Model Studies on the Function of Acidic Proteins in Biomineralization

酸性蛋白在生物矿化中的功能模型研究

• 批准号: 5456662
• 负责人: Professor Dr. Norbert Sewald
• 金额: --
• 依托单位: Arbeitskreis Organische Chemie III
• 依托单位国家: 德国
• 项目类别: Priority Programmes
• 财政年份: 2005
• 资助国家: 德国
• 起止时间: 2004-12-31 至 2007-12-31
• 项目状态: 已结题
• 来源: https://gepris.dfg.de/gepris/projekt/5456662?language=en
• 关键词: Model; Studies; Function; Acidic; Proteins

The biological processes which lead to a wide variety of biomineral structures are largely unsolved. According to the widely accepted template-matrix-hypothesis , the organic matrix of calcified tissues (e.g. bones, mollusc shells) does contain specific macromolecules, which promote or inhibit the site-selective nucleation of crystals, and which direct the spatial orientation(s) of the overgrowing crystal layer. Owing to the very limited information which is currently available about the 3D structures of the natural matrix macromolecules, we are developing synthetic macromolecules (e.g. amphiphilic calixarene carboxylic acids and highly acidic peptides), which are specifically designed such as to mimic crucial aspects of the putative function of the biological systems. Essential structural properties of natural surface-active acidic proteins (i.e. binding epitopes comprising arrays of carboxylic acid residues fixed to amphiphilic b-pleated sheets, helices or loops) are imitated by artificial peptides. Elucidating the influence of the artificial proteins on the growth of inorganic crystal phases (calcite, aragonite, vaterite) within the appropriate model system is a main focus of our research, for which we employ monolayers and immobilized thin films in a perfusion device.

导致各种各样的生物矿物结构的生物过程在很大程度上是未解决的。根据广泛接受的模板基质假说，钙化组织（例如骨骼、软体动物壳）的有机基质确实含有特定的大分子，其促进或抑制晶体的位点选择性成核，并且指导过度生长的晶体层的空间取向。由于目前关于天然基质大分子的3D结构的信息非常有限，我们正在开发合成大分子（例如两亲性杯芳烃羧酸和高酸性肽），其被专门设计以模拟生物系统的推定功能的关键方面。天然表面活性酸性蛋白质的基本结构特性（即包含固定到两亲性b-折叠片、螺旋或环的羧酸残基阵列的结合表位）被人工肽模仿。阐明的影响，人工蛋白质的生长的无机晶体相（方解石，文石，球文石）在适当的模型系统是我们的研究的一个主要焦点，为此，我们采用单层和固定化薄膜在灌注装置。