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Exploring Protein-Glycan Interactions: Advances in Nuclear Magnetic Resonance
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Resin and Magnetic Nanoparticle-Based Free Radical Probes for Glycan Capture, Isolation, and Structural

Kimberly Fabijanczuk1, Kaylee Gaspar1, Nikunj Desai1

  • 1Department of Chemistry and Biochemistry and Center for Quantitative Obesity Research , Montclair State University , Montclair , New Jersey 07043 , United States.

Analytical Chemistry
|November 14, 2019
PubMed
Summary

We developed a solid-supported free radical probe (SS-FRAGS) for efficient glycan enrichment and characterization. This method enables unambiguous differentiation of complex glycan isomers using mass spectrometry.

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Area of Science:

  • Carbohydrate Chemistry
  • Analytical Chemistry
  • Biochemistry

Background:

  • Glycan analysis is crucial for understanding biological processes.
  • Existing methods for glycan enrichment and characterization face challenges in efficiency and isomer differentiation.
  • Solid supports and free radical activated glycan sequencing (FRAGS) offer complementary advantages.

Purpose of the Study:

  • To develop a multifunctional solid-supported free radical probe (SS-FRAGS) for enhanced glycan enrichment and characterization.
  • To enable unambiguous structural elucidation of glycans, including isobaric isomers.
  • To provide a robust platform for glycomics research.

Main Methods:

  • Development of SS-FRAGS probe incorporating solid support (thio-activated resin/magnetic nanoparticles), disulfide bond, pyridyl, hydrazine, and free radical precursor.
  • Selective capture and enrichment of free glycans via the hydrazine moiety.
  • Disulfide bond cleavage for glycan release using dithiothreitol.
  • Mass spectrometry-based detection utilizing the pyridyl group for fixed charge formation.
  • Collisional activation to induce free radical generation and systematic glycan fragmentation.
  • Development of a radical-driven glycan deconstruction diagram (R-DECON) for data interpretation.

Main Results:

  • SS-FRAGS successfully enriches and isolates glycans from complex mixtures.
  • The pyridyl group prevents glycan rearrangement during mass spectrometry analysis.
  • Free radical generation upon collisional activation leads to predictable fragmentation patterns.
  • The R-DECON diagram facilitates unambiguous differentiation of isobaric glycan isomers.
  • Demonstrated efficacy of SS-FRAGS in analyzing glycans from RNase-B.

Conclusions:

  • SS-FRAGS is a powerful tool for glycan enrichment, characterization, and isomer differentiation.
  • This method simplifies complex glycan analysis and advances glycomics research.
  • The developed R-DECON approach enhances structural elucidation capabilities.