Radical-driven processes within a peptidic sequence of type I collagen upon single-photon ionisation in the gas phase

Lucas Schwob, Mathieu Lalande, Dmitrii Egorov, Jimmy Rangama, Ronnie Hoekstra, Violaine Vizcaino, Thomas Schlathölter, Jean-Christophe Poully*

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review

7 Citations (Scopus)
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Abstract

We report on an experimental single-photon absorption study on gas-phase protonated collagen peptides employing a combination of mass spectrometry and synchrotron radiation. Partial ion yields for the main photoabsorption products vary steadily with photon energy over the range from 14 to 545 eV. At low energy, non-dissociative photoionisation competes with neutral molecule loss from the precursor ion, whereas fragmentation of the peptide backbone dominates at soft X-ray energies. Neutral molecule losses from the ionised peptide are found to have low energy barriers and most likely involve amino-acid residue side-chains with radical character, in particular aspartic acid. A particularly interesting finding is photoinduced loss of proline hydroxylation. The loss of this typical collagen post-translational modification might play a destabilizing role in the collagen structure.

Original languageEnglish
Pages (from-to)22895-22904
Number of pages10
JournalPPCP : Physical Chemistry Chemical Physics
Volume19
Issue number34
DOIs
Publication statusPublished - 14-Sep-2017

Keywords

  • LASER-INDUCED IONIZATION/DISSOCIATION
  • COLLISION-INDUCED DISSOCIATION
  • ABSORPTION MASS-SPECTROMETRY
  • DENSITY-FUNCTIONAL THEORY
  • PROTONATED PEPTIDES
  • ENERGY-RANGE
  • AMINO-ACIDS
  • TRIPLE-HELIX
  • SIDE-CHAIN
  • WATER-LOSS

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