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Tunable multivalent Fe(II)-based glycoassemblies as mimetics for native high-mannose glycans.

Emerson Hall1, Yu-Shien Sung2, Chad W Priest2

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Chemically defined multivalent glycan displays mimic high mannose glycans (HMGs) and inhibit lectin binding. These Fe(II) iminopyridine complexes offer tunable interactions for biological applications.

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Area of Science:

  • Carbohydrate Chemistry
  • Biophysical Chemistry
  • Glycobiology

Background:

  • High mannose glycans (HMGs) are crucial in biological processes like protein folding and immunity.
  • Lectins bind HMGs via multivalent interactions, involving multiple sugars and lectin binding sites.

Purpose of the Study:

  • To create chemically defined multivalent glycan displays using Fe(II) iminopyridine complexes.
  • To investigate the interaction of these displays with monomeric Griffithsin (mGRFT) as a model lectin.
  • To explore their potential as HMG mimetics and competitive inhibitors.

Main Methods:

  • Synthesis of Fe(II) iminopyridine complexes with controlled glycan valency, arm length, and mannose display.
  • Characterization of interactions using biolayer interferometry (BLI), isothermal titration calorimetry (ITC), and NMR spectroscopy.
  • Systematic molecular modifications to tune binding affinity.

Main Results:

  • Fe(II) glycan assemblies exhibited a >1000-fold range in binding affinity (KD) with mGRFT.
  • Binding affinity was tunable by altering saccharide tether length and the number of displayed sugars.
  • Demonstrated the ability of these assemblies to mimic native HMGs.

Conclusions:

  • Tunable Fe(II) glycan assemblies serve as effective mimetics for high mannose glycans.
  • These assemblies can function as competitive inhibitors of native glycan binding by lectins.
  • The study provides a platform for designing glycan-based molecules with controlled binding properties.