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

(1)弹性体蛋白-水系统的温度依赖凝聚过程可以模拟弹性体蛋白前体对流层弹性蛋白的生物自组装过程。通过显微观察和激光散射测量，研究了弹性蛋白在液-液分离过程中自组装的关键特性。(2)金属阳离子对温度依赖性凝聚的影响：选择性结合位点和自组装过程。在金属氯化物溶液中，弹性体蛋白的温度依赖性凝聚表现为一种临界自组装方式，时间进展快，微凝聚液滴尺寸分布均匀。多肽链上的两种金属阳离子结合位点——侧氨基酸残基的羧基氧和主链上的肽羰基氧——影响着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：球形和长条形凝聚形成过渡金属的加入提高了弹性蛋白微凝聚液滴在高温下的稳定性。Cu^<2+>和La^<3+>离子对微凝聚液滴具有特异性和显著的稳定作用，并且这些离子完全抑制了大凝聚层的分离。在某些情况下，通过相衬显微镜观察到拉长的凝聚体与主要的精子凝聚体液滴。(3)弹性体蛋白作为原始蛋白质的特征：原始细胞模型和细胞功能材料弹性体蛋白具有蛋白质的原始性质，如在循环系统形成的早期系统发育中出现，简单的氨基酸组成与非极性丙氨酸、甘氨酸、缬氨酸和脯氨酸残基共享80%以上。有一篇报道描述了益生元细胞组织与生物前的弹性蛋白类大分子系统的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（如动脉壁、韧带、肺和皮肤）中复杂的生物弹性。弹性发生的关键步骤是在酶交联反应之前，对弹力蛋白在细胞外空间的生物自组装过程，以建立一些规则的构型。通过研究弹性蛋白-水系统在温度依赖的凝聚过程中建立的分子自组装特征，可以研究弹性蛋白的机制和功能及其结构基础。少

(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