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Issue 26, 2016
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Chemoselective modifications for the traceless ligation of thioamide-containing peptides and proteins

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Abstract

Thioamides are single-atom substitutions of canonical amide bonds, and have been proven to be versatile and minimally perturbing probes in protein folding studies. Previously, our group showed that thioamides can be incorporated into proteins by native chemical ligation (NCL) with Cys as a ligation handle. In this study, we report the expansion of this strategy into non-Cys ligation sites, utilizing radical initiated desulfurization to “erase” the side chain thiol after ligation. The reaction exhibited high chemoselectivity against thioamides, which can be further enhanced with thioacetamide as a sacrificial scavenger. As a proof-of-concept example, we demonstrated the incorporation of a thioamide probe into a 56 amino acid protein, the B1 domain of Protein G (GB1). Finally, we showed that the method can be extended to β-thiol amino acid analogs and selenocysteine.

Graphical abstract: Chemoselective modifications for the traceless ligation of thioamide-containing peptides and proteins

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Publication details

The article was received on 11 May 2016, accepted on 26 May 2016 and first published on 06 Jun 2016


Article type: Paper
DOI: 10.1039/C6OB01020B
Org. Biomol. Chem., 2016,14, 6262-6269

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    Chemoselective modifications for the traceless ligation of thioamide-containing peptides and proteins

    Y. J. Wang, D. M. Szantai-Kis and E. J. Petersson, Org. Biomol. Chem., 2016, 14, 6262
    DOI: 10.1039/C6OB01020B

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