Ion mobility in gas and liquid phases: How much orthogonality is obtained in capillary electrophoresis-ion mobility-mass spectrometry?

Ion mobility-mass spectrometry (IM-MS) is an ever-evolving tool to separate ions in the gas phase according to electrophoretic mobility with subsequent mass determination. CE is rarely coupled to IM-MS, possibly due to similar separation mechanisms based on electrophoretic mobility. Here, we investi...

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Bibliographic Details
Published in:Electrophoresis 2024-04, Vol.45 (7-8), p.735-742
Main Authors: Schairer, Jasmin, Plathe, Florian, Hudelmaier, Sonja, Belau, Eckhard, Pengelley, Stuart, Kruse, Lena, Neusüß, Christian
Format: Article
Language:English
Subjects:
Amino acids
Electrophoresis
Electrophoresis, Capillary - methods
Gases - chemistry
HeLa Cells
Humans
Ion Mobility Spectrometry - methods
Ionic mobility
Ions - chemistry
Liquid phases
Mass spectrometry
Mass Spectrometry - methods
Orthogonality
Peptides
Peptides - analysis
Peptides - chemistry
Scientific imaging
Solvation
Vapor phases
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Summary:Ion mobility-mass spectrometry (IM-MS) is an ever-evolving tool to separate ions in the gas phase according to electrophoretic mobility with subsequent mass determination. CE is rarely coupled to IM-MS, possibly due to similar separation mechanisms based on electrophoretic mobility. Here, we investigate the orthogonality of CE and ion mobility (IM) by analyzing a complex peptide mixture (tryptic digest of HeLa proteins) with trapped ion mobility mass spectrometry (TIMS-MS). Using the nanoCEasy interface, excellent sensitivity was achieved by identifying thousands of peptides and achieving a peak capacity of 7500 (CE: 203-323 in a 150 cm long capillary, IM: 27-31). Plotting CE versus mass and CE versus (inverse) mobility, a clear grouping in curved striped patterns is observed according to the charge-to-size and mass-to-charge ratios. The peptide charge in the acidic background electrolyte can be estimated from the number of basic amino acids, with a few exceptions where neighboring effects reduce the positive charge. A surprisingly high orthogonality of CE and IM is observed, which is obviously caused by solvation effects leading to different charges and sizes in the liquid phase compared to the gas phase. A high orthogonality of CE and ion mobility is expected to be observed for other peptide samples as well as other substance classes, making CE-IM-MS a promising tool for various applications.
ISSN:0173-0835
1522-2683
DOI:10.1002/elps.202300210