Efficient Chemical Synthesis and Folding of Mirror-Image Tropomyosin Receptor Kinase A Using the Strategy of Removable Glycosylation Modification

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外文摘要：The strategy of removable glycosylation modification was used to overcome the low-efficiency problem encountered in the chemical synthesis of the mirror-image D-version of the immunoglobulin(Ig)-like domain of tropomyosin receptor kinase A(DIgCTrkA),a protein molecule needed for mirror-image screening of D-peptide ligands targeting this cell membrane receptor.It was found that O-linked-β-N-acetyl-D-glucosamine(O-GIcNAc)modification at DSer312,or DSer320 can significantly improve the efficiency of DIgCTrkA synthesis and folding,while O-GIcNAc modification at DSer330 showed barely any improvement.This study provides a new example demonstrating the power of the removable glycosylation modification strategy in the chemical synthesis and folding of diffi-cult-to-obtain proteins.It also presents evidence that removable glycosylation modification at different sites would significantly affect the efficiency of protein folding promoted by this strategy.

外文关键词：

Chemical protein synthesisRemovable glycosylation modificationSynthetic methodsProtein foldingD-protein

作者：

Tongyue Wang、Weiwei Shi、Guo-Chao Chu、Yi-Ming Li

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作者单位：

Ministry of Education Key Laboratory of Bioorganic Phosphorus Chemistry and Chemical Biology,Department of Chemistry,Tsinghua University,Beijing 100084,China

School of Food and Biological Engineering,Engineering Research Center of Bio-process,Ministry of Education,Key Laboratory of Animal Source of Anhui Province,Hefei University of Technology,Hefei,Anhui 230009,China

出版年：

2024

DOI：

10.1002/cjoc.202400381

中国化学(英文版)

中国化学会上海有机化学研究所

中国化学(英文版)

CSTPCD

影响因子：0.848

ISSN：1001-604X

年,卷(期)：2024.42(19)