Gauthier, Marc A.Ayer, MaximeKowal, JustynaWurm, Frederik R.Klok, Harm-Anton2011-12-162011-12-162011-12-16201110.1039/c0py00422ghttps://infoscience.epfl.ch/handle/20.500.14299/73959WOS:000291613700011The 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, alpha-oxo-aldehyde functionalized ATRP initiator that can be used for the preparation of a variety of alpha-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 alpha-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.Noncanonical Amino-AcidsCopper-Catalyzed AtrpBlock-CopolymersMethyl-MethacrylateConjugationPegylationStrategiesPeptideKetoneDesigntext::journal::journal article::research article