Journal
JOURNAL OF THE AMERICAN SOCIETY FOR MASS SPECTROMETRY
Volume 16, Issue 7, Pages 1020-1030Publisher
SPRINGER
DOI: 10.1016/j.jasms.2005.02.010
Keywords
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Funding
- NIGMS NIH HHS [R37 GM045372, R01 GM045372, GM 45372] Funding Source: Medline
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Multiply-charged peptide cations comprised of two polypeptide chains (designated A and B) bound via a disulfide linkage have been reacted with SO2- in an electrodynamic ion trap mass spectrometer. These reactions proceed through both proton transfer (without dissociation) and electron transfer (with and without dissociation). Electron transfer reactions are shown to give rise to cleavage along the peptide backbone, loss of neutral molecules, and cleavage of the cystine bond. Disulfide bond cleavage is the preferred dissociation channel and both Chain A (or B)-S and Chain A (or B)-SH fragment ions are observed, similar to those observed with electron capture dissociation (ECD) of disulfide-bound peptides. Electron transfer without dissociation produces [M + 2H](+) ions, which appear to be less kinetically stable than the proton transfer [M + H](+) product. When subjected to collision-induced dissociation (CID), the [M + 2H](+) ions fragment to give products that were also observed as dissociation products during the electron transfer reaction. However, not all dissociation channels noted in the electron transfer reaction were observed in the CID of the [M + 2H](+) ions. The charge state of the peptide has a significant effect on ' both the extent of electron transfer dissociation observed and the variety of dissociation products, with higher charge states giving more of each. (c) 2005 American Society for Mass Spectrometry.
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