Abstract
Transition metal-mediated arylation chemistry is emerging as a powerful tool for the selective modification of native peptides and proteins, providing new opportunities in the field of bioconjugation. This highlight paper will summarize recent methodologies for the regio- and chemoselective arylation of select proteinogenic side chains and backbone amide N–H bonds within unprotected peptides and proteins. The importance of the metal–ligand complex in achieving tunable selectivity and the inherent benefits of arylation as a mode of covalent protein modification will be highlighted.
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