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Grafted ionomer complexes and their effect on protein adsorption on silica and polysulfone surfaces

We have studied the formation and the stability of ionomer complexes from grafted copolymers (GICs) in solution and the influence of GIC coatings on the adsorption of the proteins β-lactoglobulin (β-lac), bovine serum albumin (BSA), and lysozyme (Lsz) on silica and polysulfone. The GICs consist of t...

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Autores principales: Brzozowska, Agata M., de Keizer, Arie, Detrembleur, Christophe, Cohen Stuart, Martien A., Norde, Willem
Formato: Texto
Lenguaje:English
Publicado: Springer-Verlag 2010
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2974926/
https://www.ncbi.nlm.nih.gov/pubmed/21125002
http://dx.doi.org/10.1007/s00396-010-2295-6
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author Brzozowska, Agata M.
de Keizer, Arie
Detrembleur, Christophe
Cohen Stuart, Martien A.
Norde, Willem
author_facet Brzozowska, Agata M.
de Keizer, Arie
Detrembleur, Christophe
Cohen Stuart, Martien A.
Norde, Willem
author_sort Brzozowska, Agata M.
collection PubMed
description We have studied the formation and the stability of ionomer complexes from grafted copolymers (GICs) in solution and the influence of GIC coatings on the adsorption of the proteins β-lactoglobulin (β-lac), bovine serum albumin (BSA), and lysozyme (Lsz) on silica and polysulfone. The GICs consist of the grafted copolymer PAA(28)-co-PAPEO(22) {poly(acrylic acid)-co-poly[acrylate methoxy poly(ethylene oxide)]} with negatively charged AA and neutral APEO groups, and the positively charged homopolymers: P2MVPI(43) [poly(N-methyl 2-vinyl pyridinium iodide)] and PAH∙HCl(160) [poly(allylamine hydrochloride)]. In solution, these aggregates are characterized by means of dynamic and static light scattering. They appear to be assemblies with hydrodynamic radii of 8 nm (GIC-PAPEO(22)/P2MVPI(43)) and 22 nm (GIC-PAPEO(22)/PAH∙HCl(160)), respectively. The GICs partly disintegrate in solution at salt concentrations above 10 mM NaCl. Adsorption of GICs and proteins has been studied with fixed angle optical reflectometry at salt concentrations ranging from 1 to 50 mM NaCl. Adsorption of GICs results in high density PEO side chains on the surface. Higher densities were obtained for GICs consisting of PAH∙HCl(160) (1.6 ÷ 1.9 chains/nm(2)) than of P2MVPI(43) (0.6 ÷ 1.5 chains/nm(2)). Both GIC coatings strongly suppress adsorption of all proteins on silica (>90%); however, reduction of protein adsorption on polysulfone depends on the composition of the coating and the type of protein. We observed a moderate reduction of β-lac and Lsz adsorption (>60%). Adsorption of BSA on the GIC-PAPEO(22)/P2MVPI(43) coating is moderately reduced, but on the GIC-PAPEO(22)/PAH∙HCl(160) coating it is enhanced.
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spelling pubmed-29749262010-11-29 Grafted ionomer complexes and their effect on protein adsorption on silica and polysulfone surfaces Brzozowska, Agata M. de Keizer, Arie Detrembleur, Christophe Cohen Stuart, Martien A. Norde, Willem Colloid Polym Sci Original Contribution We have studied the formation and the stability of ionomer complexes from grafted copolymers (GICs) in solution and the influence of GIC coatings on the adsorption of the proteins β-lactoglobulin (β-lac), bovine serum albumin (BSA), and lysozyme (Lsz) on silica and polysulfone. The GICs consist of the grafted copolymer PAA(28)-co-PAPEO(22) {poly(acrylic acid)-co-poly[acrylate methoxy poly(ethylene oxide)]} with negatively charged AA and neutral APEO groups, and the positively charged homopolymers: P2MVPI(43) [poly(N-methyl 2-vinyl pyridinium iodide)] and PAH∙HCl(160) [poly(allylamine hydrochloride)]. In solution, these aggregates are characterized by means of dynamic and static light scattering. They appear to be assemblies with hydrodynamic radii of 8 nm (GIC-PAPEO(22)/P2MVPI(43)) and 22 nm (GIC-PAPEO(22)/PAH∙HCl(160)), respectively. The GICs partly disintegrate in solution at salt concentrations above 10 mM NaCl. Adsorption of GICs and proteins has been studied with fixed angle optical reflectometry at salt concentrations ranging from 1 to 50 mM NaCl. Adsorption of GICs results in high density PEO side chains on the surface. Higher densities were obtained for GICs consisting of PAH∙HCl(160) (1.6 ÷ 1.9 chains/nm(2)) than of P2MVPI(43) (0.6 ÷ 1.5 chains/nm(2)). Both GIC coatings strongly suppress adsorption of all proteins on silica (>90%); however, reduction of protein adsorption on polysulfone depends on the composition of the coating and the type of protein. We observed a moderate reduction of β-lac and Lsz adsorption (>60%). Adsorption of BSA on the GIC-PAPEO(22)/P2MVPI(43) coating is moderately reduced, but on the GIC-PAPEO(22)/PAH∙HCl(160) coating it is enhanced. Springer-Verlag 2010-09-26 2010 /pmc/articles/PMC2974926/ /pubmed/21125002 http://dx.doi.org/10.1007/s00396-010-2295-6 Text en © The Author(s) 2010 https://creativecommons.org/licenses/by-nc/4.0/ This article is distributed under the terms of the Creative Commons Attribution Noncommercial License which permits any noncommercial use, distribution, and reproduction in any medium, provided the original author(s) and source are credited.
spellingShingle Original Contribution
Brzozowska, Agata M.
de Keizer, Arie
Detrembleur, Christophe
Cohen Stuart, Martien A.
Norde, Willem
Grafted ionomer complexes and their effect on protein adsorption on silica and polysulfone surfaces
title Grafted ionomer complexes and their effect on protein adsorption on silica and polysulfone surfaces
title_full Grafted ionomer complexes and their effect on protein adsorption on silica and polysulfone surfaces
title_fullStr Grafted ionomer complexes and their effect on protein adsorption on silica and polysulfone surfaces
title_full_unstemmed Grafted ionomer complexes and their effect on protein adsorption on silica and polysulfone surfaces
title_short Grafted ionomer complexes and their effect on protein adsorption on silica and polysulfone surfaces
title_sort grafted ionomer complexes and their effect on protein adsorption on silica and polysulfone surfaces
topic Original Contribution
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2974926/
https://www.ncbi.nlm.nih.gov/pubmed/21125002
http://dx.doi.org/10.1007/s00396-010-2295-6
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