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Antibodies, or immunoglobulins, are critical players in the immune system's arsenal against invading pathogens. Produced by B cells and plasma cells, their primary role is to detect and bind to specific antigens, molecules found on the surface of pathogens like bacteria or viruses. Beyond antigen recognition, antibodies perform several vital functions that contribute to immune defense.
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Antibodies, also known as immunoglobulins (Ig), are essential players of the adaptive immune system. These antigen-binding proteins are produced by B cells and make up 20 percent of the total blood plasma by weight. In mammals, antibodies fall into five different classes, which each elicits a different biological response upon antigen binding.
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Area of Science:

  • Carbohydrate Chemistry
  • Structural Biology
  • Biochemistry

Background:

  • Higher-order structures of biological macromolecules are critical for their function.
  • Peptide stapling enhances pharmacological properties by tuning conformational space.
  • The 3D structures of glycans are less understood than peptides and oligonucleotides, with limited success in modulating their structure for improved protein binding.

Purpose of the Study:

  • To develop a method for stapling β-(1,3)-glucans to control their conformation.
  • To mimic the naturally occurring triple helix structure of glucans.
  • To investigate the impact of glycan conformation on antibody binding.

Main Methods:

  • Automated glycan assembly for synthesizing stapled glycans.
  • Solid-phase peptide synthesis for linker construction and ring-closure.
  • Molecular dynamics simulations to analyze conformational changes.
  • Glycan microarray experiments to assess antibody binding affinity.

Main Results:

  • Successfully synthesized stapled β-(1,3)-glucans with tunable conformations.
  • Demonstrated that stapling alters the conformational space of glycans.
  • Observed significantly enhanced binding of stapled glycans to monoclonal antibodies compared to linear glycans.

Conclusions:

  • Controlling the conformational space of short oligosaccharides is achievable through stapling.
  • Stapled glycans exhibit improved binding affinity to antibodies.
  • This approach offers potential for developing novel synthetic glycans for drug and vaccine development.