TY - JOUR
T1 - Exploiting ion‐mobility mass spectrometry for unraveling proteome complexity
AU - Perchepied, Stan
AU - Zhou, Zhuoheng
AU - Mitulović, Goran
AU - Eeltink, Sebastiaan
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.
PY - 2023/9/25
Y1 - 2023/9/25
N2 - 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.
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.
KW - timsTOF
KW - Parallel accumulation-serial fragmentation
KW - Clinical proteomics
KW - Single-cell analysis
KW - Data-independent acquisition
UR - http://www.scopus.com/inward/record.url?scp=85172087812&partnerID=8YFLogxK
U2 - 10.1002/jssc.202300512
DO - 10.1002/jssc.202300512
M3 - Article
VL - 46
JO - Journal of Separation Science
JF - Journal of Separation Science
SN - 1615-9306
IS - 18
M1 - 2300512
ER -