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Peer-reviewedCC BY-NC-ND 4.0Proceedings of the National Academy of Sciences of the United States of America

Programmable chemoenzymatic synthesis of a keratan sulfate N-glycan library for glycocode decoding

  • Kaixuan Wang1,2
  • Wenjing Ma1,3
  • Wei Zhang1
  • Tianhui Hao1,4
  • Mengjia Zhang5
  • Wentao Li5
  • Wei Zhao2
  • Zhuojia Xu1
  • Tiehai Li1,4
5 affiliations
  1. 1State Key Laboratory of Chemical Biology, Carbohydrate-Based Drug Research Center, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai 201203, China
  2. 2Qingdao Central Hospital, National Health Commission Key Laboratory of Cardiopulmonary Rehabilitation and Functional Recovery, School of Medicine, University of Health and Rehabilitation Sciences, Qingdao 266113, China
  3. 3School of Pharmacy, Xi’an Jiaotong University, Xi’an 710061, China
  4. 4University of Chinese Academy of Sciences, Beijing 100049, China
  5. 5College of Veterinary Medicine, Huazhong Agricultural University, Wuhan 430070, China
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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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Cite

BibTeXRIS
BibTeX
@article{wang2026programmable,
  title = {{Programmable chemoenzymatic synthesis of a keratan sulfate N-glycan library for glycocode decoding}},
  author = {Kaixuan Wang and Wenjing Ma and Wei Zhang and Tianhui Hao and Mengjia Zhang and Wentao Li and Wei Zhao and Zhuojia Xu and Tiehai Li},
  journal = {Proceedings of the National Academy of Sciences of the United States of America},
  year = {2026},
  month = oct,
  doi = {10.1073/pnas.2621414123},
  url = {https://doi.org/10.1073/pnas.2621414123},
  note = {CC BY-NC-ND 4.0},
}
RIS
TY  - JOUR
TI  - Programmable chemoenzymatic synthesis of a keratan sulfate N-glycan library for glycocode decoding
AU  - Kaixuan Wang
AU  - Wenjing Ma
AU  - Wei Zhang
AU  - Tianhui Hao
AU  - Mengjia Zhang
AU  - Wentao Li
AU  - Wei Zhao
AU  - Zhuojia Xu
AU  - Tiehai Li
PY  - 2026
DA  - 2026/10/20
JO  - Proceedings of the National Academy of Sciences of the United States of America
DO  - 10.1073/pnas.2621414123
UR  - https://doi.org/10.1073/pnas.2621414123
AB  - 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.
SN  - 0027-8424
SN  - 1091-6490
ER  -