Reduction of protein adsorption to a solid surface by a coating composed of polymeric micelles with a glass-like core

Hofs, B.; Brzozowska, A.M.; Keizer, A. de; Stuart, Martien A. Cohen

doi:10.1016/j.jcis.2008.06.006

Cited by 28 publications

(27 citation statements)

References 40 publications

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“…Base on these assumptions, the thickness of an unfolded C3M layer is roughly half the diameter of a micelle, i.e., half of the thickness of micelles which do not unfold. Unfolding of C3Ms on solid surfaces is, however, governed by a subtle balance between the stability of the micelles and the wetting properties of the surface, core, and corona [3]. The differences in the adsorbed amounts suggest that the micelles with the short homopolymer are more stable against unfolding than the micelles with the long homopolymer.…”

Section: Resultsmentioning

confidence: 99%

Grafted block complex coacervate core micelles and their effect on protein adsorption on silica and polystyrene

et al. 2010

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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 β-lactoglobulin, bovine serum albumin, and lysozyme. The C3Ms consist of a grafted block copolymer PAA21-b-PAPEO14 (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 PAA21-b-PAPEO14 alone adsorption of C3Ms significantly increases the amount of PAA21-b-PAPEO14 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-PAPEO14/P2MVPI43 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-PAPEO14/P2MVPI43 layer is partly removed from the surface upon exposure to an excess of β-lactoglobulin solution, due to formation of soluble aggregates consisting of β-lactoglobulin and P2MVPI43. In contrast, C3M-PAPEO14/P2MVPI228 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 PAA21-b-PAPEO14 layer causes only a moderate reduction of protein adsorption.

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Section: Resultsmentioning

confidence: 99%

Grafted block complex coacervate core micelles and their effect on protein adsorption on silica and polystyrene

et al. 2010

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“…Selective adsorption is very difficult to implement in chemical terms. Hence, brushes prepared by adsorption from solution tend to have low densities or a poorly defined lateral structure [84].…”

Section: Zipper Brushesmentioning

confidence: 99%

Polyelectrolyte complexes: Bulk phases and colloidal systems

Gucht

Spruijt

Lemmers

et al. 2011

Journal of Colloid and Interface Science

497

280

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“…On the contrary, for both cases aggregates composed of charged blocks with significantly different lengths adsorbed practically irreversibly. We have attributed these differences in adsorbed amounts after rinsing with solvent to the stability of the aggregates and to the wettability of the native surface [11]. Adsorption of regular C3Ms includes an unfolding mechanism in order to adapt the spherical geometry of the micelles to the flat geometry of the surface.…”

Section: Resultsmentioning

confidence: 99%

“…It is determined by the properties of both the protein (size, charge, wetting behavior) and the surface (hydrophobicity, charge, heterogeneity). The process is strongly influenced by the ionic strength of the solution and valence of the present ions [11, 49, 50]. Upon increasing the salt concentration, electrostatic interactions between the protein and the surface become weaker due to screening of charges; however, hydrophobic interactions remain essentially unchanged.…”

Section: Resultsmentioning

confidence: 99%

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

et al. 2010

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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 PAA28-co-PAPEO22 {poly(acrylic acid)-co-poly[acrylate methoxy poly(ethylene oxide)]} with negatively charged AA and neutral APEO groups, and the positively charged homopolymers: P2MVPI43 [poly(N-methyl 2-vinyl pyridinium iodide)] and PAH∙HCl160 [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-PAPEO22/P2MVPI43) and 22 nm (GIC-PAPEO22/PAH∙HCl160), 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∙HCl160 (1.6 ÷ 1.9 chains/nm2) than of P2MVPI43 (0.6 ÷ 1.5 chains/nm2). 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-PAPEO22/P2MVPI43 coating is moderately reduced, but on the GIC-PAPEO22/PAH∙HCl160 coating it is enhanced.

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Reduction of protein adsorption to a solid surface by a coating composed of polymeric micelles with a glass-like core

Cited by 28 publications

References 40 publications

Grafted block complex coacervate core micelles and their effect on protein adsorption on silica and polystyrene

Grafted block complex coacervate core micelles and their effect on protein adsorption on silica and polystyrene

Polyelectrolyte complexes: Bulk phases and colloidal systems

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

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