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Programmable Chemoenzymatic Assembly of a Bisected and Core-Fucosylated N-Glycan Library Reveals Glycan-Binding Protein Specificity and Branch Preference

文献类型：期刊论文

作者Liu, Jialin3,4; Zhang, Wei2; Xu, Zhuojia4; Huang, Yi4; Ma, Wenjing4; Cheng, Xi1; Li, Tiehai2,4
刊名ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
出版日期2025-09-04
页码11
关键词Biomolecular recognition Carbohydrates Chemoenzymatic synthesis Core fucosylation N-glycans
DOI10.1002/anie.202514754
通讯作者Li, Tiehai(tiehaili@simm.ac.cn)
英文摘要Bisected and core-fucosylated N-glycans represent a distinct class of complex biomolecules that are implicated in diverse biological and pathological processes. The structural complexity and synthetic challenges of these glycans hinder comprehensive understanding of their biological functions due to limited access to well-defined samples. Despite advances in the complex N-glycan synthesis, the efficient preparation of bisected and core-fucosylated asymmetric N-glycans with various branches and terminal epitopes remains an unmet challenge. In this study, we report a streamlined divergent chemoenzymatic approach for the programmable synthesis of an asymmetric bisected and core-fucosylated N-glycan library, featuring bi-, tri-, and tetra-antennary structures with variable-length oligo-LacNAc extensions and various terminal epitopes. This methodology relies on protecting-group-controlled branch extension, glycosyltransferase intrinsic branch selectivity and glyco-epitope blocking effects, enabling the precise installment of each branch with unique epitopes. These structurally diverse N-glycans are printed as a microarray to comprehensively investigate structure-function relationships, revealing that glycan-binding protein specificities are mediated by distinct branching patterns, oligo-LacNAc chain length, and terminal epitope presentation. This work provides valuable insights into glycan-protein interactions and highlights the potential of our approach for advancing glycoscience and biomedical applications.
WOS关键词SIALIC ACID ; AFFINITY ; GLYCOSYLATION ; ACTIVATION ; OLIGOSACCHARIDE ; GLYCOPEPTIDES ; BIANTENNARY ; RECOGNITION ; GLYCOFORMS ; EXPRESSION
资助项目Shanghai Municipal Science and Technology Major Project
WOS研究方向Chemistry
语种英语
WOS记录号WOS:001563005200001
出版者WILEY-V C H VERLAG GMBH
源URL[http://119.78.100.183/handle/2S10ELR8/321390]  
专题中国科学院上海药物研究所
通讯作者Li, Tiehai
作者单位1.Shanghai Jiao Tong Univ, Inst Med Artificial Intelligence, Dept Pharmaceut & Artificial Intelligence Sci, Sch Med, Shanghai 200025, Peoples R China
2.Nanjing Univ Chinese Med, Sch Chinese Mat Med, Nanjing 210023, Peoples R China
3.Fudan Univ, Inst Biomed Sci, Shanghai 200032, Peoples R China
4.Chinese Acad Sci, Shanghai Inst Mat Med, State Key Lab Chem Biol, Shanghai 201203, Peoples R China
推荐引用方式
GB/T 7714		 Liu, Jialin,Zhang, Wei,Xu, Zhuojia,et al. Programmable Chemoenzymatic Assembly of a Bisected and Core-Fucosylated N-Glycan Library Reveals Glycan-Binding Protein Specificity and Branch Preference[J]. ANGEWANDTE CHEMIE-INTERNATIONAL EDITION,2025:11.
APA Liu, Jialin.,Zhang, Wei.,Xu, Zhuojia.,Huang, Yi.,Ma, Wenjing.,...&Li, Tiehai.(2025).Programmable Chemoenzymatic Assembly of a Bisected and Core-Fucosylated N-Glycan Library Reveals Glycan-Binding Protein Specificity and Branch Preference.ANGEWANDTE CHEMIE-INTERNATIONAL EDITION,11.
MLA Liu, Jialin,et al."Programmable Chemoenzymatic Assembly of a Bisected and Core-Fucosylated N-Glycan Library Reveals Glycan-Binding Protein Specificity and Branch Preference".ANGEWANDTE CHEMIE-INTERNATIONAL EDITION (2025):11.

入库方式： OAI收割

来源：上海药物研究所

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