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

生物弹性基质的自组装：剪切应力下的结构和功能

• 批准号: 11640584
• 负责人: KAIBARA Kozue
• 金额: $ 2.3万
• 依托单位: KYUSHU UNIVERSITY
• 依托单位国家: 日本
• 项目类别: Grant-in-Aid for Scientific Research (C)
• 财政年份: 1999
• 资助国家: 日本
• 起止时间: 1999 至 2001
• 项目状态: 已结题
• 来源: https://kaken.nii.ac.jp/grant/KAKENHI-PROJECT-11640584/
• 关键词: Elastomeri protein; Elastin; Extracellular matrix; Arteriosclerosis; Self-assembly; Coacervation; Biofunctionality materials; Rheoscope

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

弹性蛋白-水体系的温度依赖凝聚(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-水体系本身的主要依赖温度的性质强调诱导分子自组装的基本驱动力是疏水相互作用。还观察到了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，在充满混合金属氯化物的水介质中，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)剪切应力下弹性蛋白-水系统的凝聚：重组细胞外条件下的自组装弹性蛋白依赖于温度凝聚的研究目标之一-w…更大的系统是检查和可视化生物自组装过程，因此需要在等同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方面发挥了重要作用。通过旋转粘度计和流变学观察来研究剪切应力对凝聚过程的影响。新开发的弹性生物功能材料的创建(1)弹性蛋白的球形和细长的凝聚体：与细胞外空间的生物自组装过程的关系在显微镜下偶尔观察到长度为5-10μm的弹性凝聚体液滴，其直径为普通球形液滴的直径1-3μm。在显微镜下几乎看不到球形液滴的融合，因此细长的凝聚体液滴似乎来自一次聚集体而不是球形聚集体。研究形成弹性凝聚体的条件似乎很重要，因为弹性蛋白在丝状排列或纤维排列中具有多种生物活性。(2)特定的和选择性的金属阳离子结合对弹性蛋白的结构和功能特性的影响多肽链上的两种金属阳离子结合部位，侧基氨基酸残基的羧氧和主链上的肽羰基氧，影响分子的自组装和构象调节，以及由此产生的弹性蛋白的多种生物功能

项目成果

井上浩義: "Effects of Anion Exchange Resin as Phosphate Binder on Serum Phosphate and iPTH Levels in Normal Rats"International Journal of Artificial Organs. 23・4. 243-249 (2000)

Hiroyoshi Inoue：“阴离子交换树脂作为磷酸盐结合剂对正常大鼠血清磷酸盐和 iPTH 水平的影响”国际人工器官杂志 23・4（2000 年）。

K. Kaibara, K. Okamoto, and K. Miyakawa: "Characterization of Proteinic Coacervate Formation: From Primeval Cell Model to Biofunctionality Materials"In: Handbook of Polyelectrolytes and Their Applications, Editors: S. Tripathy, J. Kumar, and H.S. Nalwa ,

K. Kaibara、K. Okamoto 和 K. Miyakawa：“蛋白质凝聚层形成的表征：从原始细胞模型到生物功能材料”，载于：聚电解质及其应用手册，编辑：S. Tripathy、J. Kumar 和 H.S.

K.Kaibara, H.Inoue: "Self-Assembly and Coacervate Formation of Elastomeric Protein-Water System under Shear Stress"Biopolymers. (発表予定). (2002)

K.Kaibara、H.Inoue：“剪切应力下弹性蛋白-水系统的自组装和凝聚形成”生物聚合物（即将发表）。

K.Kaibara, T.Watanabe, K.Miyakawa, K.Okamoto: "Self-Assembly and Temperature-Dependent Coacervation of Elastin Model Polypeptide, (VPGVG)_n, and Biologically Derived α-Elastin -Phase Contrast Microscopy and Light Scattering Photometry-"Biomacromolecules.

K.Kaibara、T.Watanabe、K.Miyakawa、K.Okamoto：“弹性蛋白模型多肽 (VPGVG)_n 的自组装和温度依赖性凝聚，以及生物衍生的 α-弹性蛋白 - 相差显微镜和光散射光度测定 - “生物大分子。

甲斐原梢: "Characterizations of Critical Processes in Liquid-Liquid Phase Separation of Elastomeric Protein-Water System-Microscopic Observations and Light Scattering Measurements-"Biopolymers. 53・5. 369-379 (2000)

Kozue Kaihara：“弹性蛋白-水系统液-液相分离的关键过程的表征 - 显微镜观察和光散射测量 -”生物聚合物 53・5（2000）。