Site-specific Localization of D-Amino Acids in Bioactive Peptides by Ion Mobility Spectrometry

Author(s):  
Chenxi Jia ◽  
Christopher B. Lietz ◽  
Qing Yu ◽  
Lingjun Li

2014 ◽  
Vol 86 (6) ◽  
pp. 2972-2981 ◽  
Author(s):  
Chenxi Jia ◽  
Christopher B. Lietz ◽  
Qing Yu ◽  
Lingjun Li




2021 ◽  
Author(s):  
Pan Fang ◽  
Yanlong Ji ◽  
Ivan Silbern ◽  
Rosa Viner ◽  
Thomas Oellerich ◽  
...  

The heterogeneity and complexity of glycosylation hinder the depth of site-specific glycoproteomics analysis. High-field asymmetric-waveform ion-mobility spectrometry (FAIMS) has 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 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 provided the highest quantitative accuracy and precision. Our results demonstrate the advantages of FAIMS for improved mass-spectrometry-based qualitative and quantitative N glycoproteomics.



2001 ◽  
Vol 73 (13) ◽  
pp. 3028-3034 ◽  
Author(s):  
Luther W. Beegle ◽  
Isik Kanik ◽  
Laura Matz ◽  
Herbert H. Hill


2004 ◽  
Vol 108 (27) ◽  
pp. 5785-5792 ◽  
Author(s):  
Paul V. Johnson ◽  
Hugh I. Kim ◽  
Luther W. Beegle ◽  
Isik Kanik




2000 ◽  
Vol 902 (2) ◽  
pp. 433-437 ◽  
Author(s):  
G.Reid Asbury ◽  
Herbert H Hill






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