Suchergebnisse

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. ; Financial 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)