Fast protein modification in the nanomolar concentration range using an oxalyl amide as latent thioester

Benoît Snella (1) , Benjamin Grain (1) , Jérôme Vicogne (1) , Frédéric Capet (2) , Birgit Wiltschi (3) , Oleg Melnyk (1) , Vangelis Agouridas (1)

1 CIIL - Centre d’Infection et d’Immunité de Lille - INSERM U 1019 - UMR 9017 - UMR 8204
2 UCCS - Unité de Catalyse et Chimie du Solide - UMR 8181
3 BOKU - Universität für Bodenkultur Wien = University of Natural Resources and Life [Vienne, Autriche]

We show that latent oxalyl thioester surrogates are a powerful means to modify peptides and proteins in highly dilute conditions in purified aqueous media or in mixtures as complex as cell lysates. Designed to be shelf-stable reagents, they can be activated on-demand for enabling ligation reactions down to peptide concentrations as low as a few hundreds nM at rates approaching 30 M-1 s-1 .

Mots clés: Latency; N; S-Acyl Shift Systems; Non-Native Ligation; Protein Modification; Thioester; Latency

Domaines: Chimie organique

Benoît Snella, Benjamin Grain, Jérôme Vicogne, Frédéric Capet, Birgit Wiltschi, et al.. Fast protein modification in the nanomolar concentration range using an oxalyl amide as latent thioester. Angewandte Chemie International Edition, 2022, 61 (29), pp.e202204992. ⟨10.1002/anie.202204992⟩. ⟨hal-03695080⟩