Templated chemistry offers the prospect of addressing specificity challenges occurring in bioconjugation reactions. Here, we show two peptide-templated amide-bond forming reactions that enable the concurrent labelling of two different membrane proteins with two different peptide nucleic acid () barcodes. The reaction system is based on the mutually selective coiled coil interaction between two thioester-linked -peptide conjugates and two cysteine peptides serving as genetically encoded peptide tags.
View Article and Find Full Text PDFRapid, site-selective modification of cysteine residues with chloromethyl-triazole derivatives generates pseudo-acyl sLys motifs, mimicking important post-translational modifications. Near-native biotinylation of peptide and protein substrates is shown to be site-selective and modified histone H4 retains functional activity.
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