Mass Spectral Signatures of Complex Post-Translational Modifications in Proteins: A Proof-of-Principle Based on X-ray Irradiated Vancomycin

Marwa Abdelmouleh, Mathieu Lalande, Johnny El Feghaly, Violaine Vizcaino, Andre Rebelo, Samuel Eden, Thomas Schlatholter, Jean-Christophe Poully*

*Bijbehorende auteur voor dit werk

OnderzoeksoutputAcademicpeer review

3 Citaten (Scopus)
52 Downloads (Pure)


Characterizing post-translational modifications (PTM) of proteins is of key relevance for the understanding of many biological processes, as these covalent modifications strongly influence or even determine protein function. Among the different analytical techniques available, mass spectrometry is attracting growing attention because recent instrumental and computational improvements have led to a massive rise of the number of PTM sites that can be identified and quantified. However, multiple PTM occurring at adjacent amino acid residues can lead to complex and dense chemical patterns that are a challenge to characterize. By means of X-ray synchrotron radiation coupled to mass spectrometry, and through the test-case of the glycopeptide antibiotic vancomycin, we show that such a pattern has a unique and robust signature in terms of photon energy and molecular environment. This highlights the potential of this technique in proteomics and its value as a tool to understand the biological roles of PTM.

Originele taal-2English
Pagina's (van-tot)1738-1743
Aantal pagina's6
TijdschriftJournal of the American Society for Mass Spectrometry
Nummer van het tijdschrift8
StatusPublished - 5-aug.-2020

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