Abstract
The gas-phase fragmentation reactions of singly protonated aromatic amino acids, their simple peptides as well as simple models for intermolecular disulfide bonds have been examined using a commercially available hybrid linear ion trap–Fourier transform ion cyclotron resonance (FT-ICR) mass spectrometer. Low-energy collision-induced dissociation (CID) reactions within the linear ion trap are compared with electron-induced dissociation (EID) reactions within the FT-ICR cell. Dramatic differences are observed between low-energy CID (which occurs via vibrational excitation) and EID. For example, the aromatic amino acids mainly fragment via competitive losses of NH3 and (H2O+CO) under CID conditions, while side-chain benzyl cations are major fragment ions under EID conditions. EID also appears to be superior in cleaving the S–S and S–C bonds of models of peptides containing an intermolecular disulfide bond. Systematic studies involving fragmentation as a function of electron energy reveal that the fragmentation efficiency for EID occurs at high electron energy (more than 10 eV) compared with the low-electron energy (less than 0.2 eV) typically observed for electron capture dissociation fragmentation. Finally, owing to similarities between the types of fragment ions observed under EID conditions and those previously reported in ultraviolet photodissociation experiments and the electron-ionization mass spectra, we propose that EID results in fragmentation via electronic excitation and vibrational excitation. EID may find applications in analyzing singly charged molecular ions formed by matrix-assisted laser desorption ionization.
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Notes
The reason why these two isomeric dipeptides exhibit different behavior with regard to NH3 loss is likely to arise from the ability of the indole side chains to participate in a neighboring-group reaction. In Trp-Gly, the indole group is directly adjacent to the protonated N terminus and is thus able to participate in a neighboring-group reaction similar to protonated tryptophan (Scheme 1). In contrast, the indole side chain of Gly-Trp is further away from the protonated N terminus and isomerization of the amide bond is required for the peptide to adopt a suitable geometry for NH3 loss via a neighboring-group reaction. Other lower-energy fragmentation pathways are observed instead.
NH3 loss is absent in the CID fragmentation of protonated histidine owing to the presence of other favorable processes [38].
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Acknowledgements
R.A.J.O. thanks the Australian Research Council for support of this work under the ARC Centres of Excellence program (ARC Centre of Excellence in Free Radical Chemistry and Biotechnology), the ARC-Lief program and VICS for helping fund the purchase of the LTQ FT FT-ICR instrument. H.L. acknowledges the award of an Elizabeth and Vernon Puzey Postgraduate Scholarship.
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Part 56 of the series “Gas phase ion chemistry of biomolecules”.
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Lioe, H., O’Hair, R.A.J. Comparison of collision-induced dissociation and electron-induced dissociation of singly protonated aromatic amino acids, cystine and related simple peptides using a hybrid linear ion trap–FT-ICR mass spectrometer. Anal Bioanal Chem 389, 1429–1437 (2007). https://doi.org/10.1007/s00216-007-1535-1
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DOI: https://doi.org/10.1007/s00216-007-1535-1