Tyrosine Bioconjugation with Hypervalent Iodine

11 August 2022, Version 1
This content is a preprint and has not undergone peer review at the time of posting.

Abstract

Hypervalent iodine reagents have recently emerged as powerful tools for late-stage peptide and protein functionalization. Herein we report a tyrosine bioconjugation methodology for the introduction of hypervalent iodine onto biomolecules under physiological conditions. Tyrosine residues were engaged in a selective addition onto the alkynyl bond of ethynylbenziodoxolones (EBX), resulting in stable vinylbenziodoxolones (VBX) bioconjugates. The methodology was successfully applied to peptides and proteins and tolerated all other nucleophilic residues, with the exception of cysteine. The generated VBX were further functionalized by palladium-catalyzed cross-coupling and azide-alkyne cycloaddition reactions. The method could be successfully used to modify bioactive natural products and native streptavidin to enable thiol-mediated cellular uptake.

Keywords

Bioconjugation
Peptides
Hypervalent Iodine Reagents
Proteins
Late-Stage Functionalization
Tyrosine
Cellular Uptake
Streptavidin
Benziodoxolones

Supplementary materials

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Supplementary Information
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Experimental procedures, characterization data, microscopy images and copy of NMR spectra
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