Department of Pharmaceutical Chemistry and Bioanalytics, Institute of Pharmacy, Martin Luther University Halle-Wittenberg, Halle (Saale), D-06120, Germany.
Department of Chemistry, Institute of Organic Chemistry, University of Cologne, Cologne, D-50939, Germany.
Mass Spectrom Rev. 2019 Mar;38(2):187-201. doi: 10.1002/mas.21568. Epub 2018 Apr 16.
Free radical-initiated peptide sequencing (FRIPS) has recently been introduced as an analytical strategy to create peptide radical ions in a predictable and effective way by collisional activation of specifically modified peptides ions. FRIPS is based on the unimolecular dissociation of open-shell ions and yields fragments that resemble those obtained by electron capture dissociation (ECD) or electron transfer dissociation (ETD). In this review article, we describe the fundamentals of FRIPS and highlight its fruitful combination with chemical cross-linking/mass spectrometry (MS) as a highly promising option to derive complementary structural information of peptides and proteins. FRIPS does not only yield exhaustive sequence information of cross-linked peptides, but also defines the exact cross-linking sites of the connected peptides. The development of more advanced FRIPS cross-linkers that extend the FRIPS-based cross-linking/MS approach to the study of large protein assemblies and protein interaction networks can be eagerly anticipated.
自由基引发的肽测序（FRIPS）最近被引入作为一种分析策略，通过对特定修饰的肽离子进行碰撞激活，以可预测和有效的方式产生肽自由基离子。FRIPS 基于开壳离子的单分子离解，产生的片段类似于通过电子捕获解离（ECD）或电子转移解离（ETD）获得的片段。在这篇综述文章中，我们描述了 FRIPS 的基本原理，并强调了它与化学交联/质谱（MS）的成功结合，作为获得肽和蛋白质结构信息的极具前景的选择。FRIPS 不仅提供交联肽的详尽序列信息，还定义了连接肽的确切交联位点。可以热切期待开发更先进的 FRIPS 交联剂，将基于 FRIPS 的交联/MS 方法扩展到大的蛋白质组装体和蛋白质相互作用网络的研究中。
