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Updated: Oct 22, 2026

Chemo-enzymatic Synthesis of N-glycans for Array Development and HIV Antibody Profiling
Published on: February 5, 2018
Programmable chemoenzymatic synthesis of a keratan sulfate N-glycan library for glycocode decoding
Kaixuan Wang1,2, Wenjing Ma1,3, Wei Zhang1
1State Key Laboratory of Chemical Biology, Carbohydrate-Based Drug Research Center, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai 201203, China.
Abstract:
Keratan sulfate (KS) is a unique and widely distributed glycosaminoglycans family implicated in diverse biological processes. KS features branched glycan architectures with diverse sialylation and sulfation patterns, encoding a vastly expanded chemical and biological space. The limited accessibility of well-defined structures has hindered precise investigations into the KS biological functions. Here we report a programmable chemoenzymatic platform for assembling a 106-membered library of KS N-glycans and their nonsulfated counterparts, featuring length-variable oligo-N-acetyllactosamine (LacNAc) extensions and encompassing diverse sulfation and sialylation patterns. The synthetic strategy integrates length-controlled iterative glycosylation to assemble versatile precursors, orthogonal deprotection for site-specific sulfation, and modular enzyme-driven diversification. Glycan microarray analysis of this comprehensive library reveals that glycan-protein recognition is governed by the interplay of sulfation and sialylation patterns, oligo-LacNAc chain length, and terminal epitope presentation, providing insight into the functional versatility of KS glycans.
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