Comparing peptide identifications by FAIMS versus quadrupole gas-phase fractionation
D. A. Faivre, C. D. McGann, G. E. Merrihew, D. K. Schweppe, M. J. MacCoss
Abstract
High-field asymmetric waveform ion mobility spectrometry (FAIMS) coupled to liquid chromatography-mass spectrometry (LC-MS) has been shown to increase peptide and protein detections compared to LC-MS/MS alone. However, FAIMS has not been compared to other methods of gas-phase fractionation, such as quadrupole gas-phase fractionation, which could increase our understanding of the mechanisms of improvement. The goal of this work was to assess whether FAIMS improves peptide identifications because 1) gas-phase fractionation enables the analysis of less abundant signals by excluding more abundant precursors from filling the ion trap, 2) the use of FAIMS reduces co-isolation of peptides during the MS/MS process resulting in a reduction of chimeric spectra, or 3) a combination of both. To investigate these hypotheses, pooled human brain tissue samples were measured in triplicate using FAIMS gas-phase fractionation, quadrupole gas-phase fractionation, or no gas-phase fractionation on two Thermo Eclipse Tribrid Mass Spectrometers. On both instruments, our data confirmed prior observations that FAIMS increased the number of peptides identified. We further demonstrated that the main benefit of FAIMS is due to the reduced co-isolation of persistent peptide precursor ions, which results in a decrease in chimeric spectra.
02 /Specification & Classification
Click any tag to browse matching papers- Organism
- Assay
- Research Focus
- Approach
Reproducibility ledger
Nobody has reported trying to reproduce this paper yet. Did you replicate an experiment or run the code? Your report saves the next lab a week.
Sign in to file a reproducibility report.
Related papers
- Expanding the depth and sensitivity of cross-link identification by differential ion mobility using FAIMS
L. Schnirch, M. Nadler-Holly, … F. Liu·bioRxiv·Apr 23, 2020
- False positive glycopeptide identification via in-FAIMS fragmentation
V. Rangel-Angarita, K. E. Mahoney, … S. A. Malaker·bioRxiv·May 28, 2023
- IMPROVED N- AND O-GLYCOPEPTIDE IDENTIFICATION USING HIGH-FIELD ASYMMETRIC WAVEFORM ION MOBILITY SPECTROMETRY (FAIMS)
K. Alagesan, R. Ahmed-Begrich, E. Charpentier·bioRxiv·Dec 12, 2022
- Getting more out of FLAG-Tag co-immunoprecipitation mass spectrometry experiments using FAIMS.
C.-S. Ang, J. Sacharz, … N. A. Williamson·bioRxiv·Jun 15, 2021
- Low-resolution FAIMS for increased peptide coverage in low-load and single-cell proteomics
Dominic G. Hoch, Michael W. Belford, … Manuel Matzinger·Scientific ReportsPeer-reviewed·Mar 21, 2026
- Analysis of FAIMS for the Study of Affinity-Purified Protein Complexes Using the Orbitrap Ascend Tribrid Mass Spectrometer
Pratik Goswami, Joseph Cesare, … Michael P. Washburn·Molecular OmicsPeer-reviewed·May 7, 2025