Ion Mobility Separation of Peptide Isotopomers

Kaszycki, Julia L.; Bowman, Andrew P.; Shvartsburg, Alexandre A.

doi:10.1007/s13361-016-1367-3

Cited by 45 publications

(98 citation statements)

References 33 publications

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“…The specification of isotopic envelopes was not considered in IMS until very recently (Valentine & Clemmer, ), as all isotopologues were previously indistinguishable because of limited resolution. With the improvements in resolving power of both linear IMS and FAIMS, separation of isotopologues is now possible (Shvartsburg, Clemmer, & Smith, ; Kaszycki, Bowman, & Shvartsburg, ; Kirk, Raddatz, & Zimmermann, ) and necessitates defining the isotopic composition of species in question. By analogy to MS, we propose in linear IMS the monoisotopic ion mobility (raw or reduced) for the monoisotopic species, average mobility for the integral over full mobility distribution for all natural isotopologues, and most probable mobility for the most abundant isotopologue.…”

Section: Reporting Ion Mobility Measurementsmentioning

confidence: 99%

Recommendations for reporting ion mobility Mass Spectrometry measurements

Gabelica

Shvartsburg

Afonso

et al. 2019

Mass Spectrometry Reviews

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376

477

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Here we present a guide to ion mobility mass spectrometry experiments, which covers both linear and nonlinear methods: what is measured, how the measurements are done, and how to report the results, including the uncertainties of mobility and collision cross section values. The guide aims to clarify some possibly confusing concepts, and the reporting recommendations should help researchers, authors and reviewers to contribute comprehensive reports, so that the ion mobility data can be reused more confidently. Starting from the concept of the definition of the measurand, we emphasize that (i) mobility values ( K 0 ) depend intrinsically on ion structure, the nature of the bath gas, temperature, and E / N ; (ii) ion mobility does not measure molecular surfaces directly, but collision cross section (CCS) values are derived from mobility values using a physical model; (iii) methods relying on calibration are empirical (and thus may provide method‐dependent results) only if the gas nature, temperature or E / N cannot match those of the primary method. Our analysis highlights the urgency of a community effort toward establishing primary standards and reference materials for ion mobility, and provides recommendations to do so. © 2019 The Authors. Mass Spectrometry Reviews Published by Wiley Periodicals, Inc.

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Section: Reporting Ion Mobility Measurementsmentioning

confidence: 99%

Recommendations for reporting ion mobility Mass Spectrometry measurements

Gabelica

Shvartsburg

Afonso

et al. 2019

Mass Spectrometry Reviews

Self Cite

376

477

View full text Add to dashboard Cite

show abstract

“…Whereas the separation in DTIMS is based on an ion’s CCS-to-charge ratio, the separation in FAIMS results from the mobility difference of the analyte and buffer gas interactions in both strong and weak electric fields. FAIMS has been utilized for pharmaceutical analyses (119), separating charge states (120, 121), and recently, its power to distinguish isobars (122), isomers (123), isotopomers (124), and protein conformers (125) has been highlighted. Both DTIMS and FAIMS have shown great potential in enhancing biological analyses when coupled with MS platforms by reducing chemical noise and detecting low-abundance analytes in complex biological matrices (126).…”

Section: Field Asymmetric–and Drift Tube Ion Mobility Spectrometry–mamentioning

confidence: 99%

Coupling Front-End Separations, Ion Mobility Spectrometry, and Mass Spectrometry For Enhanced Multidimensional Biological and Environmental Analyses

Zheng

Wojcik

Zhang

et al. 2017

Annual Rev. Anal. Chem.

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Ion mobility spectrometry (IMS) is a widely used analytical technique for rapid molecular separations in the gas phase. Though IMS alone is useful, its coupling with mass spectrometry (MS) and front-end separations is extremely beneficial for increasing measurement sensitivity, peak capacity of complex mixtures, and the scope of molecular information available from biological and environmental sample analyses. In fact, multiple disease screening and environmental evaluations have illustrated that the IMS-based multidimensional separations extract information that cannot be acquired with each technique individually. This review highlights three-dimensional separations using IMS-MS in conjunction with a range of front-end techniques, such as gas chromatography, supercritical fluid chromatography, liquid chromatography, solid-phase extractions, capillary electrophoresis, field asymmetric ion mobility spectrometry, and microfluidic devices. The origination, current state, various applications, and future capabilities of these multidimensional approaches are described in detail to provide insight into their uses and benefits.

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“…Previous studies have reported the benefits of FAIMS to improve proteome coverage and to reduce the extent of co-fragmentation that impedes the identification of low-abundance peptide ions (28)(29)(30)(31)(32)(33). The separation capability of FAIMS also facilitates the resolution of isomeric peptides, including histone variants and isomeric phosphopeptides (34)(35)(36)(37)(38)(39)(40)(41)(42)(43)(44). Furthermore, the reduction of peptide co-elution and co-fragmentation observed with FAIMS can significantly improve the accuracy and the comprehensiveness of multiplex proteomic analyses (45).…”

Section: Introductionmentioning

confidence: 99%