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See detailGrafted ionomer complexes and their effect on protein adsorption on silica and polysulfone surfaces
Brzozowska, Agata M.; de Keizer, Arie; Detrembleur, Christophe ULg et al

in Colloid and Polymer Science (2010), 288(16/17), 1621-1632

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 beta-lactoglobulin (beta ... [more ▼]

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 beta-lactoglobulin (beta-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 center dot 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 center dot 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 center dot HCl(160) (1.6 divided by 1.9 chains/nm(2)) than of P2MVPI(43) (0.6 divided by 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 beta-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 center dot HCl(160) coating it is enhanced. [less ▲]

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See detailGrafted block complex coacervate core micelles and their effect on protein adsorption on silica and polystyrene
Brzozowska, Agata M.; de Keizer, Arie; Norde, Willem et al

in Colloid and Polymer Science (2010), 288(10/11), 1081-1095

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 ... [more ▼]

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. [less ▲]

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See detailAdsorption and structure formation of the weak polyelectrolytic diblock copolymer, PVP-b-PDMAEMA
Mahltig, Boris; Gohy, Jean-François; Antoun, Sayed et al

in Colloid and Polymer Science (2002), 280(6), 495-502

This paper reports on the pH-dependent adsorption of weak the polyelectrolytic diblock copolymer poly(2-vinylpyridine)-block-poly(dimethylaminoethyl methacrylate), (PVP-b-PDMAEMA). Aqueous PVP-b-PDMAEMA ... [more ▼]

This paper reports on the pH-dependent adsorption of weak the polyelectrolytic diblock copolymer poly(2-vinylpyridine)-block-poly(dimethylaminoethyl methacrylate), (PVP-b-PDMAEMA). Aqueous PVP-b-PDMAEMA solutions have been adsorbed on alkaline pretreated silicon substrates. Altogether two copolymers differing in block ratio and molecular weight were used for the investigations. While the electrical charge of both samples in solution was investigated by electrophoretic measurements, the adsorbed polymer layers were studied with ellipsometry and atomic force microscopy (AFM). Depending on pH the electrical charge of both blocks of the diblock copolymer varied. Three different regimes have been identified. Under acidic conditions at pH < 5, both blocks are mainly positively charged. At medium pH between 5 and 8, only the PDMAEMA block is positively charged. At pH > 8, both blocks are nearly uncharged and a polymer precipitation occurred in solution. Each of these pH regimes was characterized by a specific adsorption behaviour leading to two adsorption maxima at acidic and alkaline pH values, while at medium pH a plateau in the adsorbed amount was observed. Moreover, the structures of the polyelectrolytes formed on the substrate after adsorption were specific to each of the three pH regimes. [less ▲]

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See detailSurface structure of thin film blends of polystyrene and poly(n-butyl methacrylate)
Affrossman, S.; Jérôme, Robert ULg; O'Neill, S. A. et al

in Colloid and Polymer Science (2000), 278(10), 993-999

Thin films of blends of polystyrene (PS) and poly(n-butyl methacrylate) (PBMA) were prepared by spin-casting onto silicon wafers in order to map the lateral distribution of the two polymers. The surfaces ... [more ▼]

Thin films of blends of polystyrene (PS) and poly(n-butyl methacrylate) (PBMA) were prepared by spin-casting onto silicon wafers in order to map the lateral distribution of the two polymers. The surfaces were examined by atomic force microscopy (AFM) secondary ion mass spectroscopy X-ray photoelectron spectroscopy (XPS) and photoemission electron microscopy (PEEM). Films with PBMA contents of 50% w/w or less were relatively smooth, but further increase in the PBMA content produced, initially, protruding PS ribbons and then, for PBMA ≥80% w/w, isolated PS islands. At all concentrations the topmost surface (0.5-1.0 nm) was covered by PBMA, whilst the PBMA concentration in the near-surface region, measured by XPS, increased with bulk content to eventual saturation. PEEM measurements of a PS-PBMA film at the composition at which ribbon features were observed by AFM also showed a PS-rich ribbon structure surrounded by a sea of mainly PBMA. [less ▲]

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See detailAdsorption of block polyampholyte micelles in monolayers at the silicon water interface
Mahltig, Boris; Gohy, Jean-François; Jérôme, Robert ULg et al

in Colloid and Polymer Science (2000), 278(6), 502-508

The adsorption of the diblock polyampholyte poly (methacrylic acid)-block-poly((di-methylamino)ethyl methacrylate) from aqueous solution on silicon substrates was investigated as a function of polymer ... [more ▼]

The adsorption of the diblock polyampholyte poly (methacrylic acid)-block-poly((di-methylamino)ethyl methacrylate) from aqueous solution on silicon substrates was investigated as a function of polymer concentration and pH. Dynamic light scattering and electrokinetic measurements were used to characterize the polyampholyte in solution. The amount of polymer adsorbed was determined by ellipsometry and lateral structures of the polymer layer were investigated by scanning force microscopy. The amount of polymer adsorbed was found to be strongly influenced by the pH of the polymer solution, while the size of the polyampholyte micelles adsorbed on the surface was hardly affected by pH during adsorption. From investigations by scanning force microscopy well-seperated micelles were seen in the dried monolayers adsorbed directly from solution. The structures at the surface are correlated to structures in solution, and the adsorbed amount depends on the relative charge of the micelles and the surface. [less ▲]

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See detailEnzyme immobilization in reactive nanoparticles produced by inverse microemulsion polymerization
Daubresse, Catherine; Grandfils, Christian ULg; Jérôme, Robert ULg et al

in Colloid and Polymer Science (1996), 274(5), 482-489

This paper deals with the immobilization of alkaline phosphatase by physical entrapment within colloidal particles produced by inverse microemulsion polymerization. Functionality has been imparted to the ... [more ▼]

This paper deals with the immobilization of alkaline phosphatase by physical entrapment within colloidal particles produced by inverse microemulsion polymerization. Functionality has been imparted to the nanoparticle surface by copolymerization of acrylamide (the main monomer), N,N'-methylene-bis-acrylamide (the cross-linking agent) with either N-acryloyl-l,6-diamino-hexane (an amine promoter) or acrylic acid (a carboxylic acid promoter). The effect of the functions comonomers on the size and zeta potential of the reactive latexes has been studied. Integrity of the immobilized enzyme has been ascertained from its catalytic activity towards hydrolysis of p-nitrophenyl-phosphate. [less ▲]

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