Selective N-terminal modification of peptides and proteins: Recent progresses and applications

Numerous strategies for linking desired chemical probes with target peptides and proteins have been developed and applied in the field of biological chemistry. Approaches for site-specific modification of native amino acid residues in test tubes and biological contexts represent novel biological tools for understanding the role of peptides and proteins. Selective N-terminal modification strategies have been broadly studied especially in the last 10 years, as N-terminal positions are typically solvent exposed and provide chemically distinct sites for many peptide and protein targets, making N terminus distinct from other functional groups. A growing number of chemical and enzymatic techniques have been developed to modify N-terminal amino acids, and those techniques have the potential in the fields of medicine, basic research and applied materials science. This review focuses on appraising modification methodologies with the potential for biological applications from the past 10 years. (C) 2021 Published by Elsevier B.V. on behalf of Chinese Chemical Society and Institute of Materia Medica, Chinese Academy of Medical Sciences.

Automated summary

Numerous strategies have been developed and applied in the field of biological chemistry to link desired chemical probes with target peptides and proteins. Site-specific modification of native amino acid residues provides novel biological tools for understanding the role of peptides and proteins. Selective N-terminal modification strategies, which have been extensively studied in the last decade, have the potential for applications in medicine, basic research, and applied materials science.