Issue 17, 2022

α-Vinyl azide–cysteine click coupling reaction enabled bioorthogonal peptide/protein modification

Abstract

α-Alkyl and α-aryl vinyl azides were found to be able to couple with cysteine-derived alkyl thiols chemoselectively under mild conditions, providing the corresponding β-ketosulfides with simultaneous extrusion of N2 and ammonia. This reaction was developed into an effective chemical platform for peptide and protein modification, which is completely cysteine selective and highly bioorthogonal, that avoids the interference from other native residues. The in situ formed ketone group can react specifically with alkoxyamines or hydrazines and therefore can serve as a versatile handle for a second modification. The modification of bovine serum albumin (BSA) with a dansyl fluorescent probe and the labeling of the genetically encoded fluorescent protein YPet-ECFP with biotin have been accomplished successfully through this platform.

Graphical abstract: α-Vinyl azide–cysteine click coupling reaction enabled bioorthogonal peptide/protein modification

Supplementary files

Article information

Article type
Research Article
Submitted
07 מאי 2022
Accepted
07 יול 2022
First published
11 יול 2022

Org. Chem. Front., 2022,9, 4654-4662

α-Vinyl azide–cysteine click coupling reaction enabled bioorthogonal peptide/protein modification

M. Shen, Y. Wang, Y. Wang, Y. Zhou, J. Gu, X. Liu, J. Guo, M. Ouyang, L. Deng and H. Xu, Org. Chem. Front., 2022, 9, 4654 DOI: 10.1039/D2QO00736C

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