| Project/Area Number |
17500320
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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 Institute of Technology |
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Principal Investigator |
HIRANO Yoshiaki Osaka Institute of Technology, Faculty of Engineering, Associate Professor, 工学部, 助教授 (80247874)
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| Co-Investigator(Kenkyū-buntansha) |
SHIMOMURA Osamu Osaka Institute of Technology, Faculty of Engineering, Associate Professor, 工学部, 助教授 (10351454)
OKA Masahito Osaka Prefecture University, Faculty of Liberal Arts and Science, Professor, 総合教育研究機構, 教授 (70203966)
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| Project Period (FY) |
2005 – 2006
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| Project Status |
Completed (Fiscal Year 2006)
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| Budget Amount *help |
¥3,400,000 (Direct Cost: ¥3,400,000)
Fiscal Year 2006: ¥1,500,000 (Direct Cost: ¥1,500,000)
Fiscal Year 2005: ¥1,900,000 (Direct Cost: ¥1,900,000)
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| Keywords | Tissue Engineering / Scaffold / Peptide / Cell-attachment peptide / RGDS peptide / Self-assembly / Conformational Analysis / β-シート構造 / ペプチドファイバー / コンホメーション解析 |
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| Research Abstract |
In tissue engineering and wound-healing application, scaffold materials are utilized to provide a mechanical support for cell growth and tissue formation. These scaffold can be modified such that they also provide specific biologic signals to cell in order to control or facilitate tissue formation or regeneration. Cell adhesion peptides Arg-Gly-Asp (RGD) have been incorporated into scaffolds to enhance cell adhesion or to allow biospecific cell adhesion.
In this work, for improving the cell-attachment activity of the Arg-Gly-Asp-Ser peptides to tissue engineering scaffold, we tried to stabilize the folded conformations of such peptides by designing the ss-strands peptides, which have the Arg-Gly-Asp-Ser sequence at the C-terminal. These sequence, (Ala-Glu-Ala-Glu-Ala-Lys-Ala-Lys)_2 (EAK16) or (Arg-Ala-Arg-Ala-Asp-Ala-Asp-Ala)_2 (RAD16) of the peptides is selected as a typical sequence for having high propensity to form ss-strands.
RGDS containing ss-strands model peptides were synthesize
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d using liquid and solid phase procedures. Fibroblast cells attaching to the peptide-immobilized cell culture dishes, indicating that difference in the cell-attachment activity were found for these peptides-immobilized cell culture dishes. EAK16RGDS and RAD16RGDS immobilized polystyrene-dish has the highest spreading activity among the peptide-immobilized ones.
The conformational constraint caused by the formation of ss-strands structure is too strong to stabilize the desired conformation at the Arg-Gly-Asp-Ser portion for the peptides in which the Arg-Gly-Asp-Ser sequence is directly linked to the sequences designed for forming ss-strands structure. It is also suggested that designing a spacer sequence is desirable for improving the activity between the Arg-Gly-Asp-Ser sequence and the sequence forming ss-strand structure. Solutions of EAK16RGDS and RAD16RGDS become gelatinous and then form fibers. EAK16RGDS and RAD16RGDS peptides interact with each other and become more structured upon fiber formation. Such peptides may find utility as in vivo tissue engineering 3D scaffolds. Less
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