Self-Assembly of Bioelastic Matrix: Structure and Function under Shear Stress

弹性蛋白-水体系的温度依赖性凝聚（1）疏水和静电相互作用：引发弹性蛋白-水体系凝聚的驱动力弹性蛋白-水体系本身的主要温度依赖性强调了诱导分子自组装的基本驱动力是疏水相互作用。还观察到基于极性氨基酸残基的静电相互作用，如pH和添加金属对凝聚过程的影响。可以预期的是，在充满含有混合金属氯化物的水性介质的细胞外空间中，疏水和静电相互作用在弹性蛋白的生物合成中起着不可或缺的作用。(2)弹性蛋白-水体系在剪切应力下的凝聚：重组胞外条件下的自组装弹性蛋白-水体系的温度依赖性凝聚的研究目标之一 ...更多信息 水系统是为了检查和可视化生物自组装过程，因此需要在相当于细胞外环境的条件下检查影响凝聚过程的其他因素。剪切诱导机制似乎在控制这种微观缝隙中的分子组装和相行为中起着重要作用。采用旋转粘度计和流变仪观察了剪切应力对凝聚过程的影响。新型弹性生物功能材料的制备（1）弹性蛋白质的球形和细长凝聚体：与细胞外空间生物自组装过程的关系显微镜下偶尔观察到长形凝聚液滴，其为长度为5-10 μm的颗粒，直径为普通球形液滴，1-3 μm。球形液滴的融合实际上在显微镜下无法观察到，因此伸长的凝聚层液滴似乎来自除球形组装体之外的初级聚集体。由于弹性蛋白以丝状排列或纤维状排列具有多种生物活性，因此对形成伸出凝聚层的条件进行研究似乎很重要。(2)特异性和选择性金属阳离子结合对弹性蛋白结构和功能特性的影响多肽链上的两种类型的金属阳离子结合位点，侧链氨基酸残基的羧基氧和主链的肽羰基氧，影响分子自组装和构象调节，以及由此产生的弹性蛋白的多种生物功能。

Temperature-Dependent Coacervation of the Elastomeric Protein-Water System(1) Hydrophobic and Electrostatic Interactions: Driving Force to Initiate Coacervation of the Elastomeric Protein-Water systemThe 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 ConditionsOne 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 SpaceElongated 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 ProteinThe 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