Probing the electron capture dissociation mass spectrometry of phosphopeptides with traveling wave ion mobility spectrometry and molecular dynamics simulations

Doyong Kim, Pei-jing Pai, Andrew J. Creese, Andrew W. Jones, David H. Russell, Helen J. Cooper

Research output: Contribution to journalArticlepeer-review

9 Citations (Scopus)
168 Downloads (Pure)

Abstract

Electron capture dissociation mass spectrometry offers several advantages for the analysis of peptides, most notably that backbone c and z fragments typically retain labile modifications such as phosphorylation. We have shown previously that, in some cases, the presence of phosphorylation has a deleterious effect on peptide sequence coverage, and hypothesized that intramolecular interactions involving the phosphate group were preventing separation of backbone fragments. In the present work, we seek to rationalize the observed ECD behavior through a combination of ECD of model peptides, traveling wave ion mobility mass spectrometry and molecular dynamics simulations. The results suggest that for doubly protonated ions of phosphopeptide APLpSFRGSLPKSYVK a salt-bridge structure is favored, whereas for the doubly-protonated ions of APLSFRGSLPKpSYVK ionic hydrogen bonds predominate.
Original languageEnglish
Pages (from-to)1004-1013
JournalJournal of the American Society for Mass Spectrometry
Volume26
Issue number6
Early online date2 Apr 2015
DOIs
Publication statusPublished - 1 Jun 2015

Keywords

  • ECD
  • TWIMS
  • MDS
  • Phosphopeptides

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