Metal?Catalyzed C(sp ² )?H Functionalization Processes of Phenylalanine? and Tyrosine?Containing Peptides

The site-selective chemical diversification of biomolecules constitutes an unmet challenge capital importance within medicinal chemistry and biology. functionalization otherwise unreactive C?H bonds holds great promise for reducing the reliance on existing functional groups, thereby streamlining syntheses. Over last years, a myriad peptide labelling techniques featuring metal-catalyzed reactions have been developed. Despite wealth reports in field, modification both phenylalanine (Phe) tyrosine (Tyr) compounds upon metal catalysis remain comparatively overlooked. This review highlights these promising tagging strategies, which generally occur through formation challenging 6-membered metallacycles enable late-stage peptides tailored fashion.