TY - JOUR
T1 - Identifying Sialylation Linkages at the Glycopeptide Level by Glycosyltransferase Labeling Assisted Mass Spectrometry (GLAMS)
AU - Zhu, He
AU - Wang, Shuaishuai
AU - Liu, Ding
AU - Ding, Lang
AU - Chen, Congcong
AU - Liu, Yunpeng
AU - Wu, Zhigang
AU - Bollag, Roni
AU - Liu, Kebin
AU - Alexander, William Max
AU - Yin, Jun
AU - Ma, Cheng
AU - Li, Lei
AU - Wang, Peng George
N1 - Publisher Copyright:
© 2020 American Chemical Society.
PY - 2020/5/5
Y1 - 2020/5/5
N2 - 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.
AB - 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.
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U2 - 10.1021/acs.analchem.9b05068
DO - 10.1021/acs.analchem.9b05068
M3 - Article
AN - SCOPUS:85084830654
SN - 0003-2700
VL - 92
SP - 6297
EP - 6303
JO - Analytical Chemistry
JF - Analytical Chemistry
IS - 9
ER -