A Click-Chemistry-Based Enrichable Crosslinker for Structural and Protein Interaction Analysis by Mass Spectrometry

Michael Stadlmeier, Leander Simon Runtsch, Filipp Streshnev, Martin Wühr, Thomas Carell

Research output: Contribution to journalArticle

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 MS2 and potentially for MS3 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.

Original languageEnglish (US)
Pages (from-to)103-107
Number of pages5
JournalChemBioChem
Volume21
Issue number1-2
DOIs
StatePublished - Jan 15 2020

All Science Journal Classification (ASJC) codes

  • Molecular Medicine
  • Molecular Biology
  • Biochemistry
  • Organic Chemistry

Keywords

  • click chemistry
  • crosslinking mass spectrometry
  • interactome analysis
  • proteomics
  • structure elucidation

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