Synthesis and Evaluation of Peptide-based Hybrid Materials for Tissue Engineering
| Project/Area Number |
15500333
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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) |
OKA Masahito Osaka Prefecture University, Advance Science and Technology, Associate Professor, 先端科学研究所, 助教授 (70203966)
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| Project Period (FY) |
2003 – 2004
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| Project Status |
Completed (Fiscal Year 2004)
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| Budget Amount *help |
¥3,600,000 (Direct Cost: ¥3,600,000)
Fiscal Year 2004: ¥1,600,000 (Direct Cost: ¥1,600,000)
Fiscal Year 2003: ¥2,000,000 (Direct Cost: ¥2,000,000)
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| Keywords | Cell-attachment peptide / RGDS / Tissue Engineering / Scaffold / RGDS-natural polymer hybrid / Alginate / Conformational Analysis / Structure-activity relationship / Arg-Gly-Asp-Ser (RGDS) / RGDS ペプチド-高分子複合体 |
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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 have been incorporated into scaffolds to enhance cell adhesion or to allow biospecific cell adhesion.
It is shown that oligopeptides having the Arg-Gly-Asp (RGD) sequence, which is related to the cell-attachment activity of fibronectin, vitronectin, collagen, and fibrinogen, may act as the ligands for the cell-attachment receptors on the cell membranes. It is also shown that the cell-attachment activity site of fibronectin and its related peptides form compactly folded conformations.
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 suc
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h peptides by designing the ss-hairpin peptides, which have the Arg-Gly-Asp-Ser sequence at the turn portion. These sequence, Ala-Glu-Ala-Glu-Ala-Lys-Ala-Lys (EAK8), (Ala-Glu-Ala-Glu-Ala-Lys-Ala-Lys)_2 (EAK16) or (Arg-Ala-Arg-Ala-Asp-Ala-Asp-Ala)_2 (RAD 16) of the peptides is selected as a typical sequence for having high propensity to form ss-strands.
RGDS containing ss-sheet model peptides were synthesized using liquid and solid phase procedures. All peptides were characterized by NMR,MALDI-TOF MS, amino acid analysis, and elemental analysis. Cell-attachment activities of these peptides were examined by cell-attachment test using L929 fibroblast cell toward peptide-immobilized substrate.
L929 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. These results suggest that the RGDS sequence of designed peptides commonly interact with integrin receptor of the cell. EAK16RGDS and RAD 16RGDS immobilized polystyrene-dish has the highest spreading activity among the peptide-immobilized ones.
The conformational constraint caused by the formation of ss-hairpin 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-hairpin 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. It was possible to prepare the tissue engineering 3D scaffold with comparative ease. Less
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Report
(3 results)
Research Products
(28 results)
