A Click‐Chemistry‐Based Enrichable Crosslinker for Structural and Protein Interaction Analysis by Mass Spectrometry
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.
- Authors:
-
[1];
[2];
[3];
[2]
- Department of Chemistry Ludwig-Maximilians-Universität München Butenandtstrasse 5–13 81377 Munich Germany, Department of Molecular Biology and the Lewis-Sigler Institute for Integrative Genomics Princeton University Washington Road Princeton NJ 08544 USA
- Department of Chemistry Ludwig-Maximilians-Universität München Butenandtstrasse 5–13 81377 Munich Germany
- Department of Molecular Biology and the Lewis-Sigler Institute for Integrative Genomics Princeton University Washington Road Princeton NJ 08544 USA
- Publication Date:
- Research Org.:
- Univ. of Illinois at Urbana-Champaign, IL (United States)
- Sponsoring Org.:
- USDOE Office of Science (SC)
- OSTI Identifier:
- 1592509
- Alternate Identifier(s):
- OSTI ID: 1592510; OSTI ID: 1623501
- Grant/Contract Number:
- SC0018260
- Resource Type:
- Published Article
- Journal Name:
- ChemBioChem: a European journal of chemical biology
- Additional Journal Information:
- Journal Name: ChemBioChem: a European journal of chemical biology Journal Volume: 21 Journal Issue: 1-2; Journal ID: ISSN 1439-4227
- Publisher:
- Wiley Blackwell (John Wiley & Sons)
- Country of Publication:
- France
- Language:
- English
- Subject:
- Biochemistry & Molecular Biology; Pharmacology & Pharmacy
Citation Formats
Stadlmeier, Michael, Runtsch, Leander Simon, Streshnev, Filipp, Wühr, Martin, and Carell, Thomas. A Click‐Chemistry‐Based Enrichable Crosslinker for Structural and Protein Interaction Analysis by Mass Spectrometry. France: N. p., 2019.
Web. doi:10.1002/cbic.201900611.
Stadlmeier, Michael, Runtsch, Leander Simon, Streshnev, Filipp, Wühr, Martin, & Carell, Thomas. A Click‐Chemistry‐Based Enrichable Crosslinker for Structural and Protein Interaction Analysis by Mass Spectrometry. France. https://doi.org/10.1002/cbic.201900611
Stadlmeier, Michael, Runtsch, Leander Simon, Streshnev, Filipp, Wühr, Martin, and Carell, Thomas. Thu .
"A Click‐Chemistry‐Based Enrichable Crosslinker for Structural and Protein Interaction Analysis by Mass Spectrometry". France. https://doi.org/10.1002/cbic.201900611.
@article{osti_1592509,
title = {A Click‐Chemistry‐Based Enrichable Crosslinker for Structural and Protein Interaction Analysis by Mass Spectrometry},
author = {Stadlmeier, Michael and Runtsch, Leander Simon and Streshnev, Filipp and Wühr, Martin and Carell, Thomas},
abstractNote = {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.},
doi = {10.1002/cbic.201900611},
journal = {ChemBioChem: a European journal of chemical biology},
number = 1-2,
volume = 21,
place = {France},
year = {Thu Nov 28 00:00:00 EST 2019},
month = {Thu Nov 28 00:00:00 EST 2019}
}
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https://doi.org/10.1002/cbic.201900611
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