A Click‐Chemistry‐Based Enrichable Crosslinker for Structural and Protein Interaction Analysis by Mass Spectrometry. (28th November 2019)

• Record Type: Journal Article
• Authors: Stadlmeier, Michael; Runtsch, Leander Simon; Streshnev, Filipp; Wühr, Martin; Carell, Thomas
• Is Part Of: Chembiochem. Volume 21:Number 1/2(2020)
• Page Start: 103
• Page End: 107
• Publication Date: 2019-11-28
• Subjects: click chemistry -- crosslinking mass spectrometry -- interactome analysis -- proteomics -- structure elucidation; Biochemistry -- Periodicals; Molecular biology -- Periodicals; Pharmaceutical chemistry -- Periodicals; 572
• DOI: 10.1002/cbic.201900611
• Languages: English
• ISSNs: 1439-4227

Abstract

Abstract: Mass spectrometry is the method of choice for the characterisation of proteomes. Most proteins operate in protein complexes, in which their close association modulates their function. However, with standard MS analysis, information on protein–protein interactions is lost and no structural information is retained. To gain structural and interactome data, new crosslinking reagents are needed that freeze inter‐ and intramolecular interactions. Herein, the development of a new reagent, which has several features that enable highly sensitive crosslinking MS, is reported. The reagent enables enrichment of crosslinked peptides from the majority of background peptides to facilitate efficient detection of low‐abundant crosslinked peptides. Due to the special cleavable properties, the reagent can be used for MS 2 and potentially for MS 3 experiments. Thus, the new crosslinking reagent, in combination with high‐end MS, should enable sensitive analysis of interactomes, which will help researchers to obtain important insights into cellular states in health and diseases. Abstract : Freezing interactions for identification : A new crosslinking reagent, with a sulfoxide fragmentation group and a click site, is reported for crosslink enrichment. Due to special cleavable properties, the reagent can be used for MS 2 and potentially for MS 3 experiments.