Abstract
The chemical diversification of biomolecules set forth a significant area of research
that constitutes an important intersection between chemistry and biology. Amino acids
and peptides are the fundamental building blocks of proteins and play essential roles
in all living organisms. While significant efforts have been geared toward the chemical
modification of amino acid residues, particularly the functionalization of reactive
functional groups such as lysine NH2 and cysteine SH, the exploration of the aromatic amino acid residues of tryptophan,
tyrosine, phenylalanine, and histidine has been relatively limited. Therefore, this
review highlights strategies for the side-chain functionalization of these four aromatic
amino acids in peptides, with a focus on elucidating the underlying mechanisms. We
have also illustrated the use of these modifications in the chemical and biological
realm.
1 Introduction
2 Tryptophan Modifications
3 Tyrosine Modifications
4 Phenylalanine Modifications
5 Histidine Modifications
6 Perspectives and Future Outlook
Key words
aromatic amino acids - bioconjugation chemistry - C–H functionalization - macrocyclization
- photocatalysis - side-chain modifications - transition-metal catalysis
