Staff Publications

Staff Publications

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    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

    Full text documents are added when available. The database is updated daily and currently holds about 240,000 items, of which 72,000 in open access.

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Record number 364778
Title Self-consistent field theory of protein adsorption in a non-Gaussian polyelectrolyte brush
Author(s) Biesheuvel, P.M.; Leermakers, F.A.M.; Stuart, M.A.C.
Source Physical Review. E, Statistical nonlinear, and soft matter physics 73 (2006)1. - ISSN 1539-3755 - 9 p.
Department(s) Physical Chemistry and Colloid Science
Publication type Refereed Article in a scientific journal
Publication year 2006
Keyword(s) including charge regulation - electrical double-layer - grafted polymer brush - finite extensibility - free-energy - model - sedimentation - equilibrium - interfaces - equation
Abstract To describe adsorption of globular protein molecules in a polyelectrolyte brush we use the strong-stretching approximation of the Edwards self-consistent field equation, combined with corrections for a non-Gaussian brush. To describe chemical potentials in this mixture of (globular) species of widely varying sizes (ions, brush polyelectrolyte segments, globular protein molecules), we use the Boublik-Mansoori-Carnahan-Starling-Leland equation of state derived for polydisperse mixtures of spherical particles. The polyelectrolyte chain is described in this approach as a string of beads with the beads of a size related to the chain diameter. We use the one-dimensional Poisson equation to describe the electrostatic field and include the ionizable character of both the brush polyions and the protein molecules. This model explains the experimental observation of high amounts of protein adsorption in a polyacid brush for pH values above the isoelectric point of the protein as being due to charge reversal of the protein molecules upon entry in the brush. We find a distinct minimum in protein concentration near the edge of the brush. With increasing pH this barrier to protein transfer becomes larger, but much less so when we increase the ionic strength, a difference that might relate to an experimentally observed difference in the protein release rate in these two cases. A free energy analysis shows that the release of small ions from the brush and the increase of brush ionization are the two driving forces for protein adsorption in a like-charged brush
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