Abstract
Carbohydrate-protein conjugates have diverse applications. They have been used clinically as vaccines against bacterial infection and have been developed for high-throughput assays to elucidate the ligand specificities of glycan-binding proteins (GBPs) and antibodies. Here, we report an effective process that combines highly efficient chemoenzymatic synthesis of carbohydrates, production of carbohydrate-bovine serum albumin (glycan-BSA) conjugates using a squarate linker, and convenient immobilization of the resulting neoglycoproteins on carboxylate-coated fluorescent magnetic beads for the development of a suspension multiplex array platform. A glycan-BSA-bead array containing BSA and 50 glycan-BSA conjugates with tuned glycan valency was generated. The binding profiles of six plant lectins with binding preference towards Gal and/or GalNAc, as well as human galectin-3 and galectin-8, were readily obtained. Our results provide useful information to understand the multivalent glycan-binding properties of human galectins. The neoglycoprotein-immobilized fluorescent magnetic bead suspension multiplex array is a robust and flexible platform for rapid analysis of glycan and GBP interactions and will find broad applications.
Highlights
IntroductionThe related studies have attracted increasing interest for both basic and clinical research purposes
(3), glycans terminated with GlcNAc, Gal, GalNAc at the non-reducing end that we synthesized
We found that a co-solvent containing a 1:1 ratio of 100 mM NaHCO3 and ethanol at pH 9.0 and a diethyl squarate:glycan molar concentration ratio of 2.5:1 were efficient conditions for the formation of the desired glycan squarate monoamide
Summary
The related studies have attracted increasing interest for both basic and clinical research purposes
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