Proteomics

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High-field asymmetric waveform ion mobility spectrometry interface enhances parallel reaction monitoring on an Orbitrap mass spectrometer

ABSTRACT: High-field asymmetric waveform ion mobility spectrometry (FAIMS) enables gas phase separations on a chromatographic timescale and has become a useful tool for proteomic applications. Despite its emerg-ing utility, however, the molecular determinants underlying peptide separation by FAIMS have not been systematically investigated. Here, we characterize peptide transmission in a FAIMS device across a broad range of compensation voltages (CV) and used machine learning to identify charge state and 3D electrostatic peptide potential as major contributors to peptide intensity at a given CV. We also demon-strate that the machine learning model can be used to predict optimized CV values for peptides which significantly improves parallel reaction monitoring workflows. Together these data provide insight into peptide separation by FAIMS and highlight its utility in targeted proteomic applications.

INSTRUMENT(S): Orbitrap Eclipse

ORGANISM(S): Homo Sapiens (ncbitaxon:9606)

SUBMITTER: James Wohlschlegel  

PROVIDER: MSV000089014 | MassIVE | Mon Mar 07 09:43:00 GMT 2022

REPOSITORIES: MassIVE

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High-Field Asymmetric Waveform Ion Mobility Spectrometry Interface Enhances Parallel Reaction Monitoring on an Orbitrap Mass Spectrometer.

Deng Weixian W   Sha Jihui J   Xue Fanglei F   Jami-Alahmadi Yasaman Y   Plath Kathrin K   Wohlschlegel James J  

Analytical chemistry 20221108 46

High-field asymmetric waveform ion mobility spectrometry (FAIMS) enables gas-phase separations on a chromatographic time scale and has become a useful tool for proteomic applications. Despite its emerging utility, however, the molecular determinants underlying peptide separation by FAIMS have not been systematically investigated. Here, we characterize peptide transmission in a FAIMS device across a broad range of compensation voltages (CVs) and used machine learning to identify charge state and  ...[more]

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