Proximity-driven, Regioselective Chemical Modification of Peptides and Proteins

Chemical methods to covalently modify recombinant peptides and proteins are becoming increasingly valuable as the development of biological therapeutics accelerates. Rapid advances in chemoselectivity have been achieved to modify desired proteogenic and non-proteogenic amino acids. However, regioselectivity, in which a specific amino acid can be modified in the presence of chemically identical residues, has been much more difficult to achieve. This mini-review focuses on recent advances in regioselective chemical modification of peptides and proteins utilizing microenvironment and/or proximity-driven effects to achieve selectivity.

Automated summary

As biological therapeutics continue to develop, chemical methods for modifying recombinant peptides and proteins are becoming more valuable. Recent advancements have been made in modifying specific amino acids, but achieving regioselectivity in the presence of chemically identical residues remains challenging. This mini-review explores the latest progress in regioselective chemical modification of peptides and proteins using microenvironment and/or proximity-driven effects for achieving selectivity.