Low-resolution FAIMS for increased peptide coverage in low-load and single-cell proteomics
Field Asymmetric Ion Mobility Spectrometry (FAIMS) is an indispensable tool in single-cell and low-input proteomics. Here, we show that tuning FAIMS resolution via electrode temperature modulation improves sensitivity. We demonstrate that lowering FAIMS resolution broadens the compensation voltage window, thereby increasing ion transmission. This significantly improves ion counts, quantitative precision and peptide identifications by 25-34%. These results were mirrored when analyzing single cell samples.
Authors
- Karl Mechtler (ORCID: https://orcid.org/0000-0002-3392-9946)
- Manuel Matzinger (ORCID: https://orcid.org/0000-0002-9765-7951)
- Michael W. Belford
- Dominic G. Hoch (ORCID: https://orcid.org/0000-0002-3323-1468)
- Lilian R. Heil (ORCID: https://orcid.org/0000-0002-9462-7327)
Institutions
- Institute of Molecular Biotechnology (AT)
- Gregor Mendel Institute of Molecular Plant Biology (AT)
- Research Institute of Molecular Pathology (AT)
- Thermo Fisher Scientific (Switzerland) (CH)
- Thermo Fisher Scientific (United States) (US)
- Vienna Biocenter (AT)
Publication Details
- Journal
- Scientific Reports
- Published
- 2026-03-21
- DOI
- https://doi.org/10.1038/s41598-026-45228-3
- Primary Topic
- Mass Spectrometry Techniques and Applications
- Type
- article
- Field-Weighted Citation Impact
- 0.00