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Metal‐Catalyzed C(sp 2 )−H Functionalization Processes of Phenylalanine‐ and Tyrosine‐Containing Peptides
Author(s) -
Correa Arkaitz
Publication year - 2021
Publication title -
european journal of inorganic chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.667
H-Index - 136
eISSN - 1099-0682
pISSN - 1434-1948
DOI - 10.1002/ejic.202100374
Subject(s) - chemistry , surface modification , biomolecule , catalysis , tyrosine , phenylalanine , combinatorial chemistry , peptide , bioconjugation , chemical modification , organic chemistry , amino acid , biochemistry
The site‐selective chemical diversification of biomolecules constitutes an unmet challenge of capital importance within medicinal chemistry and chemical biology. The functionalization of otherwise unreactive C−H bonds holds great promise for reducing the reliance on existing functional groups, thereby streamlining chemical syntheses. Over the last years, a myriad of peptide labelling techniques featuring metal‐catalyzed C−H functionalization reactions have been developed. Despite the wealth of reports in the field, the site‐selective modification of both phenylalanine (Phe) and tyrosine (Tyr) compounds upon metal catalysis remain comparatively overlooked. This review highlights these promising tagging strategies, which generally occur through the formation of challenging 6‐membered metallacycles and enable the late‐stage diversification of peptides in a tailored fashion.