Identifying Sialylation Linkages at the Glycopeptide Level by Glycosyltransferase Labeling Assisted Mass Spectrometry (GLAMS)
| Autor: | Congcong Chen, Zhigang Wu, Jun Yin, Peng George Wang, Cheng Ma, William M. Alexander, Lang Ding, Shuaishuai Wang, Roni J. Bollag, Ding Liu, Lei Li, Yunpeng Liu, He Zhu, Kebin Liu |
|---|---|
| Rok vydání: | 2020 |
| Předmět: |
Azides
Glycosylation Sialoglycoproteins 010402 general chemistry Mass spectrometry 01 natural sciences Article Analytical Chemistry Campylobacter jejuni chemistry.chemical_compound Bacterial Proteins Isomerism Sialoglycopeptides Tandem Mass Spectrometry Glycosyltransferase Animals Humans Amino Acid Sequence Fetuins Peptide sequence Chromatography High Pressure Liquid Monomeric GTP-Binding Proteins chemistry.chemical_classification biology Chemistry 010401 analytical chemistry Hexosamines Blood Proteins 0104 chemical sciences Glycoproteomics Glycopeptide level Biochemistry Carbohydrate Sequence biology.protein Cattle Glycoprotein |
| Zdroj: | Anal Chem |
| ISSN: | 1520-6882 |
| Popis: | Precise assignment of sialylation linkages at the glycopeptide level is of importance in bottom-up glycoproteomics and an indispensable step to understand the function of glycoproteins in pathogen-host interactions and cancer progression. Even though some efforts have been dedicated to the discrimination of α2,3/α2,6-sialylated isomers, unambiguous identification of sialoglycopeptide isomers is still needed. Herein, we developed an innovative glycosyltransferase labeling assisted mass spectrometry (GLAMS) strategy. After specific enzymatic labeling, oxonium ions from higher-energy C-trap dissociation (HCD) fragmentation of α2,3-sailoglycopeptides then generate unique reporters to distinctly differentiate those of α2,6-sailoglycopeptide isomers. With this strategy, a total of 1236 linkage-specific sialoglycopeptides were successfully identified from 161 glycoproteins in human serum. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|