Arginine-specific protein modification using α-oxo-aldehyde functional polymers prepared by atom transfer radical polymerization

Marc A. Gauthier, Maxime Ayer, Justyna Kowal, Frederik R. Wurm, Harm Anton Klok*

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review

9 Citations (Scopus)

Abstract

The residue-specific modification of peptides and proteins is a powerful strategy for preparing biomolecular-synthetic polymer conjugates with advanced properties. This manuscript aims at expanding the present toolbox of residue-selective protein modification reactions and targets arginine, a residue for which selective polymer coupling chemistry has only recently been established. To this end, a protected, α-oxo-aldehyde functionalized ATRP initiator that can be used for the preparation of a variety of α-oxo-aldehyde functionalized polymethacrylates has been developed. Polymerization kinetics for four different methacrylate monomers have been investigated in detail and optimized conditions for the chain-end deprotection to reveal the α-oxo-aldehyde end-group have been elaborated. As a final proof of concept, the residue-specific modification of a model protein, chicken egg white lysozyme (HEWL), at arginine residues has been demonstrated.

Original languageEnglish
Pages (from-to)1490-1498
Number of pages9
JournalPolymer chemistry
Volume2
Issue number7
DOIs
Publication statusPublished - 1 Jul 2011
Externally publishedYes

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