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Related Experiment Video

Updated: Apr 22, 2026

An Efficient Sample Preparation Method to Enhance Carbohydrate Ion Signals in Matrix-assisted Laser Desorption/Ionization Mass Spectrometry
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Quantifying protein-carbohydrate interactions using liquid sample desorption electrospray ionization mass

Yuyu Yao1, Km Shams-Ud-Doha, Rambod Daneshfar

  • 1Alberta Glycomics Center and Department of Chemistry, University of Alberta, Edmonton, AB, T6G 2G2, Canada.

Journal of the American Society for Mass Spectrometry
|October 16, 2014
PubMed
Summary

Liquid sample desorption electrospray ionization mass spectrometry (DESI-MS) accurately quantifies protein-carbohydrate interactions in vitro. This method effectively corrects for nonspecific binding and works in high salt concentrations, unlike traditional ESI-MS.

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Analyzing Large Protein Complexes by Structural Mass Spectrometry
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Area of Science:

  • Analytical Chemistry
  • Biochemistry
  • Mass Spectrometry

Background:

  • Protein-carbohydrate interactions are crucial in biological processes.
  • Accurate quantification of these interactions is essential for understanding molecular mechanisms.
  • Existing methods like isothermal titration calorimetry and ESI-MS have limitations in certain conditions.

Purpose of the Study:

  • To describe and validate the application of liquid sample desorption electrospray ionization mass spectrometry (liquid sample DESI-MS) for quantifying protein-carbohydrate interactions.
  • To assess the method's ability to correct for nonspecific binding.
  • To evaluate the suitability of liquid sample DESI-MS for measurements in high salt buffer conditions.

Main Methods:

  • Liquid sample DESI-MS was employed to measure association constants for lysozyme and a single chain antibody with specific carbohydrate ligands.
  • Results were compared with those obtained from isothermal titration calorimetry and direct ESI-MS.
  • The reference protein method was adapted to correct for nonspecific binding in liquid sample DESI-MS spectra.
  • Experiments were conducted in phosphate-buffered saline (PBS) solutions of varying concentrations.

Main Results:

  • Liquid sample DESI-MS yielded association constants in good agreement with established methods.
  • The reference protein method effectively corrected for nonspecific binding in liquid sample DESI-MS.
  • Liquid sample DESI-MS successfully monitored lysozyme-carbohydrate binding in up to 1× PBS.
  • Traditional ESI-MS binding measurements were limited to concentrations below 0.02× PBS.

Conclusions:

  • Liquid sample DESI-MS is a robust and accurate technique for quantifying protein-carbohydrate interactions in vitro.
  • The method demonstrates superior performance in high salt concentrations compared to traditional ESI-MS.
  • Liquid sample DESI-MS offers a valuable alternative for binding studies in biologically relevant buffer conditions.