Self-assembly und structure formation of spider silk proteins in (ultra-)thin films

（超）薄膜中蜘蛛丝蛋白的自组装和结构形成

• 批准号: 410872515
• 负责人: Professor Dr. Andreas Fery
• 金额: --
• 依托单位: Leibniz-Institut für Polymerforschung Dresden (IPF)
• 依托单位国家: 德国
• 项目类别: Research Grants
• 财政年份: 2018
• 资助国家: 德国
• 起止时间: 2017-12-31 至 2021-12-31
• 项目状态: 已结题
• 来源: https://gepris.dfg.de/gepris/projekt/410872515?language=en
• 关键词: Self; assembly; und; structure; formation

The preparation of (ultra) thin spider silk films (d = 2 – 100 nm) in combination with the design of various (new) recombinant spider silk proteins offers the unique possibility to investigate the structure formation and self-assembly behavior of silk proteins in thin films at defined interfaces and allows to compare these processes to those in bulk solution. The coating of the substrates and preparation of the films is achieved by deposition from aqueous solution. By self-assembly as well as surface interaction phase separated structures with domains in the nanoscale are formed. This proposal aims at the elucidation of structure formation within spider silk proteins in dependence of their amino acid sequence (amino acid composition as well as sequence of defined amino acid modules). The general question of this proposal addresses the modalities of deposition and orientation of spider silk-related films as well as the influence of primary structure (i.e. sequence), of amino acid charge, and of the molecular weight of spider silk proteins in (ultra-)thin films, as well as the influence of surface chemistry and topography of the used support materials. The size of the gained structural nano-sized domains will be controlled via the sequence of the modules. The following aims are tackled in detail:• Time course (kinetics, dynamics) of the folding (secondary structure) and orientation of the structural elements in spider silk protein films at surfaces• Influence of charge (exchange of amino acid E by K, from C- to Kappa-module) and its relation to salinity and pH• Role of the typically major fraction of the random coil/alpha-helix rich hydrophilic amorphous phase concerning the formation of the minor fraction of beta-sheet rich hydrophobic crystalline phases within spider silk materials (embedding) • Role of the aqueous (buffer, pH, salinity) respectively organic solvent• Role of mechanical textures, orientation and surface properties of substrates concerning structure formation and orientation of the domainsThe characterization of the orientation of secondary structural elements by polarised FTIR spectroscopy and of the separation of spider silk peptide blocks by high resolution atomic force microscopy techniques allows to draw conclusions with respect to the mechanism of structure formation and to create a general assembly model of spider silk based thin films.

（超）薄蜘蛛丝膜（d = 2 - 100 nm）的制备与设计（新的）重组蜘蛛丝蛋白的设计相结合，提供了研究薄膜中丝蛋白在定义的界面中丝蛋白的结构形成和自组装行为的独特可能性，并允许将这些过程与Bulk溶液中的这些过程进行比较。底物的涂层和膜的制备是通过水溶液中的沉积来实现的。通过自组装以及表面相互作用相分离的结构与纳米级中的结构。该建议旨在阐明蜘蛛丝蛋白内的结构形成，以依赖其氨基酸序列（氨基酸组成以及定义的氨基酸模块）。该提案的一般问题涉及蜘蛛丝丝相关膜的沉积和取向的方式，以及原发性结构（即序列），氨基酸电荷的影响以及（超）薄膜中蜘蛛丝蛋白的分子量的影响，以及使用材料的表面化学和地形的影响。获得的结构纳米大小域的大小将通过模块的序列控制。 The following aims are tackled in detail:• Time course (kinetics, dynamics) of the folding (secondary structure) and orientation of the structural elements in spider silk protein films at surfaces• Influence of charge (exchange of amino acid E by K, from C- to Kappa-module) and its relation to salinity and pH• Role of the typically major fraction of the random coil/alpha-helix rich hydrophilic amorphous phase使蜘蛛丝材料内丰富疏水晶体相位的小比例的形成（嵌入）•分别（缓冲，pH，pH，盐度）的作用分别通过高分辨率原子力显微镜技术的蜘蛛丝肽块的块可以对结构形成机理得出结论，并创建了蜘蛛丝绸基薄膜的大会模型。