Tryptophan-specific modification and diversification of peptides and proteins

Abstract

In spite of being the second-lowest abundant proteinogenic amino acid, approximately 90% of proteins contain at least one tryptophan residue. Hence, the chemoselective functionalization of tryptophan residue can provide access to site-selective bioconjugation of almost all known proteins. With the increase in the utility of bioconjugated proteins and peptides as drugs and therapeutic agents, the development of smart protocols to fabricate and modulate biomolecules has flourished. This review provides a comprehensive summary of the latest advances in tryptophan-specific modification and diversification of peptides and proteins that exhibit significant applications in proteomics, protein engineering, living cell imaging, drug discovery, etc. The article also highlights literature gaps and new opportunities for the sake of future innovation in the field.