期刊
INTERNATIONAL JOURNAL OF MASS SPECTROMETRY
卷 367, 期 -, 页码 28-34出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.ijms.2014.04.015
关键词
CID; Phosphotransfer; Phosphoramidate; Histidine phosphorylation; Gas-phase dimer; Non-covalent interactions
资金
- Biotechnology and Biological Sciences Research Council (BBSRC) [BB/H007113/1, BB/F00561X/1]
- BBSRC DTP-funded studentship
- Biotechnology and Biological Sciences Research Council [BB/H007113/1, BB/F00561X/1] Funding Source: researchfish
- BBSRC [BB/F00561X/1, BB/H007113/1] Funding Source: UKRI
The hydrogen bonds and electrostatic interactions that form between the protonated side chain of a basic residue and the negatively charged phosphate of a phosphopeptide can play crucial roles in governing their dissociation pathways under low-energy collision-induced dissociation (CID). Understanding how phosphoramidate (i.e. phosphohistidine, phospholysine and phosphoarginine), rather than phosphomonoester-containing peptides behave during CID is paramount in investigation of these problematic species by tandem mass spectrometry. To this end, a synthetic peptide containing either phosphohistidine (pHis) or phospholyisine (pLys) was analyzed by ESI-MS using a Paul-type ion trap (AmaZon, Bruker) and by traveling wave ion mobility-mass spectrometry (Synapt G2-Si, Waters). Analysis of the products of low-energy CID demonstrated formation of a doubly `phosphorylated' product ion arising from intermolecular gas-phase phosphate transfer within a phosphopeptide dimer. The results are explained by the formation of a homodimeric phosphohistidine (pHis) peptide non-covalent complex (NCX), likely stabilized by the electrostatic interaction between the pHis phosphate group and the protonated C-terminal lysine residue of the peptide. To the best of our knowledge this is the first report of intermolecular gas-phase phosphate transfer from one phosphopeptide to another, leading to a doubly phosphorylated peptide product ion. (c) 2014 The Authors. Published by Elsevier B.V.
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