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Updated: Sep 21, 2025
Synthesis and Bioconjugation of Thiol-Reactive Reagents for the Creation of Site-Selectively Modified Immunoconjugates
Published on: March 6, 2019
Tyrosine-Triazolinedione Bioconjugation as Site-Selective Protein Modification Starting from RAFT-Derived Polymers
Stef Vandewalle1, Ruben De Coen2, Bruno G De Geest2
1Polymer Chemistry Research Group, Centre of Macromolecular Chemistry (CMaC), Department of Organic and Macromolecular Chemistry, Ghent University, Krijgslaan 281 S4-bis, B-9000 Ghent, Belgium.
Abstract:
The electrophilic aromatic substitution (SEAr) reaction of triazolinediones (TADs) with the phenol moiety of tyrosine amino acid residues is a potent method for the site-selective formation of polymer-protein conjugates. Herein, using poly(N,N-dimethylacrylamide) (pDMA) and bovine serum albumin (BSA) as model reagents, the performance of this tyrosine-TAD bioconjugation in aqueous solutions is explored. At first, reversible addition-fragmentation chain transfer (RAFT) polymerization with a functional urazole, a precursor for TAD, chain transfer agent is used for the synthesis of a TAD end-functionalized pDMA. Eventually, the BSA ligation efficiency and selectivity of this polymer was evaluated in different aqueous solvent mixtures using SDS-PAGE and mass spectroscopy after trypsin digestion.
