Mechanistic insights into intramolecular phosphate group transfer during collision induced dissociation of phosphopeptides
| Autor: | Nick C. Polfer, Laura S. Bailey, Amanda L. Patrick, Nicolas Galy, Mélanie Alves |
|---|---|
| Rok vydání: | 2019 |
| Předmět: |
Phosphopeptides
Binding Sites Collision-induced dissociation 010405 organic chemistry Stereochemistry Chemistry 010401 analytical chemistry 01 natural sciences Acceptor Mass Spectrometry Organophosphates Peptide Fragments Dissociation (chemistry) 0104 chemical sciences Serine Deprotonation Intramolecular force Phosphorylation Histidine Protons Spectroscopy Protein Binding |
| Zdroj: | Journal of Mass Spectrometry. 54:449-458 |
| ISSN: | 1096-9888 1076-5174 |
| DOI: | 10.1002/jms.4351 |
| Popis: | We report on the rearrangement chemistry of model phosphorylated peptides during collision-induced dissociation (CID), where intramolecular phosphate group transfers are observed from donor to acceptor residues. Such "scrambling" could result in inaccurate modification localization, potentially leading to misidentifications. Systematic studies presented herein provide mechanistic insights for the unusually high phosphate group rearrangements presented some time ago by Reid and coworkers (Proteomics 2013, 13 [6], 964-973). It is postulated here that a basic residue like histidine can play a key role in mediating the phosphate group transfer by deprotonating the serine acceptor site. The proposed mechanism is consistent with the observation that fast collisional activation by collision-cell CID and higher-energy collisional dissociation (HCD) can shut down rearrangement chemistry. Additionally, the rearrangement chemistry is highly dependent on the charge state of the peptide, mirroring previous studies that less rearrangement is observed under mobile proton conditions. |
| Databáze: | OpenAIRE |
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