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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 phosphopeptides

Reputable Mentor II
Reputable Mentor II
Xuan Y, Creese AJ, Horner JA, Cooper HJ.
Rapid Commun Mass Spectrom. 2009 Jul;23(13):1963-9.
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.
Thermo Fisher Scientific, Hanna-Kunath-Str. 11, 28199 Bremen, Germany.
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‎10-15-2021 11:34 AM
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