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Molecular sieving on the surface of a protein provides protection without loss of activity

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Liu, Mi, Tirino, Pasquale, Radivojevic, Milos, Phillips, Daniel J., Gibson, Matthew I., Leroux, Jean-Christophe and Gauthier, Marc A. (2013) Molecular sieving on the surface of a protein provides protection without loss of activity. Advanced Functional Materials, Volume 23 (Number 16). pp. 2007-2015. doi:10.1002/adfm.201202227

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Official URL: http://dx.doi.org/10.1002/adfm.201202227

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Abstract

Tethering polymers to surfaces represents the cornerstone of a wide range of applications, including the stabilization of colloids/biomolecules and the preparation of functional coatings. Unfortunately, despite the prevalence of protein-tethered polymers in the pharmaceutical sector, the analysis of such polymer monolayers on a molecular level is difficult. In this work, simple 1H NMR spectroscopy and the catalytic properties of α-chymotrypsin are used to analyze the conformational/permeability properties of protein-bound monolayers of poly(oligoethyleneglycol monomethylether methacrylate) (pOEGMA), a biocompatible comb-polymer of interest in the biomedical field. By analyzing >100 distinct conjugates of α-chymotrypsin and pOEGMA, a detailed picture of the behavior of pOEGMA on the surface of a protein was obtained. Remarkably, control of polymer conformation and inter-penetration produced a thus far overlooked molecular sieving effect. The application of this effect for the “smart” PEGylation of proteins is portrayed, from which insight is provided for the design of other therapeutic bioconjugates and functional coatings with selective permeability properties.

Item Type: Journal Article
Divisions: Faculty of Science > Chemistry
Journal or Publication Title: Advanced Functional Materials
Publisher: Wiley - V C H Verlag GmbH & Co. KGaA
ISSN: 1616-301X
Official Date: 25 April 2013
Dates:
DateEvent
25 April 2013Published
15 November 2012Available
7 August 2012Submitted
Volume: Volume 23
Number: Number 16
Page Range: pp. 2007-2015
DOI: 10.1002/adfm.201202227
Status: Peer Reviewed
Publication Status: Published
Access rights to Published version: Restricted or Subscription Access

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