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Issue 39, 2011
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Interaction strength between proteins and polyelectrolyte brushes: a small angle X-ray scattering study

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Abstract

We present an investigation of β-lactoglobulin adsorption onto spherical polyelectrolyte brushes (SPBs) by small angle X-ray scattering (SAXS). The SPB consists of a polystyrene core onto which long chains of poly(styrene sulfonate) are grafted. The amount and the distribution of proteins adsorbed in the brush layer at low ionic strength can be derived from SAXS. The analysis of the SAXS data reveals additionally that some of the protein molecules form aggregates of about six monomers in the adsorbed state. Furthermore, the position and the amount of slightly bound protein can be detected by the combination of the SAXS results and the SPB loading after extensive ultrafiltration. The total amount of adsorbed protein is compared to data derived from isothermal titration calorimetry. The comparison of both sets of data demonstrates that the protein molecules in the inner layers of the spherical polyelectrolyte brush are firmly bound. Proteins located in the outer layers are only weakly bound and can be washed out by prolonged ultrafiltration.

Graphical abstract: Interaction strength between proteins and polyelectrolyte brushes: a small angle X-ray scattering study

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Publication details

The article was received on 08 Mar 2011, accepted on 09 Aug 2011 and first published on 05 Sep 2011


Article type: Paper
DOI: 10.1039/C1CP20663J
Citation: Phys. Chem. Chem. Phys., 2011,13, 17599-17605
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    Interaction strength between proteins and polyelectrolyte brushes: a small angle X-ray scattering study

    K. Henzler, B. Haupt, S. Rosenfeldt, L. Harnau, T. Narayanan and M. Ballauff, Phys. Chem. Chem. Phys., 2011, 13, 17599
    DOI: 10.1039/C1CP20663J

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