Dissociation Pattern of Sodiated Amide Peptides as a Tool for De Novo Sequencing
peer-reviewed · Journal of the American Society for Mass Spectrometry · 2020
| Date | 2020-11-04 |
| Type | peer-reviewed |
| Venue | Journal of the American Society for Mass Spectrometry |
| Publisher | American Chemical Society (ACS) |
| Contribution | adjacent |
| DOI | 10.1021/jasms.0c00269 |
| Citations (OpenAlex) | 9 |
| Venue 2-year citedness | 2.84 |
Abstract
As part of the de novo sequencing issue, new approaches have to be found to sequence small natural peptides (+ , followed by collision-induced dissociations (CID) or the postsource metastable decay (PSD) of such cationized molecular ions was found to improve the sequence coverage of native peptides through the formation of [b n -1 + Na + OH] + ions issued from C-terminal residue exclusion. Concerned by the identification of peptides with a C-terminal amide, the fragmentation pattern of their sodiated molecular ions was investigated. In contrast to the peptides featuring unmodified C-termini, the C-terminal loss did not occur, with the amide function triggering different fragmentation pathways. However, several residues, such as aspartic acid (D), glutamic acid (E), and arginine (R), influenced the dissociation of fixed-charge sodiated ions similarly to protonated peptides; more surprisingly, serine (S), threonine (T), and tyrosine (Y), which exhibit a hydroxyl function on their side chains, showed a very peculiar behavior that could help de novo peptide sequencing.
Methods and tools
- Sodiated amide peptide dissociation: Studies how sodiated C-terminally amidated peptides fragment under CID and PSD, as a basis for de novo sequencing of small natural peptides.