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Rapid diazotransfer for selective lysine labelling.

作者信息

Calvert Susannah H, Pawlak Tomasz, Hessman Gary, McGouran Joanna F

机构信息

School of Chemistry, Trinity Biomedical Science Institute, Trinity College Dublin, D02 R590, Ireland.

SSPC, The SFI Research Centre for Pharmaceuticals, Ireland.

出版信息

Org Biomol Chem. 2024 Oct 9;22(39):7976-7981. doi: 10.1039/d4ob01094a.

DOI:10.1039/d4ob01094a
PMID:39283514
Abstract

Azide functionalization of protein and peptide lysine residues allows selective bioorthogonal labeling to introduce new, site selective functionaltiy into proteins. Optimised diazotransfer reactions under mild conditions allow aqueous diazotransfer to occur in just 20 min at pH 8.5 on amino acid, peptide and protein targets. In addition, conditons can be modified to selectively label a single lysine residue in both protein targets investigated. Finally, we demonstrate selective modification of proteins containing a single azidolysine using copper(I)-catalyzed triazole formation.

摘要

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