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Chemo-enzymatic Synthesis of N-glycans for Array Development and HIV Antibody Profiling

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Melanin Building Block as Scaffold for Dynamic Submicromolar Galectin Inhibitors.

Emanuele Carrella¹, Luciano Pirone², Rita Russo²

¹Department of Physics Ettore Pancini, University of Naples Federico II, Via Cinthia 4, 80126 Naples, Italy.

|April 13, 2026

Summary

This summary is machine-generated.

Researchers developed a novel multivalent ligand using a biocompatible eumelanin backbone to inhibit galectin-3. This promising approach offers a new strategy for developing selective galectin inhibitors for therapeutic applications.

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Area of Science:

Biochemistry
Polymer Chemistry
Glycobiology

Background:

Galectins are β-galactoside-binding proteins implicated in various biological functions and diseases.
Developing selective galectin inhibitors, particularly multivalent ligands on biocompatible backbones, is crucial for therapeutic applications.

Purpose of the Study:

To synthesize and characterize a novel multivalent ligand for galectin-3 using a eumelanin-based backbone.
To investigate the interaction between the synthesized ligand and galectin-3.

Main Methods:

Oxidative polymerization of 5,6-dihydroxyindole (DHI) to create a eumelanin backbone.
Nuclear magnetic resonance (NMR) spectroscopy for complete characterization.
UV-vis spectrometry, dynamic light scattering (DLS), isothermal titration calorimetry (ITC), and biolayer interferometry (BLI) to study protein-ligand interactions.

Main Results:

Successful synthesis and characterization of a submicromolar multivalent ligand of galectin-3.
Quantification of galectin-3-ligand binding affinity (K_D) using multiple biophysical techniques.
Proposal of a model for galectin-3-polymer interaction.

Conclusions:

Eumelanin-based multivalent ligands represent a promising platform for developing high-performance, selective galectin-3 inhibitors.
The developed ligand demonstrates potential for therapeutic applications targeting galectin-related diseases.
This study provides insights into protein-polymer interactions relevant to biomaterials and drug development.