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Precision dendritic-supramolecular glycan assemblies for probing multivalent lectin interactions.

Tanvi M Bhide1, Garrett J Musil1, Wade Shipley2

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Researchers developed novel glycan nanoassemblies by combining dendritic structures with metallosupramolecular frameworks. These new assemblies show enhanced binding affinity to lectins, offering a promising tool for studying glycan-protein interactions.

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Area of Science:

  • Carbohydrate Chemistry
  • Supramolecular Chemistry
  • Nanotechnology

Background:

  • Multivalent glycan-protein interactions are crucial in biological processes like cell signaling and immunity.
  • Developing precisely controlled glycan nanoassemblies is key for studying these interactions but remains a synthetic challenge.
  • Existing synthetic glyconanomaterials show promise but lack architectural control.

Purpose of the Study:

  • To create a new method for synthesizing molecular glycan nanoassemblies with precise architecture.
  • To integrate dense dendritic functionalization with preorganized metallosupramolecular frameworks.
  • To develop enhanced tools for probing and modulating glycan-protein interactions.

Main Methods:

  • Synthesized Fe(II)-anchored superassemblies with varying peripheral mannoside densities (24, 36, 72).
  • Characterized the glycan nanoassemblies using spectroscopic, microscopic, and light scattering techniques.
  • Evaluated lectin binding affinity using isothermal titration calorimetry (ITC).

Main Results:

  • Successfully prepared and characterized glycan nanoassemblies with controlled architectures.
  • Demonstrated strong binding of the assemblies to lectins Concanavalin A (Con A) and Griffithsin (GRFT).
  • The 72-mannoside assembly exhibited low nanomolar binding affinity (Kd = 28 ± 4 nM for Con A; 12 ± 1 nM for GRFT).

Conclusions:

  • Integrating dendritic architectures with rigid metallosupramolecular cores enhances lectin recognition.
  • The developed hybrid glycoassemblies provide a new framework for probing glycan-protein interactions.
  • These findings offer insights into designing advanced glycoassemblies for biomedical applications.