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Related Experiment Video

Updated: Nov 11, 2025

Glycomics-Guided Glycoproteomics Facilitates Comprehensive Profiling of the Glycoproteome in Complex Tumor Microenvironments

Glycomics-Guided Glycoproteomics Facilitates Comprehensive Profiling of the Glycoproteome in Complex Tumor Microenvironments

Published on: February 7, 2025

Glycoproteomics using chemical immobilization.

¹Johns Hopkins University, Baltimore, Maryland, USA.

Current Protocols in Protein Science

|April 23, 2008

Summary

This summary is machine-generated.

This study presents a novel method for isolating and identifying glycopeptides and their glycosylation sites using solid-phase extraction and mass spectrometry. This technique aids in the analysis of important extracellular proteins for diagnostic and therapeutic applications.

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Last Updated: Nov 11, 2025

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Glycopeptide Capture for Cell Surface Proteomics

Glycopeptide Capture for Cell Surface Proteomics

Published on: May 9, 2014

Area of Science:

Biochemistry
Proteomics
Analytical Chemistry

Background:

Protein glycosylation is a crucial post-translational modification, particularly for extracellular proteins.
These modified proteins are vital in cellular communication and are key targets for diagnostics and therapeutics.
Analyzing glycosylation patterns provides insights into protein function and disease states.

Purpose of the Study:

To develop and describe a robust method for the solid-phase extraction of glycopeptides.
To enable the subsequent identification of glycopeptides and pinpoint specific glycosylation sites.
To facilitate the analysis of glycosylated proteins from diverse biological samples.

Main Methods:

Solid-phase extraction utilizing hydrazide chemistry for glycopeptide conjugation.
Specific cleavage and release of formerly glycosylated peptides from the solid support.
Identification of recovered peptides and glycosylation sites via tandem mass spectrometry.

Main Results:

Successful isolation and enrichment of glycopeptides from complex biological matrices.
Accurate identification of glycopeptides and precise localization of glycosylation sites.
Demonstrated applicability to proteins derived from cells, body fluids, and tissues.

Conclusions:

The described method offers an efficient approach for glycopeptide enrichment and site analysis.
This technique enhances the study of extracellular protein glycosylation.
It provides a valuable tool for advancing glycoproteomics in diagnostics and therapeutics.