Confinement effects on the conformation, dynamics and phase transitions of biomolecular systems

限域效应对生物分子系统的构象、动力学和相变

• 批准号: 203755245
• 负责人: Professor Dr. Roland Winter
• 金额: --
• 依托单位: Lehrstuhl für Physikalische Chemie I
• 依托单位国家: 德国
• 项目类别: Research Units
• 财政年份: 2011
• 资助国家: 德国
• 起止时间: 2010-12-31 至 2018-12-31
• 项目状态: 已结题
• 来源: https://gepris.dfg.de/gepris/projekt/203755245?language=en
• 关键词: Confinement; effects; conformation; dynamics; phase

The aim of our project is to explore the effects of geometry, hydroaffinity and softness of confinement conditions on the structure, dynamics and phase behavior of biomolecular and supramolecular systems. We plan to study the effect of geometrical restrictions on the conformation, dynamics and "inverse phase transition" of the model peptide elastin, as well as the selfassociation and aggregation of amyloidogenic peptides, focusing on the initial nucleation and growth process of amyloid fibrils. In addition to concluding measurements on the islet amyloid polypeptide (IAPP), we are planning to study confinement effects on the self-assembly and fibril formation of polylysine stereoisomers. Moreover, we aim at investigating the intermolecular interactions and dynamics of dense protein solutions as well as their phase behavior in the region of the solid-liquid and liquid-liquid phase separation region in well-defined nanoporous structures, including variations of the confinement conditions (i.e., the size, form, heterogeneity of the confinement, and the chemical nature of the walls). Finally, the effects of soft and hard matter confinement on the structure (topology) and phase behavior of lipid mesophases will be studied.

本项目的目的是探索限制条件的几何构型、亲水性和柔软性对生物分子和超分子体系的结构、动力学和相行为的影响。我们计划研究几何限制对模型多肽弹性蛋白的构象、动力学和逆相变的影响，以及淀粉样多肽的自结合和聚集，重点研究淀粉样蛋白纤维的初始成核和生长过程。除了总结胰岛淀粉样多肽(IAPP)的测量结果外，我们还计划研究限制对多赖氨酸立体异构体自组装和纤维形成的影响。此外，我们的目标是研究致密蛋白质溶液的分子间相互作用和动力学，以及它们在定义良好的纳米孔道结构中固-液和液-液相分离区域的相行为，包括限制条件的变化(即限制条件的大小、形式、非均质性和壁的化学性质)。最后，研究了软、硬物质限制对脂类中间相结构(拓扑)和相行为的影响。