| Project/Area Number |
14540537
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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 |
機能・物性・材料
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| Research Institution | KYUSHU KYORITSU UNINERSITY (2004)
Kyushu University (2002-2003) |
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Principal Investigator |
KAIBARA Kozue KYUSHU KYORITSU UNINERSITY, FUCULTY OF ENGINEERING, PROFESSOR, 工学部, 助教授 (90080564)
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| Co-Investigator(Kenkyū-buntansha) |
INOUE Hiroyoshi KURUME UNIV., SCH.OF MEDICINE, ASSOCIATE PROFESSOR, 医学部, 助教授 (10213175)
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| Project Period (FY) |
2002 – 2004
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| Project Status |
Completed (Fiscal Year 2004)
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| Budget Amount *help |
¥3,700,000 (Direct Cost: ¥3,700,000)
Fiscal Year 2004: ¥700,000 (Direct Cost: ¥700,000)
Fiscal Year 2003: ¥700,000 (Direct Cost: ¥700,000)
Fiscal Year 2002: ¥2,300,000 (Direct Cost: ¥2,300,000)
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| Keywords | Elastomeric Protein / Coacervation / Self-Assembly / Arteriosclerosis / Extracellular Matrix / Biofuctionality Materials / Primeval Cell Model / Critical Process / 選択性イオン結合部位 |
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| Research Abstract |
(1)Temperature-Dependent Coacervation of Elastomeric Protein-Water System : Characteristic Critical Process Biological self-assembly process of tropoelastin, precursor of elastomeric protein, can be mimicked by the temperature-dependent coacervation of an elastomeric protein-water system. Critical characteristics of the self-assembly of elastomeric protein during the liquid-liquid phase separation were investigated by the image analysis of microscopic observation and laser light scattering measurements.
(2)Metal Cation Effects on the Temperature-Dependent Coacervation : Selective Binding Sites and Self-Assembly Process In metal chloride solution, the temperature-dependent coacervation of elastomeric protein was characterized as a critical self-assembly manner with a fast time progress and abroad size distribution of microcoacervate droplets. Two types of metal cation binding sites on polypeptide chains, carboxy oxygen of side amino acid residues and peptide carbonyl oxygen of backbone c
… More
hains, affect the self-assembly and conformational regulation of elastomeric protein.
(2)Transition Metal Effects on the Critical Process : Spherical and Elongated Coacervate Formation The stability of microcoacervate droplets of elastomeric protein at high temperature are improved by the addition of transition metals. Microcoacervate droplets are specifically and significantly stabilized by Cu^<2+> and La^<3+> ions, and the separation of macrocoacervate layer is totally suppressed by these ions. In some cases, elongated coacervates are observed with major sperical coacervate droplets by phase contrast microscopy.
(3)Elastomeric Protein Characteristics as a Primitive Protein : Primeval Cell Model and Cellular Functionality Materials The elastomeric protein has the primitive nature of protein, such as the early phylogenic appearance in the formation of circulatory system and the simple amino acid compositions shared more than 80% with nonpolar alanine, glycine, valine, and proline residues. There is a report describing a link between the prebiotic cellular organization and the prebiological molecular evolution of an elastin-like macromolecular system.
(5)Self-Assembly and Function of Elastomeric Protein : Biofunctionality Materials Development An elastomeric protein called elastin is fully responsible for sophisticated biological elasticity in mammalian tissues such as the arterial wall, ligament, lung, and skin. A key step to elastogenesis is a biological self-assembly process of tropoelastin in extracellular space to establish some regular configulatlons before enzymatic cross-linking reaction. The mechanism and function of elastomeric proteins and their structural foundations can be examined by investigating the characteristics of molecular self-assembly established during the temperature-dependent coacervation of an elastomeric protein-water system. Less
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