Journal of the American Society for Mass Spectrometry

, Volume 21, Issue 4, pp 511–521

Fragmentation of α-radical cations of arginine-containing peptides


    • Chemical and Materials Sciences DivisionPacific Northwest National Laboratory
  • Zhibo Yang
    • Chemical and Materials Sciences DivisionPacific Northwest National Laboratory
  • C. M. Dominic Ng
    • Department of ChemistryUniversity of Hong Kong
  • Ivan K. Chu
    • Department of ChemistryUniversity of Hong Kong

DOI: 10.1016/j.jasms.2009.12.021

Cite this article as:
Laskin, J., Yang, Z., Ng, C.M.D. et al. J Am Soc Mass Spectrom (2010) 21: 511. doi:10.1016/j.jasms.2009.12.021


Fragmentation pathways of peptide radical cations, M, with well-defined initial location of the radical site were explored using collision-induced dissociation (CID) experiments. Peptide radical cations were produced by gas-phase fragmentation of CoIII(salen)-peptide complexes [salen=N,N′-ethylenebis (salicylideneiminato)]. Subsequent hydrogen abstraction from the β-carbon of the side-chain followed by Cα-Cβ bond cleavage results in the loss of a neutral side chain and formation of an α-radical cation with the radical site localized on the α-carbon of the backbone. Similar CID spectra dominated by radical-driven dissociation products were obtained for a number of arginine-containing α-radicals, suggesting that for these systems radical migration precedes fragmentation. In contrast, proton-driven fragmentation dominates CID spectra of α-radicals produced via the loss of the arginine side chain. Radical-driven fragmentation of large M peptide radical cations is dominated by side-chain losses, formation of even-electron a-ions and odd-electron x-ions resulting from Cα-C bond cleavages, formation of odd-electron z-ions, and loss of the N-terminal residue. In contrast, charge-driven fragmentation produces even-electron y-ions and odd-electron b-ions.

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© American Society for Mass Spectrometry 2010