LAUSR

The chemical diversification of biomolecules set forth a significant area that constitutes an important intersection between chemistry and biology. Amino acids and peptides, are the fundamental building blocks of proteins, play an ubiquitous role in all living organisms. While significant efforts have been geared to the chemical modifications of amino acid residues, particularly the functionalization of reactive functional groups such as Lysine-NH2 and Cysteine –SH, the exploration of aromatic amino acid residues of Tryptophan, Tyrosine, Phenylalanine, and Histidine has been relatively limited. Therefore, this review highlights on the strategies for side chain functionalization of these four aromatic amino acids in peptides, with a focus on elucidating the underlying mechanisms. We have also illustrated the usage of these chemical modifications in the chemical and biological realm.