Exploiting ion‐mobility mass spectrometry for unraveling proteome complexity

Stan Perchepied; Zhuoheng Zhou; Goran Mitulović; Sebastiaan Eeltink

doi:10.1002/jssc.202300512

Exploiting ion‐mobility mass spectrometry for unraveling proteome complexity

Stan Perchepied, Zhuoheng Zhou, Goran Mitulović, Sebastiaan Eeltink

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Abstract

Ion mobility spectrometry-mass spectrometry (IMS-MS) is experiencing rapid growth in proteomic studies, driven by its enhancements in dynamic range and throughput, increasing the quantitation precision, and the depth of proteome coverage. The core principle of ion mobility spectrometry is to separate ions in an inert gas under the influence of an electric field based on differences in drift time. This minireview provides an introduction to IMS operation modes and a description of advantages and limitations is presented. Moreover, the principles of trapped IMS-MS (TIMS-MS), including parallel accumulation-serial fragmentation are discussed. Finally, emerging applications linked to TIMS focusing on sample throughput (in clinical proteomics) and sensitivity (single-cell proteomics) are reviewed, and the possibilities of intact protein analysis are discussed.

Original language	English
Article number	2300512
Journal	Journal of Separation Science
Volume	46
Issue number	18
DOIs	https://doi.org/10.1002/jssc.202300512
Publication status	Published - 25 Sep 2023

Bibliographical note

Funding Information:
Support of this work by a grant from the Research Foundation Flanders-FWO (grant number: G033018N) is gratefully acknowledged. SE acknowledges an Excellence of Science grant (30897864) of the Research Foundation Flanders and the Fonds de la Recherche Scientifique (FWO-FRNS).

Funding Information:
Support of this work by a grant from the Research Foundation Flanders‐FWO (grant number: G033018N) is gratefully acknowledged. SE acknowledges an Excellence of Science grant (30897864) of the Research Foundation Flanders and the Fonds de la Recherche Scientifique (FWO‐FRNS).

Publisher Copyright:
© 2023 Wiley-VCH GmbH.

Keywords

timsTOF
Parallel accumulation-serial fragmentation
Clinical proteomics
Single-cell analysis
Data-independent acquisition

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2023_JSS_SP_Review TIMS_pureAccepted author manuscript, 744 KBLicence: Unspecified

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title = "Exploiting ion‐mobility mass spectrometry for unraveling proteome complexity",

abstract = "Ion mobility spectrometry-mass spectrometry (IMS-MS) is experiencing rapid growth in proteomic studies, driven by its enhancements in dynamic range and throughput, increasing the quantitation precision, and the depth of proteome coverage. The core principle of ion mobility spectrometry is to separate ions in an inert gas under the influence of an electric field based on differences in drift time. This minireview provides an introduction to IMS operation modes and a description of advantages and limitations is presented. Moreover, the principles of trapped IMS-MS (TIMS-MS), including parallel accumulation-serial fragmentation are discussed. Finally, emerging applications linked to TIMS focusing on sample throughput (in clinical proteomics) and sensitivity (single-cell proteomics) are reviewed, and the possibilities of intact protein analysis are discussed.",

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note = "Funding Information: Support of this work by a grant from the Research Foundation Flanders-FWO (grant number: G033018N) is gratefully acknowledged. SE acknowledges an Excellence of Science grant (30897864) of the Research Foundation Flanders and the Fonds de la Recherche Scientifique (FWO-FRNS). Funding Information: Support of this work by a grant from the Research Foundation Flanders‐FWO (grant number: G033018N) is gratefully acknowledged. SE acknowledges an Excellence of Science grant (30897864) of the Research Foundation Flanders and the Fonds de la Recherche Scientifique (FWO‐FRNS). Publisher Copyright: {\textcopyright} 2023 Wiley-VCH GmbH.",

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N1 - Funding Information: Support of this work by a grant from the Research Foundation Flanders-FWO (grant number: G033018N) is gratefully acknowledged. SE acknowledges an Excellence of Science grant (30897864) of the Research Foundation Flanders and the Fonds de la Recherche Scientifique (FWO-FRNS). Funding Information: Support of this work by a grant from the Research Foundation Flanders‐FWO (grant number: G033018N) is gratefully acknowledged. SE acknowledges an Excellence of Science grant (30897864) of the Research Foundation Flanders and the Fonds de la Recherche Scientifique (FWO‐FRNS). Publisher Copyright: © 2023 Wiley-VCH GmbH.

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AB - Ion mobility spectrometry-mass spectrometry (IMS-MS) is experiencing rapid growth in proteomic studies, driven by its enhancements in dynamic range and throughput, increasing the quantitation precision, and the depth of proteome coverage. The core principle of ion mobility spectrometry is to separate ions in an inert gas under the influence of an electric field based on differences in drift time. This minireview provides an introduction to IMS operation modes and a description of advantages and limitations is presented. Moreover, the principles of trapped IMS-MS (TIMS-MS), including parallel accumulation-serial fragmentation are discussed. Finally, emerging applications linked to TIMS focusing on sample throughput (in clinical proteomics) and sensitivity (single-cell proteomics) are reviewed, and the possibilities of intact protein analysis are discussed.

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Exploiting ion‐mobility mass spectrometry for unraveling proteome complexity

Abstract

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Keywords

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