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    Arginine-Specific Modification of Proteins with Polyethylene Glycol
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    École Polytechnique Fédérale de Lausanne (EPFL), Institut des Matériaux and Institut des Sciences et Ingénierie Chimiques, Laboratoire des Polymères, Bâtiment MXD, Station 12, CH-1015 Lausanne, Switzerland
    * To whom correspondence should be addressed. E-mail: [email protected]
    †Current address: Swiss Federal Institute of Technology Zürich (ETHZ), Department of Chemistry and Applied Biosciences, Institute of Pharmaceutical Sciences, Drug Formulation and Delivery, Wolfgang-Pauli Str. 10, HCl J 396.4, 8093 Zürich, Switzerland.
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    Biomacromolecules

    Cite this: Biomacromolecules 2011, 12, 2, 482–493
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    https://doi.org/10.1021/bm101272g
    Published December 23, 2010
    Copyright © 2010 American Chemical Society
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    Abstract

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    In this study, the residue-selective modification of proteins with polymers at arginine residues is reported. The difficulty in modifying arginine residues lies in the fact that they are less reactive than lysine residues. Consequently, typical chemo-selective reactions which employ “kinetic” selectivity (active esters, Michael addition, etc.) cannot be used to target these residues. The chemistry exploited herein relies on “thermodynamic” selectivity to achieve selective modification of arginine residues. ω-Methoxy poly(ethylene glycol) bearing an α-oxo-aldehyde group was synthesized and used to demonstrate the selective modification of lysozyme at arginine residues. In addition, the optimization of reaction conditions for coupling as well as the stability of the formed adduct toward dilution, toward a nucleophilic buffer, and toward acidification are reported. It was concluded that this approach is a convenient, mild, selective, and catalyst-free method for protein modification.

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    Supplementary synthetic protocols and characterization of compounds (NMR and MALDI TOF spectra). Kinetics, raw chromatograms, and mass spectra for model reactions of methylglyoxal with N-acetyl amino acids. Raw chromatograms for reaction of 6−9 with HEWL. MS spectra of tryptic digest of conjugates. This material is available free of charge via the Internet at http://pubs.acs.org.

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    Biomacromolecules

    Cite this: Biomacromolecules 2011, 12, 2, 482–493
    Click to copy citationCitation copied!
    https://doi.org/10.1021/bm101272g
    Published December 23, 2010
    Copyright © 2010 American Chemical Society
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