Buijs Jos, Franklin Gary C
Biacore AB, Rapsgatan 7, 754 50 Uppsala, Sweden.
Brief Funct Genomic Proteomic. 2005 May;4(1):39-47. doi: 10.1093/bfgp/4.1.39.
The mapping of protein networks and the establishment of the functional relationships between expressed proteins and their effects on cellular processes represents a great challenge for functional or interaction proteomics. The combination of surface plasmon resonance (SPR)-based technology with mass spectrometry (MS) has created a unique analytical tool for functional proteomics investigations. Proteins are affinity purified, quantified and characterised in terms of their interactions, while the mass spectrometer identifies and structurally characterises the biomolecules. Recent developments have led to a closer integration of these key technologies, providing a combined approach which enables identification of proteins selected on the basis of their functional binding criteria. In addition to a historical overview of this field, some recent detailed examples of combined SPR-MS approaches will be reviewed in a number of key application areas, including ligand fishing, peptide sequence and post-translational modification analysis by SPR-MS/MS and enzyme inhibitor screening.
蛋白质网络的绘制以及已表达蛋白质之间功能关系的建立，及其对细胞过程的影响，是功能蛋白质组学或相互作用蛋白质组学面临的巨大挑战。基于表面等离子体共振（SPR）的技术与质谱（MS）相结合，为功能蛋白质组学研究创造了一种独特的分析工具。蛋白质通过亲和纯化进行定量，并根据其相互作用进行表征，而质谱仪则对生物分子进行鉴定和结构表征。最近的发展使得这些关键技术实现了更紧密的整合，提供了一种组合方法，能够鉴定基于功能结合标准选择的蛋白质。除了对该领域的历史概述之外，还将在一些关键应用领域回顾一些最近结合SPR-MS方法的详细实例，包括配体钓取、通过SPR-MS/MS进行肽序列和翻译后修饰分析以及酶抑制剂筛选。
