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Related Concept Videos

Protein Networks02:26

Protein Networks

An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...

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Quantifying Protein-Glycan Interactions Using Native Mass Spectrometry.

Duong T Bui1, Elena N Kitova1, Ling Han1

  • 1Department of Chemistry, University of Alberta, Edmonton, Alberta, Canada.

Mass Spectrometry Reviews
|June 30, 2025
PubMed
Summary
This summary is machine-generated.

Glycan-binding proteins (GBPs) interactions are crucial for health but poorly understood. Native mass spectrometry (nMS) offers a powerful method to map these interactions and define the full glycan interactome.

Keywords:
affinityglycansglycan‐binding proteinsnative mass spectrometrynoncovalent interactions

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Area of Science:

  • Biochemistry and Molecular Biology
  • Analytical Chemistry
  • Glycoscience

Background:

  • Glycan-binding protein (GBP) interactions with carbohydrates (glycans) are vital for numerous biological processes, impacting human health and disease.
  • The complete glycan interactome, including the repertoire and specificity of recognized glycans for most GBPs, remains largely undefined.
  • Challenges in mapping GBP-glycan interactions include glycan structural diversity, limited availability of purified glycans, complex presentation as glycoconjugates, and weak binding affinities.

Purpose of the Study:

  • To review established native mass spectrometry (nMS) methodologies for detecting and quantifying GBP-glycan interactions.
  • To discuss experimental and instrumental considerations for reliable in vitro analysis of GBP-glycan stoichiometry and affinity.
  • To highlight recent advancements in nMS for high-throughput screening, glycomics, and interactions with complex biomolecules like glycoproteins and glycosphingolipids.

Main Methods:

  • Utilizing native mass spectrometry (nMS) as a sensitive, label-free technique for discovering GBP-glycan interactions.
  • Applying nMS to quantify the stoichiometry and thermodynamic parameters of these molecular interactions.
  • Incorporating advanced nMS methods for high-throughput screening, shotgun glycomics, and analysis of interactions with glycoproteins and glycosphingolipids.

Main Results:

  • Native mass spectrometry (nMS) is demonstrated as a versatile tool for identifying GBP-glycan binding events.
  • nMS enables accurate quantification of interaction stoichiometry and thermodynamic properties.
  • Recent nMS advancements facilitate high-throughput analysis and characterization of complex glycan interactions.

Conclusions:

  • Native mass spectrometry (nMS) is poised to be a leading technology for defining the glycan interactome of GBPs.
  • Established and emerging nMS methodologies provide robust means to overcome challenges in glycan interaction mapping.
  • This review underscores the potential of nMS to advance our understanding of GBP functions in health and disease.