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Recent developments in peptide ligation independent of amino acid side-chain functional group

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Abstract

Chemical synthesis of peptides and proteins has evolved into an indispensable tool for chemical biology. Peptide ligation is a straightforward technique for joining two short peptide fragments together via a native peptide bond to afford a larger natural peptide or protein. However, the junction sites are limited to several specific amino acids because most peptide ligations involve participation of the side-chain functional groups of the junction-site amino acids. To overcome such intrinsic limitations, “general” peptide ligations which do not rely on the side-chain functional group have been developed. This review summarized the recent developments in peptide ligations that are independent of side-chain functional group of ligation-junction-site amino acid.

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Acknowledgments

This work was supported by the National Natural Science Foundation of China (21462023), and the Natural Science Foundation of Jiangxi Province (20143ACB20007, 20153BCB23018).

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  1. Key Laboratory of Chemical Biology of Jiangxi Province, College of Chemistry & Chemical Engineering, Jiangxi Normal University, Nanchang, 330022, China

    Jinhua Yang & Junfeng Zhao

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Yang, J., Zhao, J. Recent developments in peptide ligation independent of amino acid side-chain functional group. Sci. China Chem. 61, 97–112 (2018). https://doi.org/10.1007/s11426-017-9056-5

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