| Project/Area Number |
16350121
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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 | 一般 |
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| Research Field |
Polymer/Textile materials
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| Research Institution | National University Corporation Tokyo University of Agriculture and Technology |
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Principal Investigator |
ASAKURA Tetsuo Tokyo University of Agriculture and Technology Graduate School, Institute of Symbiotic Science and Technology, Professor, 大学院・共生科学技術研究部, 教授 (30139208)
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| Co-Investigator(Kenkyū-buntansha) |
NISHIYAMA Norihiro Nihon University, School of dentistry at Matsudo, Professor, 松戸歯学部, 教授 (90112953)
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| Project Period (FY) |
2004 – 2005
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| Project Status |
Completed (Fiscal Year 2005)
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| Budget Amount *help |
¥16,100,000 (Direct Cost: ¥16,100,000)
Fiscal Year 2005: ¥2,900,000 (Direct Cost: ¥2,900,000)
Fiscal Year 2004: ¥13,200,000 (Direct Cost: ¥13,200,000)
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| Keywords | Silk-like Protein / Solid state NMR Analysis / Biomaterials / Ca Binding Site / Lamella Structure / Peptide Solid Phase Synthesis / CalbindinD9K / Shell Nacreous Matrix Protein |
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| Research Abstract |
The purpose of this project is to develop new silk-like materials for regeneration of bone on the basis of the lamella structure of the crystalline domain of silk fibroins and selective Ca^<2+> binding to the turn region.
The generation of the lamella structure was proved for ^<13>C selectively -labeled (Ala-Gly)_<15> peptide which can be considered as the model of the crystalline domain using solid state NMR method. The stem part consisted of the repeated eight amino acid sequences. Several model peptides with silk sequences, (Ala)_<12>, (Ala-Gly)_6, (Ala-Gly-Gly)_4,(Ala-Gly-Gly-Gly)_3 and Ca^<2+> binding sites from Calbindin D_<9k> or Shell Nacreous Matrix Protein MSI60 were synthesized to study the character of new silk-like materials containing Ca^<2+> binding sites using solid state NMR.
In addition, the silk-like proteins containing Ca binding site from MSI60 with longer sequences were also prepared with genetic engineering method. The yield of the proteins prepared by the cultivation of E.coli was relatively high ; about 50 mg/l.
Ca binding to the surface of the proteins was performed by soaking the film of the protein in Ca-containing aqueous solvents alternatively. These silk-like proteins with hydroxyl apatite could be produced after these Ca binding experiments. These materials can be used for new silk-like materials for regeneration of bone.
These results have been published in the international Journals, Protein Science and Biomacromolecules.
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