Issue 34, 2017

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

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.

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

Article information

Article type
Paper
Submitted
19 May 2017
Accepted
24 Jul 2017
First published
25 Jul 2017

Phys. Chem. Chem. Phys., 2017,19, 22895-22904

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

L. Schwob, M. Lalande, D. Egorov, J. Rangama, R. Hoekstra, V. Vizcaino, T. Schlathölter and J. Poully, Phys. Chem. Chem. Phys., 2017, 19, 22895 DOI: 10.1039/C7CP03376A

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