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Unusual fragmentation of β-Linked peptides by ExD tandem mass spectrometry
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Sargaeva, Nadezda P., Lin, Cheng and O’Connor, Peter B. (2011) Unusual fragmentation of β-Linked peptides by ExD tandem mass spectrometry. Journal of The American Society for Mass Spectrometry, Vol.22 (No.3). pp. 480-491. doi:10.1007/s13361-010-0049-9
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Official URL: http://dx.doi.org/10.1007/S13361-010-0049-9
Abstract
Ion-electron reaction based fragmentation methods (ExD) in tandem mass spectrometry (MS), such as electron capture dissociation (ECD) and electron transfer dissociation (ETD) represent a powerful tool for biological analysis. ExD methods have been used to differentiate the presence of the isoaspartate (isoAsp) from the aspartate (Asp) in peptides and proteins. IsoAsp is a β3-type amino acid that has an additional methylene group in the backbone, forming a Cα–Cβ bond within the polypeptide chain. Cleavage of this bond provides specific fragments that allow differentiation of the isomers. The presence of a Cα–Cβ bond within the backbone is unique to β-amino acids, suggesting a similar application of ExD toward the analysis of peptides containing other β-type amino acids. In the current study, ECD and ETD analysis of several β-amino acid containing peptides was performed. It was found that N–Cβ and Cα–Cβ bond cleavages were rare, providing few c and z type fragments, which was attributed to the instability of the Cβ radical. Instead, the electron capture resulted primarily in the formation of a and y fragments, representing an alternative fragmentation pathway, likely initiated by the electron capture at a backbone amide nitrogen protonation site within the β amino acid residues.
| Item Type: | Journal Article | ||||
|---|---|---|---|---|---|
| Subjects: | Q Science > QD Chemistry | ||||
| Divisions: | Faculty of Science > Chemistry | ||||
| Library of Congress Subject Headings (LCSH): | Fragmentation reactions, Ions, Molecules, Tandem mass spectrometry, Peptides | ||||
| Journal or Publication Title: | Journal of The American Society for Mass Spectrometry | ||||
| Publisher: | Springer New York LLC | ||||
| ISSN: | 1044-0305 | ||||
| Official Date: | March 2011 | ||||
| Dates: |
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| Volume: | Vol.22 | ||||
| Number: | No.3 | ||||
| Number of Pages: | 12 | ||||
| Page Range: | pp. 480-491 | ||||
| DOI: | 10.1007/s13361-010-0049-9 | ||||
| Status: | Peer Reviewed | ||||
| Publication Status: | Published | ||||
| Access rights to Published version: | Restricted or Subscription Access | ||||
| Funder: | National Heart, Lung, and Blood Institute (NHLBI), National Institute of General Medical Sciences (U.S.) (NIGMS), National Center for Research Resources (U.S.) (NCRR), National Institutes of Health (U.S.) (NIH), Engineering and Physical Sciences Research Council (EPSRC) | ||||
| Grant number: | EP/F034210/1 (EPSRC), EP/F034210/1 (EPSRC), P41 RR10888 (NIH/NCRR), N01HV28178 (NIH/NHLBI), R01GM078293 (NIH/NIGMS), S10 RR025082 (NIH/NIGMS) |
Data sourced from Thomson Reuters' Web of Knowledge
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