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AuthorVantourout, Julien C; Rao Adusumalli, Srinivasa; Knouse, Kyle W.; Flood, Dillon; Ramirez, Antonio; Muñoz Padial, Natalia; Israte, Alena; Maziarz, Katarzyna; deGruyter, Justine N.; Merchant, Rohan R.; Qiao, Jennifer X.; Schmidt, Michael A.; Deery, Michael J.; Eastgate, Martin D.; Dawson, Philip E.; Bernardes, Gonçalo J. L.; Baran, Phil S.
American Chemical Society
J. Am. Chem. Soc. 2020, 142, 41, 17236–17242
SponsorshipFinancial support for this work was provided by the Marie Skłodow-ska-Curie Global Fellowships (749359-EnanSET, N.M.P) within the European Union research and inno-vation framework programme (2014-2020)
This Communication reports the first general method for rapid, chemoselective, and modular functionalization of serine residues in native polypeptides, which uses a reagent platform based on the P(V) oxidation state. This redox-economical approach can be used to append nearly any kind of cargo onto serine, generating a stable, benign, and hydrophilic phosphorothioate linkage. The method tolerates all other known nucleophilic functional groups of naturally occurring proteinogenic amino acids. A variety of applications can be envisaged by this expansion of the toolbox of site-selective bioconjugation methods.