In:
Frontiers in Chemistry, Frontiers Media SA, Vol. 9 ( 2021-8-11)
Abstract:
Reversible protein glycosylation and phosphorylation tightly modulate important cellular processes and are closely involved in pathological processes in a crosstalk dependent manner. Because of their significance and low abundances of glyco- and phosphopeptides, several strategies have been developed to simultaneously enrich and co-elute glyco- and phosphopeptides. However, the co-existence of deglycosylated peptides and phosphopeptides aggravates the mass spectrometry analysis. Herein we developed a novel strategy to analyze glyco- and phosphopeptides based on simultaneous enrichment with TiO 2 , on-line deglycosylation and collection of deglycosylated peptides, and subsequent elution of phosphopeptides. To optimize on-line deglycosylation conditions, the solution pH, buffer types and concentrations, and deglycosylation time were investigated. The application of this novel strategy to 100 μg mouse brain resulted in 355 glycopeptides and 1,975 phosphopeptides, which were 2.5 and 1.4 folds of those enriched with the reported method. This study will expand the application of TiO 2 and may shed light on simultaneously monitoring protein multiple post-translational modifications.
Type of Medium:
Online Resource
ISSN:
2296-2646
DOI:
10.3389/fchem.2021.703176
DOI:
10.3389/fchem.2021.703176.s001
DOI:
10.3389/fchem.2021.703176.s002
DOI:
10.3389/fchem.2021.703176.s003
DOI:
10.3389/fchem.2021.703176.s004
DOI:
10.3389/fchem.2021.703176.s005
DOI:
10.3389/fchem.2021.703176.s006
DOI:
10.3389/fchem.2021.703176.s007
DOI:
10.3389/fchem.2021.703176.s008
DOI:
10.3389/fchem.2021.703176.s009
Language:
Unknown
Publisher:
Frontiers Media SA
Publication Date:
2021
detail.hit.zdb_id:
2711776-5
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