ABSTRACT Bioconjugation chemistry is an important tool for studying proteins, developing pharmaceutical agents, and for many other applications. Conventional methods for protein functionalization rely on chemoselective reactions but often have poor regioselectivity. Peptide tags facilitating site‐selective chemical covalent modification of proteins are of great value in the synthesis of protein conjugates. Ideally, a protein would only have to be minimally mutated prior to chemical modification to avoid interfering with native protein folding, trafficking, and function. This short review summarizes the advances in the developments and applications of peptide tags for covalent modifications that proceed without enzymatic assistance.
Møller et al. (Sun,) studied this question.