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Simple capillary electrophoresis-mass spectrometry method for complex glycan analysis using a flow-through microvial

Roxana G Jayo1, Morten Thaysen-Andersen, Petrus W Lindenburg

  • 1Department of Chemistry, University of British Columbia , Vancouver V6T 1Z4, British Columbia, Canada.

Analytical Chemistry
|May 31, 2014
PubMed
Summary

This study introduces a novel capillary electrophoresis-mass spectrometry (CE-MS) method for simultaneous profiling of neutral and sialylated glycans without labeling. The advanced CE-MS technique offers comprehensive glycosylation analysis for therapeutic glycoproteins.

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Area of Science:

  • Analytical Chemistry
  • Biochemistry
  • Glycomics

Background:

  • Glycosylation analysis is crucial for characterizing therapeutic glycoproteins.
  • Existing methods often require derivatization or labeling, complicating analysis.
  • Simultaneous profiling of neutral and sialylated glycans presents a significant challenge.

Purpose of the Study:

  • To develop and optimize a capillary electrophoresis-mass spectrometry (CE-MS) method for simultaneous profiling of neutral and sialylated glycans.
  • To analyze N-glycans from human immunoglobulin G (IgG) and recombinant human erythropoietin (rHuEPO) without derivatization or labeling.
  • To demonstrate the potential of CE-MS for comprehensive glycosylation profiling and characterization of secondary glycan modifications.

Main Methods:

  • Utilized a flow-through microvial to interface capillary electrophoresis (CE) with mass spectrometry (MS).
  • Employed a neutral, hydrophilic coated capillary with near-zero electroosmotic flow and reversed CE polarity.
  • Optimized with negative ion electrospray ionization mass spectrometry (ESI-MS), including triple quadrupole MS and ultrahigh resolution TOF-MS.

Main Results:

  • Successfully profiled both neutral and sialylated N-glycans from IgG and rHuEPO without labeling or desialylation.
  • Identified over 70 glycans in rHuEPO using high sensitivity and high mass accuracy TOF-MS.
  • Reported novel mono- and di-sialylated tetra-antennary N-glycans and a mono-sialylated tri-antennary N-glycan of rHuEPO for the first time.
  • Revealed extensive glycan heterogeneity, including acetylation, Neu5Ac/Neu5Gc variation, and N-acetyl-lactosamine repeats in rHuEPO N-glycans.
  • Comparative analysis with porous graphitic carbon-based LC-MS/MS confirmed the comprehensive profiling capabilities.

Conclusions:

  • The developed CE-MS method provides a powerful, label-free approach for simultaneous profiling of neutral and sialylated glycans.
  • This technique offers detailed insights into secondary glycan modifications and heterogeneity.
  • CE-MS serves as a valuable complementary tool for characterizing therapeutic glycoproteins, simplifying the analytical workflow.