Fragmentation of cationized phosphotyrosine containing peptides by atmospheric pressure MALDI/Ion trap mass spectrometry

Journal of the American Society for Mass Spectrometry
S C MoyerR J Cotter

Abstract

An investigation of phosphate loss from sodium-cationized phosphotyrosine containing peptide ions was conducted using liquid infrared (2.94 microm) atmospheric pressure matrix-assisted laser desorption/ionization (AP MALDI) coupled to an ion trap mass spectrometer (ITMS). Previous experiments in our laboratory explored the fragmentation patterns of protonated phosphotyrosine containing peptides, which experience a loss of 98 Da under CID conditions in the ITMS. This loss of 98 Da is unexpected for phosphotyrosine, given the structure of its side chain. Phosphate loss from phosphotyrosine residues seems to be dependent on the presence of arginine or lysine residues in the peptide sequence. In the absence of a basic residue, the protonated phosphotyrosine peptides do not undergo losses of HPO(3) (Delta 80 Da) nor HPO(3) + H(2)O (Delta 98 Da) in their CID spectra. However, sodium cationized phosphotyrosine containing peptides that do not contain arginine or lysine residues within their sequences do undergo losses of HPO(3) (Delta 80 Da) and HPO(3) + H(2)O (Delta 98 Da) in their CID spectra.

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Citations

Jan 31, 2006·Journal of the American Society for Mass Spectrometry·Scott D HantonJerry Zweigenbaum
Jun 27, 2008·Journal of Proteome Research·Amina S WoodsShelley N Jackson
Sep 15, 2011·Journal of Mass Spectrometry : JMS·Marko Rožman
Jun 9, 2009·Journal of Mass Spectrometry : JMS·Paul J BoersemaAlbert J R Heck
Feb 25, 2015·European Journal of Mass Spectrometry·Andreas BierstedtJens Riedel
Oct 6, 2017·Journal of the American Society for Mass Spectrometry·Mohammad A HalimMarion Girod

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