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  Evaluation and optimization of high-field asymmetric waveform ion-mobility spectrometry for multiplexed quantitative site-specific N-glycoproteomics

Fang, P., Ji, Y., Silbern, I., Viner, R., Oellerich, T., Pan, K. T., et al. (2021). Evaluation and optimization of high-field asymmetric waveform ion-mobility spectrometry for multiplexed quantitative site-specific N-glycoproteomics. Analytical Chemistry, 93(25), 8846-8855. doi:10.1021/acs.analchem.1c00802.

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 Creators:
Fang, P.1, Author              
Ji , Y., Author
Silbern, I.1, Author              
Viner, R., Author
Oellerich, T.2, Author              
Pan, K. T.1, Author              
Urlaub, H.2, Author              
Affiliations:
1Research Group of Bioanalytical Mass Spectrometry, MPI for Biophysical Chemistry, Max Planck Society, ou_578613              
2Research Group of Bioanalytical Mass Spectrometry, MPI for biophysical chemistry, Max Planck Society, ou_578613              

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Free keywords: Mass spectrometry, Peptides and proteins, Carbohydrates, Mathematical methods, Chemical biology
 Abstract: The heterogeneity and complexity of glycosylation hinder the depth of site-specific glycoproteomics analysis. High-field asymmetric-waveform ion-mobility spectrometry (FAIMS) has been shown to improve the scope of bottom-up proteomics. The benefits of FAIMS for quantitative N-glycoproteomics have not been investigated yet. In this work, we optimized FAIMS settings for N-glycopeptide identification, with or without the tandem mass tag (TMT) label. The optimized FAIMS approach significantly increased the identification of site-specific N-glycopeptides derived from the purified immunoglobulin M (IgM) protein or human lymphoma cells. We explored in detail the changes in FAIMS mobility caused by N-glycopeptides with different characteristics, including TMT labeling, charge state, glycan type, peptide sequence, glycan size, and precursor m/z. Importantly, FAIMS also improved multiplexed N-glycopeptide quantification, both with the standard MS2 acquisition method and with our recently developed Glyco-SPS-MS3 method. The combination of FAIMS and Glyco-SPS-MS3 methods provided the highest quantitative accuracy and precision. Our results demonstrate the advantages of FAIMS for improved mass spectrometry-based qualitative and quantitative N-glycoproteomics.

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Language(s): eng - English
 Dates: 2021-06-162021-06-29
 Publication Status: Published in print
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 Rev. Type: Peer
 Identifiers: DOI: 10.1021/acs.analchem.1c00802
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Title: Analytical Chemistry
Source Genre: Journal
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Pages: - Volume / Issue: 93 (25) Sequence Number: - Start / End Page: 8846 - 8855 Identifier: -