Journal
ANALYST
Volume 138, Issue 22, Pages 6759-6765Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/c3an01333b
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Funding
- NSF [CHE-1308114]
- Direct For Mathematical & Physical Scien
- Division Of Chemistry [1308114] Funding Source: National Science Foundation
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Direct characterization of peptides with multiple disulfide bonds by mass spectrometry is highly desirable. In this study, electron transfer dissociation (ETD) of peptide disulfide regio-isomers was studied using model peptides containing two intrachain disulfide bonds. ETD provided rich sequence information (c/z ions) even for the backbone region under the coverage of two disulfide bonds. This behavior presented an analytical advantage over low energy collision-induced dissociation (CID) of protonated intact peptide ions, which produced very limited sequence (b/y) ions. Mechanistic studies suggested that the formation of c/z ions under the two disulfide bond covered region resulted from an initial N-C-alpha bond cleavage, followed by radical cascades to cleave multiple disulfide bonds. The ETD spectra of the disulfide regio-isomers produced similar product ions due to radical cascades; while the relative intensities of the product ions varied, to a certain degree, which could be helpful in distinguishing isomers with overlapping disulfide bonds.
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