attachment activity / peptide / polypeptide / conformation / fibronectin / tissue engineering / biomaterial / hybrids / フィブロネクチン / アメロゲニン |
|---|
| Research Abstract |
Peptides related to the cell-attachment and spreading activity were synthesized, and their molecular conformations and cell-attachment and spreading activity were analyzed. For Arg-Gly-Asp-Ser mimetic peptides, we found new designed sequences having higher cell-attachment activity than the native sequence, then they were hybridized on the surface of polymer materials such as poly(vinyl alcohol). For laminin related peptides, designed peptides exhibited the cell-attachment and spreading activity. Periodic polypeptides having repetitive amino-acid sequences, which are found in many native periodic proteins such as collagen, were synthesized and their conformations in solutions were analyzed by the CD measurement. It was shown that they take new secondary structures different from well-known α-helix, β-strand and polyproline-II structures.
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