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Tyrosine conjugation methods for protein labelling

Abstract : 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 functionalize 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 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.
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https://www.hal.inserm.fr/inserm-02877776
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Submitted on : Monday, November 16, 2020 - 11:28:37 AM
Last modification on : Monday, November 16, 2020 - 3:51:25 PM
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Dimitri Alvarez Dorta, David Deniaud, Mathieu Mével, Sébastien Gouin. Tyrosine conjugation methods for protein labelling. Chemistry - A European Journal, Wiley-VCH Verlag, 2020, Online ahead of print. ⟨10.1002/chem.202001992⟩. ⟨inserm-02877776⟩

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