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Updated: Oct 15, 2025

Chemically-blocked Antibody Microarray for Multiplexed High-throughput Profiling of Specific Protein Glycosylation in Complex Samples

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Published on: May 4, 2012

A Neoglycoprotein-Immobilized Fluorescent Magnetic Bead Suspension Multiplex Array for Galectin-Binding Studies.

Libo Zhang¹, Hai Yu¹, Yuanyuan Bai¹

¹Department of Chemistry, University of California, Davis, CA 95616, USA.

Molecules (Basel, Switzerland)

|October 23, 2021

Summary

This study presents a novel platform for analyzing carbohydrate-protein interactions using fluorescent magnetic beads. The developed suspension multiplex array enables rapid and flexible analysis of glycan-binding proteins (GBPs).

Keywords:

carbohydrate-protein conjugate galectin glycan-binding protein lectin multiplex assay

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Last Updated: Oct 15, 2025

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Published on: June 28, 2024

Area of Science:

Biochemistry
Analytical Chemistry
Immunology

Background:

Carbohydrate-protein conjugates are crucial in biological processes and clinical applications, including vaccines and diagnostic assays.
Understanding the specificities of glycan-binding proteins (GBPs) is essential for elucidating biological functions and developing targeted therapeutics.
Existing methods for analyzing glycan-GBP interactions can be limited in throughput and flexibility.

Purpose of the Study:

To develop a robust and flexible suspension multiplex array platform for high-throughput analysis of glycan-binding protein interactions.
To create a system for efficient chemoenzymatic synthesis of carbohydrates and their conjugation to proteins.
To enable rapid characterization of glycan-binding specificities of various proteins, including human galectins.

Main Methods:

Chemoenzymatic synthesis of diverse carbohydrate structures.
Production of carbohydrate-bovine serum albumin (glycan-BSA) conjugates utilizing a squarate linker.
Immobilization of neoglycoproteins onto carboxylate-coated fluorescent magnetic beads to form a suspension multiplex array.
Characterization of lectin and galectin binding profiles using the developed array.

Main Results:

A glycan-BSA-bead array was successfully generated, featuring 50 distinct glycan-BSA conjugates with controlled valency.
The binding profiles of six plant lectins and two human galectins (galectin-3 and galectin-8) were readily determined.
The platform demonstrated efficient and rapid analysis of glycan-GBP interactions, providing insights into multivalent binding properties.

Conclusions:

The neoglycoprotein-immobilized fluorescent magnetic bead suspension multiplex array is a powerful tool for rapid glycan-GBP interaction analysis.
This platform offers a robust and flexible approach for studying glycan recognition mechanisms.
The findings contribute to a better understanding of human galectin multivalent binding properties and have broad application potential.