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

文献情報

出版日 2011-03-15

DOI 10.1039/C0PY00422G

インパクトファクター 5.582

著者

Maxime Ayer, Justyna Kowal, Frederik R. Wurm, Harm-Anton Klok

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要旨

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.

掲載誌

Polymer Chemistry

CiteScore: 8.6

自己引用率: 7.3%

年間論文数: 457

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

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