Tyrosine-Triazolinedione Bioconjugation as Site-Selective Protein Modification Starting from RAFT-Derived Polymers
| Autor: | Filip Du Prez, Bruno G. De Geest, Stef Vandewalle, Ruben De Coen |
|---|---|
| Rok vydání: | 2017 |
| Předmět: |
Aqueous solution
Bioconjugation Polymers and Plastics biology Chemistry Organic Chemistry Chain transfer 02 engineering and technology Raft Electrophilic aromatic substitution 010402 general chemistry 021001 nanoscience & nanotechnology 01 natural sciences Combinatorial chemistry 0104 chemical sciences Inorganic Chemistry Polymerization Materials Chemistry biology.protein Moiety Bovine serum albumin 0210 nano-technology |
| Zdroj: | ACS Macro Letters. 6:1368-1372 |
| ISSN: | 2161-1653 |
| DOI: | 10.1021/acsmacrolett.7b00795 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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