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 397000
Title Reduction of protein adsorption on silica and polysulfone surfaces coated with complex coacervate core micelles with poly(vinyl alcohol) as a neutral brush forming block
Author(s) Brzozowska, A.M.; Zhang, Q.; Keizer, A. de; Norde, W.; Cohen Stuart, M.A.
Source Colloids and Surfaces. A: Physicochemical and Engineering Aspects 368 (2010)1-3. - ISSN 0927-7757 - p. 96 - 104.
DOI https://doi.org/10.1016/j.colsurfa.2010.07.023
Department(s) Physical Chemistry and Colloid Science
WIMEK
Publication type Refereed Article in a scientific journal
Publication year 2010
Keyword(s) bovine serum-albumin - polyelectrolyte multilayers - ultrafiltration membranes - poly(ethylene glycol) - polyvinyl pyridine - aqueous-solution - assembled monolayers - aquatic environment - organic pollutants - polymeric micelles
Abstract We have studied the formation and stability of complex coacervate core micelles (C3Ms) in solution, and the influence of C3M coatings on the adsorption of the proteins ß-lactoglobulin (ß-lac), bovine serum albumin (BSA), and lysozyme (Lsz) on silica and polysulfone surfaces. The C3Ms consist of a block copolymer PAA50-65-b-PVA445 (poly(acrylic acid)-b-poly(vinyl alcohol)), with a neutral PVA block, and the positively charged homopolymers: P2MVPI (poly(N-methyl 2-vinyl pyridinium iodide), or PAH·HCl (poly(allylamine hydrochloride)). In solution at pH 7 these micelles disintegrate if the salt concentration exceeds 100 mM NaCl. Adsorption of C3Ms and proteins was studied by fixed angle optical reflectometry at salt concentrations ranging from 1 to 50 mM NaCl. C3M consisting of PAH·HCl strongly suppresses protein adsorption on silica, also at low salt concentration. However, at high salt concentrations it enhances adsorption of BSA on hydrophobic polysulfone, probably due to the formation of complexes between BSA and PAH·HCl. Much smaller reduction of protein adsorption on silica and polysulfone was obtained by C3Ms consisting of P2MVPI.. In this case the effectiveness of the coating strongly depends on the type of protein. On polysulfone at 50 mM NaCl we have observed only reduction of Lsz adsorption whereas adsorption of the negatively charged proteins is enhanced rather than reduced by the coating. We relate the results obtained for C3M with P2MVPI to the low density of the PVA chains on the surfaces, partial segregation of polymer chains within coacervate layer, and penetration of the adsorbed layer by the proteins.
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