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Published on 08.01.2020
Recent years have seen an exponentially growing interest in chemical reactions enabling the selective modification of proteins and peptides. These advances are intimately linked to the development of methodologies for protein engineering with an atomic precision, for the generation of well-defined antibody-drug conjugates or on-demand probes to decipher biological processes. Such chemoselective reactions are also widely utilized for the total synthesis and semi-synthesis of proteins through chemical ligation of unprotected peptide fragments, an approach highly complementary to recombinant production. The chemical reactions implemented for both purposes share the same requirements: compatibility with dilute aqueous solution at physiological pH, and tolerance to the myriad functional groups commonly found in biomolecules. These remarkable features inspired the advent of biorthogonal reactions, which can be carried out in living systems.
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