Identifying Sialylation Linkages at the Glycopeptide Level by Glycosyltransferase Labeling Assisted Mass Spectrometry

ABSTRACT: Precise assignment of sialylation linkages at the glycopeptide level is of importance in bottom-up glycoproteomics, and is also 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, an innovative strategy of glycosyltransferase labeling assisted mass spectrometry (GLAMS) was developed. After specific enzymatic labeling, oxonium ions from higher-energy C-trap dissociation (HCD) fragmentation of α2,3-sailoglycopeptides generate unique reporters to distinctly differentiate those of α2,6-sailoglycopeptide isomers.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: He Zhu  

LAB HEAD: Peng George Wang

PROVIDER: PXD016151 | Pride | 2020-04-21

REPOSITORIES: Pride