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A Quantitative Glycomics and Proteomics Combined Purification Strategy
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High-throughput glycomics: optimization of sample preparation.

I Trbojević Akmačić1, I Ugrina, J Štambuk

  • 1Genos Glycoscience Research Laboratory, Zagreb, 10000, Croatia. mpucicbakovic@genos.hr.

Biochemistry. Biokhimiia
|November 7, 2015
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Summary

This study presents a new, efficient method for preparing plasma N-glycans for analysis. The optimized hydrophilic interaction liquid chromatography method ensures high reproducibility for detecting biological variations in the plasma N-glycome.

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Area of Science:

  • Biochemistry
  • Analytical Chemistry
  • Proteomics

Background:

  • Glycosylation is crucial for protein structure, folding, and function.
  • Altered glycosylation patterns are linked to various diseases.
  • Plasma N-glycan analysis is challenging due to sample complexity, unlike antibody glycan analysis.

Purpose of the Study:

  • To develop and optimize a high-throughput sample preparation method for plasma N-glycan analysis.
  • To improve the reproducibility and efficiency of plasma N-glycan purification.
  • To enable reliable detection of biological variability in the plasma N-glycome.

Main Methods:

  • Development of a solid-phase extraction method for labeled plasma glycans.
  • Evaluation of different stationary phases (cellulose, silica gel, Bio-Gel, GHP filter) for glycan clean-up.
  • Optimization using Plackett-Burman screening design and validation for reproducibility.

Main Results:

  • The hydrophilic GHP filter plate with cold 96% acetonitrile demonstrated the highest reproducibility and ease of use for glycan purification.
  • The developed method is fast, cost-effective, and robust over time.
  • Validated method shows minimal variation across different steps, days, and individuals.

Conclusions:

  • A highly reproducible, cost-effective, and user-friendly method for plasma N-glycan preparation has been established.
  • This method facilitates accurate analysis of the plasma N-glycome.
  • Enables better understanding of disease-associated glycan alterations.