4.7 Article

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

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POLYMER CHEMISTRY
卷 2, 期 7, 页码 1490-1498

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ROYAL SOC CHEMISTRY
DOI: 10.1039/c0py00422g

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  1. NCCR Nanoscale Science, the Fonds Quebecois de la Recherche sur la Nature et les Technologies (Quebec, Canada)
  2. Alexander von Humboldt-Foundation

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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, 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.

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