Reference : Grafted block complex coacervate core micelles and their effect on protein adsorption on...
Scientific journals : Article
Engineering, computing & technology : Materials science & engineering
Physical, chemical, mathematical & earth Sciences : Chemistry
http://hdl.handle.net/2268/100225
Grafted block complex coacervate core micelles and their effect on protein adsorption on silica and polystyrene
English
Brzozowska, Agata M. [Wetsus, Centre of Excellence for Sustainable Water Technology, Leeuwarden, The Netherlands > > > >]
de Keizer, Arie [Wageningen University, The Netherlands > > Laboratory of Physical Chemistry and Colloid Science, > >]
Norde, Willem [University Medical Center Groningen and University of Groningen, The Netherlands > > > >]
Detrembleur, Christophe mailto [University of Liège (ULg) > Department of Chemistry > Center for Education and Research on Macromolecules (CERM) > >]
Cohen Stuart, Martien A. [Wageningen University, The Netherlands > > Laboratory of Physical Chemistry and Colloid Science > >]
Jul-2010
Colloid and Polymer Science
Springer Science
288
10/11
1081-1095
International
0303-402X
1435-1536
Heidelberg
Germany
[en] self-assembly in solution ; micelle ; stimuli responsive micelle
[en] We have studied the formation and the stability of grafted block complex coacervate core micelles (C3Ms) in solution and the influence of grafted block C3M coatings on the adsorption of the proteins beta-lactoglobulin, bovine serum albumin, and lysozyme. The C3Ms consist of a grafted block copolymer PAA(21)-b-PAPEO(14) (poly(acrylic acid)-b-poly(acrylate methoxy poly(ethylene oxide)), with a negatively charged PAA block and a neutral PAPEO block and a positively charged homopolymer P2MVPI (poly(N-methyl 2-vinyl pyridinium iodide). In solution, these C3Ms partly disintegrate at salt concentrations between 50 and 100 mM NaCl. Adsorption of C3Ms and proteins has been studied with fixed-angle optical reflectometry, at salt concentrations ranging from 1 to 100 mM NaCl. In comparison with the adsorption of PAA(21)-b-PAPEO(14) alone adsorption of C3Ms significantly increases the amount of PAA(21)-b-PAPEO(14) on the surface. This results in a higher surface density of PEO chains. The stability of the C3M coatings and their influence on protein adsorption are determined by the composition and the stability of the C3Ms in solution. A C3M-PAPEO(14)/P2MVPI(43) coating strongly suppresses the adsorption of all proteins on silica and polystyrene. The reduction of protein adsorption is the highest at 100 mM NaCl (> 90%). The adsorbed C3M-PAPEO(14)/P2MVPI(43) layer is partly removed from the surface upon exposure to an excess of beta-lactoglobulin solution, due to formation of soluble aggregates consisting of beta-lactoglobulin and P2MVPI(43). In contrast, C3M-PAPEO(14)/P2MVPI(228) which has a fivefold longer cationic block enhances adsorption of the negatively charged proteins on both surfaces at salt concentrations above 1 mM NaCl. A single PAA(21)-b-PAPEO(14) layer causes only a moderate reduction of protein adsorption.
Center for Education and Research on Macromolecules (CERM)
Politique Scientifique Fédérale (Belgique) = Belgian Federal Science Policy ; Fonds de la Recherche Scientifique (Communauté française de Belgique) - F.R.S.-FNRS
Researchers
http://hdl.handle.net/2268/100225
10.1007/s00396-010-2228-4
http://www.springerlink.com/content/84m44127tq347170/fulltext.pdf
The original publication is available at www.springerlink.com (open acces)

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