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Correction: Tyrosine bioconjugation – an emergent alternative
Peter A.
Szijj
,
Kristina A.
Kostadinova
,
Richard J.
Spears
and
Vijay
Chudasama
*
Department of Chemistry, University College London, London, UK. E-mail: v.chudasama@ucl.ac.uk
First published on 31st October 2022
Abstract
Correction for ‘Tyrosine bioconjugation – an emergent alternative’ by Peter A. Szijj et al., Org. Biomol. Chem., 2020, 18, 9018–9028, https://doi.org/10.1039/D0OB01912G.
The authors regret that there were some errors in the compound numbering shown in Scheme 7. The correct scheme is shown below.
 | ||
| Scheme 1 Enzyme-mediated strategies for tyrosine bioconjugation. (a) Strategies relying on the enzyme tyrosinase. The catechol generated via this enzyme can be O-alkylated or reacted with boronate esters. If oxidation is allowed to progress to the o-quinones, these can be reacted with bicyclononynes in a strain-promoted cycloaddition or with N or S nucleophiles. (b) Strategy relying on incorporation of unnatural tyrosine residues via the enzyme tubulin tyrosine ligase. | ||
In addition, in the paragraph starting ‘The o-quinones (e.g. compound 35) produced in the second step can be attacked by nucleophiles’, the sentence ‘Recently, the suitability of anilines and cyclic amines as nucleophiles was compared, with anilines (e.g. compound 28) exhibiting higher efficiency.51’ should read ‘Recently, the suitability of anilines and cyclic amines as nucleophiles was compared, with anilines (e.g. compound 38) exhibiting higher efficiency.51’
The Royal Society of Chemistry apologises for these errors and any consequent inconvenience to authors and readers.
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