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Issue 35, 2017
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Selective lysine modification of native peptides via aza-Michael addition

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Abstract

A series of vinylsulfonamides were synthesized and screened for site-selective modification of the ε-amino group of lysine-bearing free α-amine residues. N-Methyl-N-phenylethenesulfonamide has emerged as an applicable reagent and has been developed for efficient and highly selective modification of the lysine residue of native peptides in the presence of a free N-terminus via aza-Michael addition. We demonstrated that functional N-phenylvinylsulfonamide derivatives with a fluorescent moiety or drug could also be conjugated to the lysine residue of octreotide and insulin with high specificity, without modifying the N-terminus. Our method provides a promising strategy for site-selective lysine functionalization in native peptides with a free N-terminus.

Graphical abstract: Selective lysine modification of native peptides via aza-Michael addition

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Supplementary files

Article information


Submitted
27 Jul 2017
Accepted
21 Aug 2017
First published
22 Aug 2017

This article is Open Access

Org. Biomol. Chem., 2017,15, 7339-7345
Article type
Paper

Selective lysine modification of native peptides via aza-Michael addition

H. Chen, R. Huang, Z. Li, W. Zhu, J. Chen, Y. Zhan and B. Jiang, Org. Biomol. Chem., 2017, 15, 7339
DOI: 10.1039/C7OB01866E

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