Journal
CHEMISTRY-A EUROPEAN JOURNAL
Volume 26, Issue 63, Pages 14257-14269Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/chem.202001992
Keywords
bioconjugation; bioorthogonality; click chemistry; protein modification; tyrosine
Categories
Funding
- Centre National de la Recherche Scientifique (CNRS)
- Ministre de l'Enseignement Suprieur et de la Recherche in France
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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.
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