Department of Biochemistry, University of Wisconsin-Madison, Madison, Wisconsin.
Curr Protoc. 2023 Jun;3(6):e798. doi: 10.1002/cpz1.798.
Protein and peptide N termini are important targets for selective modification with chemoproteomics reagents and bioconjugation tools. The N-terminal ⍺-amine occurs only once in each polypeptide chain, making it an attractive target for protein bioconjugation. In cells, new N termini can be generated by proteolytic cleavage and captured by N-terminal modification reagents that enable proteome-wide identification of protease substrates through tandem mass spectrometry (LC-MS/MS). An understanding of the N-terminal sequence specificity of the modification reagents is critical for each of these applications. Proteome-derived peptide libraries in combination with LC-MS/MS are powerful tools for profiling the sequence specificity of N-terminal modification reagents. These libraries are highly diverse, and LC-MS/MS enables analysis of the modification efficiencies of tens of thousands of sequences in a single experiment. Proteome-derived peptide libraries are a powerful tool for profiling the sequence specificities of enzymatic and chemical peptide labeling reagents. Subtiligase, an enzymatic modification reagent, and 2-pyridinecarboxaldehyde (2PCA), a chemical modification reagent, are two reagents that have been developed for selective N-terminal peptide modification and can be studied using proteome-derived peptide libraries. This protocol outlines the steps for generating N-terminally diverse proteome-derived peptide libraries and for applying these libraries to profile the specificity of N-terminal modification reagents. Although we detail the steps for profiling the specificity of 2PCA and subtiligase in Escherichia coli and human cells, these protocols can easily be adapted to alternative proteome sources and other N-terminal peptide labeling reagents. © 2023 The Authors. Current Protocols published by Wiley Periodicals LLC. Basic Protocol 1: Generation of N-terminally diverse proteome-derived peptide libraries from E. coli Alternate Protocol: Generation of N-terminally diverse proteome-derived peptide libraries from human cells Basic Protocol 2: Characterizing the specificity of 2-pyridinecarboxaldehyde using proteome-derived peptide libraries Basic Protocol 3: Characterizing the specificity of subtiligase using proteome-derived peptide libraries.
蛋白质和肽的 N 端是用化学蛋白质组学试剂和生物偶联工具进行选择性修饰的重要靶标。每个多肽链中的 N 端 ⍺- 胺仅出现一次,使其成为蛋白质生物偶联的有吸引力的靶标。在细胞中,新的 N 端可以通过蛋白水解切割产生,并被 N 端修饰试剂捕获,这些试剂可以通过串联质谱(LC-MS/MS)对蛋白酶底物进行蛋白质组范围的鉴定。了解修饰试剂的 N 端序列特异性对于这些应用都至关重要。蛋白质组衍生的肽文库与 LC-MS/MS 结合是分析 N 端修饰试剂序列特异性的强大工具。这些文库高度多样化,LC-MS/MS 能够在单个实验中分析成千上万种序列的修饰效率。蛋白质组衍生的肽文库是分析酶和化学肽标记试剂序列特异性的有力工具。Subtiligase 是一种酶修饰试剂,2-吡啶甲醛(2PCA)是一种化学修饰试剂,这两种试剂已被开发用于选择性 N 端肽修饰,并可以使用蛋白质组衍生的肽文库进行研究。本方案概述了生成 N 端多样化蛋白质组衍生肽文库的步骤,并应用这些文库来分析 N 端修饰试剂的特异性。虽然我们详细介绍了在大肠杆菌和人细胞中分析 2PCA 和 Subtiligase 特异性的步骤,但这些方案可以轻松适应替代蛋白质组来源和其他 N 端肽标记试剂。 © 2023 作者。 Wiley Periodicals LLC 出版的《当代生物技术》。 基本方案 1:从大肠杆菌中生成 N 端多样化的蛋白质组衍生肽文库 可选方案 1:从人细胞中生成 N 端多样化的蛋白质组衍生肽文库 基本方案 2:使用蛋白质组衍生肽文库分析 2-吡啶甲醛的特异性 基本方案 3:使用蛋白质组衍生肽文库分析 Subtiligase 的特异性