Xiao Xie, Patrick J Moon, Steven W M Crossley, Amanda J Bischoff, Dan He, Gen Li, Nam Dao, Angel Gonzalez-Valero, Audrey G Reeves, Jeffrey M McKenna, Susanna K Elledge, James A Wells, F Dean Toste, Christopher J Chang
Methods for selective covalent modification of amino acids on proteins can enable a diverse array of applications, spanning probes and modulators of protein function to proteomics1-3 . Owing to their high nucleophilicity, cysteine and lysine residues are the most common points of attachment for protein bioconjugation chemistry through acid-base reactivity3,4 . Here we report a redox-based strategy for bioconjugation of tryptophan, the rarest amino acid, using oxaziridine reagents that mimic oxidative cyclization reactions in indole-based alkaloid biosynthetic pathways to achieve highly efficient and specific tryptophan labelling...
March 6, 2024: Nature