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Chembiochem. 2019 Oct 8. doi: 10.1002/cbic.201900611. [Epub ahead of print]

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

Author information

1
Department of Chemistry, Ludwig-Maximilians-Universität München, Butenandtstrasse 5-13, 81377, Munich, Germany.
2
Department of Molecular Biology and the, Lewis-Sigler Institute for Integrative Genomics, Princeton University, Washington Road, Princeton, NJ, 08544, USA.

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.

KEYWORDS:

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

PMID:
31593346
DOI:
10.1002/cbic.201900611

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