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Controlled Reversible N-Terminal Modification of Peptides and Proteins

文献类型：期刊论文

作者Lin, Zeng2,3,4; Liu, Bo3,4; Lu, Mengru2,3,4; Wang, Yongqin2,3,4; Ren, Xuelian1,4; Liu, Zhaoxi2,3,4; Luo, Caili4; Shi, Wei3; Zou, Xiangman3; Song, Xiaohan1,4
刊名JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
出版日期2024-08-15
卷号146期号:34页码:23752-23763
ISSN号0002-7863
DOI10.1021/jacs.4c04894
通讯作者Liu, Bo(boliu1984@hotmail.com) ; Huang, He(hhuang@simm.ac.cn) ; Huang, Wei(huangwei@simm.ac.cn)
英文摘要A reversible modification strategy enables a switchable cage/decage process of proteins with an array of applications for protein function research. However, general N-terminal selective reversible modification strategies which present site selectivity are specifically limited. Herein, we report a general reversible modification strategy compatible with 20 canonical amino acids at the N-terminal site by the palladium-catalyzed cinnamylation of native peptides and proteins under biologically relevant conditions. This approach broadens the substrate adaptability of N-terminal modification of proteins and shows a potential impact on the more challenging protein substrates such as antibodies. In the presence of 1,3-dimethylbarbituric acid, palladium-catalyzed deconjugation released native peptides and proteins efficiently. Harnessing the reversible nature of this protocol, practical applications were demonstrated by precise function modulation of antibodies and traceless enrichment of the protein-of-interest for proteomics analysis. This novel on/off strategy working on the N-terminus will provide new opportunities in chemical biology and medicinal research.
WOS关键词SITE-SPECIFIC PEGYLATION ; FUNCTIONALIZATION ; BIOCONJUGATION ; CYSTEINES ; CHEMISTRY ; RESIDUES ; CLEAVAGE ; TYROSINE ; DESIGN
资助项目Natural Science Foundation of China (NSFC)[82325045] ; Natural Science Foundation of China (NSFC)[92153301] ; Natural Science Foundation of China (NSFC)[82003574] ; Shanghai Sail Program[19YF1457100] ; Shanghai Sail Program[22YF1457400] ; Special Research Assistant Program (Chinese Academy of Sciences, CAS) ; Shanghai Municipal Science and Technology Major Project ; Hangzhou innovation and entrepreneurship leading team project[TD2020005] ; Lingang Laboratory[LG-QS-202206-03]
WOS研究方向Chemistry
语种英语
WOS记录号WOS:001292281300001
出版者AMER CHEMICAL SOC
源URL[http://119.78.100.183/handle/2S10ELR8/312797]  
专题新药研究国家重点实验室
通讯作者Liu, Bo; Huang, He; Huang, Wei
作者单位1.Chinese Acad Sci, Shanghai Inst Mat Med, State Key Lab Chem Biol, Shanghai 201203, Peoples R China
2.Univ Chinese Acad Sci, Beijing 100049, Peoples R China
3.Chinese Acad Sci, Shanghai Inst Mat Med, State Key Lab Drug Res, Shanghai 201203, Peoples R China
4.Hangzhou Inst Adv Study, Sch Pharmaceut Sci & Technol, Hangzhou 310024, Peoples R China
推荐引用方式
GB/T 7714		 Lin, Zeng,Liu, Bo,Lu, Mengru,et al. Controlled Reversible N-Terminal Modification of Peptides and Proteins[J]. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY,2024,146(34):23752-23763.
APA Lin, Zeng.,Liu, Bo.,Lu, Mengru.,Wang, Yongqin.,Ren, Xuelian.,...&Huang, Wei.(2024).Controlled Reversible N-Terminal Modification of Peptides and Proteins.JOURNAL OF THE AMERICAN CHEMICAL SOCIETY,146(34),23752-23763.
MLA Lin, Zeng,et al."Controlled Reversible N-Terminal Modification of Peptides and Proteins".JOURNAL OF THE AMERICAN CHEMICAL SOCIETY 146.34(2024):23752-23763.

入库方式： OAI收割

来源：上海药物研究所

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