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SELF-ASSEMBLY AND FUNCTION OF ARTERIAL WALL PROTEIN : MATERIALS DEVELOPMENT MIMICKING PRIMEVAL CELL AND BIOELASTIC TISSUE FUNCTIONS

动脉壁蛋白的自组装和功能：模拟原始细胞和生物弹性组织功能的材料开发

基本信息

批准号：
14540537
负责人：
KAIBARA Kozue
金额：
$ 2.37万
依托单位：
KYUSHU KYORITSU UNINERSITY (2004)Kyushu University (2002-2003)
依托单位国家：
日本
项目类别：
Grant-in-Aid for Scientific Research (C)
财政年份：
2002
资助国家：
日本
起止时间：
2002 至 2004
项目状态：
已结题

项目摘要

(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

（1）弹性蛋白质-水系统的温度依赖性凝聚：特征关键过程弹性蛋白质的前体原弹性蛋白的生物自组装过程可以通过弹性蛋白质-水系统的温度依赖性凝聚来模拟。采用显微图像分析和激光光散射技术研究了弹性蛋白质在液-液相分离过程中自组装的临界特性。（2）金属阳离子对变温凝聚的影响：选择性结合位点与自组装过程在金属氯化物溶液中，弹性蛋白的变温凝聚是一种临界的自组装方式，其时间进程快，微凝聚液滴的粒径分布广。多肽链上的两类金属阳离子结合位点，侧链氨基酸残基的羧基氧和主链C的肽羰基氧， ...更多信息链，影响弹性蛋白的自组装和构象调节。（2）过渡金属对关键过程的影响：球形和细长凝聚层的形成通过添加过渡金属，弹性蛋白质的微凝聚层液滴在高温下的稳定性得到改善。Cu^<2+>和La^<3+>离子对微凝聚层液滴的稳定性具有特异性和显著性，而这些离子完全抑制了大凝聚层的分离。在某些情况下，通过相差显微镜观察到细长的凝聚层，其中主要是球状凝聚层液滴。（3）作为原始蛋白质的弹性蛋白质的特性：原始细胞模型和细胞功能材料弹性蛋白质具有蛋白质的原始性质，例如在循环系统形成中的早期促分化外观，以及与非极性丙氨酸、甘氨酸、缬氨酸和脯氨酸残基共享80%以上的简单氨基酸组成。有一份报告描述了弹性蛋白样大分子系统的前生物细胞组织和前生物分子进化之间的联系。（5）弹性蛋白的自组装和功能：生物功能材料的开发一种称为弹性蛋白的弹性蛋白完全负责哺乳动物组织中复杂的生物弹性，如动脉壁，韧带，肺和皮肤。弹性蛋白原在细胞外空间的生物自组装过程是弹性蛋白发生的关键步骤，在酶促交联反应之前，弹性蛋白原在细胞外空间中建立一些规则的构象。弹性蛋白质及其结构基础的机制和功能，可以通过研究弹性蛋白质-水系统的温度依赖性凝聚过程中建立的分子自组装的特性来检查。少