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Surface Ligand Density Switches Glycovesicles between Monomeric and Multimeric Lectin Recognition.

Shivender Yadav¹, Kottari Naresh^1,2, Narayanaswamy Jayaraman¹

¹Department of Organic Chemistry, Indian Institute of Science, Bangalore, 560012, India.

Chembiochem : a European Journal of Chemical Biology

|September 14, 2020

Summary

Synthetic glycovesicles mimic cell surfaces to control lectin interactions. Ligand density on these vesicles determines if lectin binding forms a crosslinked complex or a soluble one, offering insights into cellular recognition.

Keywords:

carbohydrates cell-surface mimics lectins polydiacetylene polymers vesicles

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Bioinformatics Resources for the Study of Glycan-Mediated Protein Interactions

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Published on: January 20, 2022

Area of Science:

Biochemistry and Molecular Biology
Supramolecular Chemistry
Cellular Biology

Background:

Carbohydrate-protein interactions are fundamental to cellular recognition processes.
Understanding lectin-carbohydrate binding is crucial for deciphering cell surface events.
Existing models often lack the dynamic control seen in biological systems.

Purpose of the Study:

To develop synthetic cell-surface mimics (glycovesicles) for studying lectin recognition.
To investigate how ligand density on artificial surfaces influences lectin binding behavior.
To demonstrate the switchable nature of lectin interactions based on surface presentation.

Main Methods:

Preparation of covalent glycovesicles using diacetylene monomers via photo-polymerization.
Varying the density of embedded carbohydrate ligands on the vesicle surfaces.
Assessing lectin binding modes (multimeric vs. monomeric) as a function of ligand density.
Quantification of binding affinity using ligand-displacement assays to determine dissociation constants.

Main Results:

Sparsely ligated glycovesicles promoted lectin-mediated crosslinking, forming dense multimeric complexes.
Densely ligated or fully covered glycovesicles induced lectin interaction leading to soluble monomeric complexes.
Interactions were characterized by nanomolar dissociation constants, indicating high affinity.
A clear switch between multimeric and monomeric binding states was observed with changing ligand density.

Conclusions:

Ligand presentation density on synthetic surfaces critically controls lectin binding outcomes.
Glycovesicles serve as effective cell-surface mimics to study dynamic recognition events.
Findings provide a framework for understanding ligand density-dependent interactions at the cell surface.