| Project/Area Number |
11640584
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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 UNIVERSITY |
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Principal Investigator |
KAIBARA Kozue Graduate School of Science, Kyushu University, Assist. Prof., 大学院・理学研究院, 助手 (90080564)
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| Co-Investigator(Kenkyū-buntansha) |
INOUE Hiroyoshi Kurume Univ. Sch. of Medicine, Lecturer, 医学部, 講師 (10213175)
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| Project Period (FY) |
1999 – 2001
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| Project Status |
Completed (Fiscal Year 2001)
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| Budget Amount *help |
¥3,600,000 (Direct Cost: ¥3,600,000)
Fiscal Year 2001: ¥600,000 (Direct Cost: ¥600,000)
Fiscal Year 2000: ¥700,000 (Direct Cost: ¥700,000)
Fiscal Year 1999: ¥2,300,000 (Direct Cost: ¥2,300,000)
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| Keywords | Elastomeri protein / Elastin / Extracellular matrix / Arteriosclerosis / Self-assembly / Coacervation / Biofunctionality materials / Rheoscope |
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| Research Abstract |
Temperature-Dependent Coacervation of the Elastomeric Protein-Water System
(1) Hydrophobic and Electrostatic Interactions: Driving Force to Initiate Coacervation of the Elastomeric Protein-Water system
The primary temperature-dependent nature of the elastomeric protein-water system itself emphasizes that the fundamental driving force to induce the molecular self-assembly is hydrophobic interactions. Electrostatic interactions based on the polar amino acid residues are also observed as the pH and adding metal effects on Coacervation process. It can be expected that both the hydrophobic and the electrostatic interactions play indispensable roles in the biosynthesis of elastin in an extracellular space filled with aqueous media containing mixed metal chlorides.
(2) Coacervation of the Elastomeric Protein-Water System under Shear Stress: Self-Assembly in Reconstituted Extracellular Conditions
One of the research objectives for the temperature-dependent Coacervation of the elastomeric protein-w
… More
ater system is to inspect and visualize the biological self-assembly process, so that it is required to examine additional factors affecting the Coacervation process under the conditions equivalent to extracellular environments. A shear-induced mechanism seems to play an important role in controlling molecular assembly and phase behavior in such a microscopic crevice. Rotary viscometry and rheoscopic observations were employed to examine the effects of shear stress on Coacervation process.
Creation of the Newly Developed Elastic Biofunctionality Materials
(1)Spherical and Elongated Coacervates of Elastomeric Protein: Relation to the Biological Self-Assembly Process in Extracellular Space
Elongated coacervate droplets are observed occasionally by microscopy as particles with length of 5-10 μm and diameter of ordinary spherical droplets, 1-3 μm. The fusion of spherical droplets cannot be observed practically under a microscope, so the elongated coacervate droplets seem to be derived from a primary aggregates other than the spherical assembly. Examination on the conditions to form elogated coacervates seems to important, since elastin functions with multiple biological activities in a filamentous array or a fibrous arrangements.
(2) Effects of Specific and Selective Metal Cation Binding on the Structural and Functional Characteristics of Elastomeric Protein
The two types of metal cation binding site on polypeptide chains, carboxy oxygen of side amino acid residues and peptide carbonyl oxygen of backbone chains, affect the molecular self-assembly and conformational regulation, as well as the resultant multiple biofunctionality of elastomeric proteins Less
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