|Abstract Title:||FAIMS mass spectrometry for the analysis of peptides and proteins|
|Session Choice:||Ion Mobility - Mass Spectrometry (BMSS)|
|Presenter Name:||Prof Helen Cooper|
|Company/Organisation:||University of Birmingham|
Abstract Information :
High field asymmetric waveform ion mobility spectrometry (FAIMS), also known as differential ion mobility spectrometry, is emerging as a powerful technique in biomolecular analysis. FAIMS relies on differences in ion mobility in high and low electric fields to achieve gas phase separation of ions at atmospheric pressure, offering advantages including reduced interference from ions of similar mass-to-charge (m/z), and separation of isomers and positional variants.
Here, we demonstrate the application of FAIMS in proteomics analyses and in ambient surface analyses. The inclusion of FAIMS in large-scale phosphoproteomics analysis of the fibroblast growth factor signalling pathway resulted in an increase in the relative proportion of pThr and pTyr and increase in the identification of multiply-phosphorylated peptides. The application of FAIMS to the study of O-glycosylation in flagellin from Campylobacter jejuni 11168 revealed multiply- and differentially glycosylated peptides. We also show that by coupling liquid extraction surface analysis (LESA) with FAIMS significant improvements in the direct analysis of complex biological samples are achieved. The inclusion of FAIMS results in improved signal to noise ratios, shorter acquisition times, and separation of molecular classes, e.g., proteins and lipids. The benefits afforded by FAIMS suggest that the technique could find applications in LESA mass spectrometry imaging protocols. We show LESA FAIMS mass spectrometry imaging of proteins in sections of mouse brain and liver tissue, and compared those results with LESA mass spectrometry images obtained in the absence of FAIMS.