ArticleOrganic & biomolecular chemistry2016
Chemoselective modifications for the traceless ligation of thioamide-containing peptides and proteins.
Article in Organic & biomolecular chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 15 citations in OpenAlex.
- Incorporating thioamides into proteins by native chemical ligation.Methods in enzymology · 2021Article
- Chemoenzymatic Semisynthesis of Proteins.Chemical reviews · 2020Review
- Biosynthesis and Chemical Applications of Thioamides.ACS chemical biology · 2019Review
- Synthesis and semisynthesis of selenopeptides and selenoproteins.Current opinion in chemical biology · 2018Review
- Site-Specific Incorporation of Selenocysteine Using an Expanded Genetic Code and Palladium-Mediated Chemical Deprotection.Journal of the American Chemical Society · 2018Article
- The effects of thioamide backbone substitution on protein stability: a study in α-helical, β-sheet, and polyproline II helical contexts.Chemical science · 2017Article
- Utilizing Selenocysteine for Expressed Protein Ligation and Bioconjugations.Journal of the American Chemical Society · 2017Article
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Authors and funding
3 authors at 3 institutions in 1 country.
Funding
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.
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