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High‐field asymmetric waveform ion mobility spectrometry (FAIMS) coupled with high‐resolution electron transfer dissociation mass spectrometry for the analysis of isobaric phosphopeptides
Author(s) -
Xuan Yue,
Creese Andrew J.,
Horner Julie A.,
Cooper Helen J.
Publication year - 2009
Publication title -
rapid communications in mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.528
H-Index - 136
eISSN - 1097-0231
pISSN - 0951-4198
DOI - 10.1002/rcm.4101
Subject(s) - chemistry , ion mobility spectrometry , electron transfer dissociation , mass spectrometry , chromatography , isobaric labeling , tandem mass spectrometry , phosphopeptide , protein mass spectrometry , dissociation (chemistry) , analytical chemistry (journal) , resolution (logic) , peptide , organic chemistry , biochemistry , artificial intelligence , computer science
We have applied high‐field asymmetric waveform ion mobility spectrometry (FAIMS) to the analysis of the phosphopeptides APLpSFRGSLPKSYVK, APLSFRGpSLPKSYVK, and APLSFRGSLPKpSYVK. The peptides have identical amino acid sequences and differ only in the site of phosphorylation. The results show that FAIMS is capable of at least partially separating these species. Separation was confirmed by coupling FAIMS with high‐resolution electron transfer dissociation (ETD) mass spectrometry. Phosphorylation is retained on the ETD peptide fragments thereby allowing assignment of the site of the modification. Co‐eluting phosphopeptides which differ only in the site of modification are frequently observed in liquid chromatography/tandem mass spectrometry phosphoproteomics experiments, and therefore these proof‐of‐principle results have implications for the application of FAIMS in that field. Copyright © 2009 John Wiley & Sons, Ltd.