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Issue 7, 2011
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Arginine-specific protein modification using α-oxo-aldehyde functional polymers prepared by atom transfer radical polymerization

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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.

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

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Article information


Submitted
27 Dec 2010
Accepted
22 Feb 2011
First published
15 Mar 2011

Polym. Chem., 2011,2, 1490-1498
Article type
Paper

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

M. A. Gauthier, M. Ayer, J. Kowal, F. R. Wurm and H. Klok, Polym. Chem., 2011, 2, 1490
DOI: 10.1039/C0PY00422G

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