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Tyrosine Conjugation Methods for Protein Labelling
Author(s) -
Alvarez Dorta Dimitri,
Deniaud David,
Mével Mathieu,
Gouin Sébastien G.
Publication year - 2020
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.202001992
Subject(s) - bioconjugation , labelling , biomolecule , conjugate , cysteine , chemistry , lysine , tyrosine , combinatorial chemistry , biochemistry , ligand (biochemistry) , fluorescence , amino acid , enzyme , physics , mathematical analysis , receptor , mathematics , quantum mechanics
Over the last two decades, the development of chemical biology and the need for more defined protein conjugates have fostered active research on new bioconjugation techniques. In particular, a wide range of biorthogonal labelling strategies have been reported to functionalise the phenol side chain of tyrosines (Tyr). Tyr occur at medium frequency and are partially buried at the protein surface, offering interesting opportunities for site‐selective labelling of the most reactive residues. Tyr‐targeting has proved effective for designing a wide range of important biomolecules including antibody–drug conjugates, fluorescent or radioactive protein probes, glycovaccines, protein aggregates, and PEG conjugates. Innovative methods have also been reported for site‐specific labelling with ligand‐directed anchors and for the specific affinity capture of proteins. This review will present and discuss these promising alternatives to the conventional labelling of the nucleophilic lysine and cysteine residues.