Proteomics

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Sialo-glycoproteome of Human lung cancer cell by LC-MSMS

ABSTRACT: Alterations in protein glycosylation, especially the terminal sialylation, are closely correlated with physiological and pathological regulation. Due to the low ionization efficiency of sialo-glycopeptides and frequently observed dissociation of sialic acid residues during mass spectrometry analysis, tools to enrich the sialo-glycopeptides are essential to enhance detection sensitivity and identification efficiency in sialo-glycoproteomics. In this study, we present the first application of zwitterionic hydrophilic interaction chromatography (ZIC-cHILIC) material in StageTip for simultaneous enrichment and fractionation of intact glycopeptides at proteome scale. With the demonstrated enrichment specificity and identification depth, the stepwise-ZIC-cHILIC can be an efficient enrichment method for the discovery of glycosylation sites and native glycotope for many sample types.

INSTRUMENT(S): Orbitrap Fusion

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture

DISEASE(S): Non-small Cell Lung Carcinoma

SUBMITTER: Yi-Ju Chen  

LAB HEAD: Yu-Ju Chen

PROVIDER: PXD010456 | Pride | 2022-02-25

REPOSITORIES: Pride

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ZIC-cHILIC-Based StageTip for Simultaneous Glycopeptide Enrichment and Fractionation toward Large-Scale N-Sialoglycoproteomics.

Chen Yi-Ju YJ   Yen Ta-Chi TC   Lin Yu-Hsien YH   Chen Yan-Lin YL   Khoo Kay-Hooi KH   Chen Yu-Ju YJ  

Analytical chemistry 20211115 48

Alterations of protein glycosylation are closely related with pathophysiological regulation. Due to the structural macro- and microheterogeneity, low stoichiometry, and low ionization efficiency of glycopeptides, high-performance tools to enrich glycopeptides, especially the negatively charged and labile sialoglycopeptides, are essential to enhance the identification of the underexplored glycoproteome. Here, we present the first implementation of zwitterionic hydrophilic interaction chromatograp  ...[more]

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