Molecularly Imprinted Polymers for the selective trageting of phosphotyrosine-containing proteins and peptides

用于选择性支持含磷酸酪氨酸的蛋白质和肽的分子印迹聚合物

• 批准号: 27215077
• 负责人: Professorin Dr. Katrin Marcus-Alic
• 金额: --
• 依托单位: Abteilung Funktionelle Proteomik
• 依托单位国家: 德国
• 项目类别: Research Grants
• 财政年份: 2006
• 资助国家: 德国
• 起止时间: 2005-12-31 至 2014-12-31
• 项目状态: 已结题
• 来源: https://gepris.dfg.de/gepris/projekt/27215077?language=en
• 关键词: Molecularly; Imprinted; Polymers; selective; trageting

In this project, we aim at the realisation of new generations of hierachically imprinted materials based on structural control at both the 1 and 100 nm length scales. Control at the 1 nm length scale is achieved by using host monomers designed to bind to the side chain of given amino acids of modified amino acids, here phosphorylated ones. Control at the 10 nm length scale is achieved by using non-proteinaceous protein surrogates as templates, thus allowing the preparation of size complementary peptide of protein binding sites. We anticipate that combining these approaches will result in robust receptors capable of capturing peptide or protein targets of a certain size but with a defined substitution of substitution pattern. In the area of proteomics, such phases could play the role of class selective affinity phases for fractionation and enrichment of low abundant modified proteins. Phosphorylation is a modification of profound biological importance. Phosphorylated proteins are of critical importance in intercellular signal transduction processes and their analyses forms an important part of proteomics research. The application of MIPs prepared via the above substructure approaches may lead to a new concept in addressing labile biomolecules with MIPs and open the way to a wide range of tailored materials for affinity-based enrichment of proteins, thus representing a major advance in the field of targeted proteomics.

在这个项目中，我们的目标是在1和100 nm长度尺度上实现基于结构控制的新一代分级印迹材料。通过使用被设计为结合至修饰的氨基酸（此处为磷酸化的氨基酸）的给定氨基酸的侧链的宿主单体来实现在Inm长度尺度下的控制。通过使用非蛋白质性蛋白替代物作为模板实现10 nm长度尺度的控制，从而允许制备蛋白结合位点的大小互补肽。我们预计，结合这些方法将导致强大的受体能够捕获一定大小的肽或蛋白质靶标，但具有确定的取代模式。在蛋白质组学领域，这些相可以起到类选择性亲和相的作用，用于分离和富集低丰度修饰蛋白质。磷酸化是一种具有深远生物学意义的修饰。磷酸化蛋白质在细胞间信号转导过程中起着至关重要的作用，其分析是蛋白质组学研究的重要组成部分。通过上述子结构方法制备的MIPs的应用可能会导致一个新的概念，在处理不稳定的生物分子与MIPs和开放的方式，以广泛的定制材料的亲和力为基础的蛋白质富集，从而代表了靶向蛋白质组学领域的重大进展。