Chloromethyl-triazole: a new motif for site-selective pseudo-acylation of proteins† †Electronic supplementary information (ESI) available: Synthesis and characterisation of compounds 3b, 4b, and peptides Pep1–3. Peptide and protein alkylation procedures. See DOI: 10.1039/c6cc06801d. Primary data files can be found at http://dx.doi.org/10.7488/ds/1484 Click here for additional data file.
نویسندگان
چکیده
Rapid, 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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3-Mercaptopropionic acid-mediated synthesis of peptide and protein thioesters† †Electronic supplementary information (ESI) available: Experimental procedures for the production of 1, all model peptides and proteins and their reactions with MPA including HPLC, LC-MS and NMR characterisation of selected products. See DOI: 10.1039/b815888f Click here for additional data file.
Peptides and proteins fragment sequence-specifically in the presence of 3-mercaptopropionic acid to afford thioesters which can be used in native chemical ligation reactions.
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School of Chemistry, University of Bristol, B bris.ac.uk AstraZeneca, Alderley Park, Maccleseld, C AstraZeneca, Pepparedsleden 1, Mölndal, 4 † Electronic supplementary information ( and characterisation data for all compou 1438660. For ESI and crystallographic dat DOI: 10.1039/c6sc04466b ‡ These authors contributed equally. § Author to whom correspondence shou structures of 3b and Pd[(Sa,S)-L-...
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