The adsorption and elution of the antimicrobial peptide nisin at hydrophobic,
silanized silica surfaces coated with the poly[ethylene oxide]-poly[propylene oxide]-
poly[ethylene oxide] surfactant Pluronic® F108 was measured in situ, with ellipsometry.
While such layers are known to inhibit protein adsorption, nisin was observed to adsorb in
multilayer quantities, to an...
While hydrophobic surfaces coated with the poly[ethylene oxide]-poly[propylene oxide]-poly[ethylene oxide] (PEO-PPO-PEO) surfactant Pluronic® F108 are highly resistant to plasma protein adsorption, the antimicrobial peptide nisin has been observed to adsorb in multilayer quantities at such surfaces, and the PEO chains themselves suggested to inhibit nisin exchange by blood proteins. But...
The adsorption behavior of a human recombinant Factor VIII (rFVIII) in the presence of the nonionic, poly(ethylene oxide)-poly(propylene oxide)-poly(ethylene oxide) (PEO-PPO-PEO) triblock surfactant Pluronic® F-68 was evaluated by dynamic air-water tensiometry. Surface tension kinetics were recorded for F-68 in the absence of protein at concentrations ranging from 0 to 10,000...
Adsorption kinetic data recorded for α-lactalbumin, β-casein, β-lactoglobulin, bovine serum albumin and lysozyme at silianized silica surfaces of low and high hydrophobicity, along with a simple model for adsorption and surfactant-mediated elution of protein, were used to analyze the removal of each protein by sodium dodecylsulfate (SDS) and dodecyltrimethylammonium bromide...
The role of the nonionic surfactant Tween 80 on the behavior of the therapeutic recombinant protein Factor VIII (rFVIII) was investigated at solid/liquid and air/water interfaces. In order to provide a model system to compare results obtained for the complicated rFVIII-Tween system, a well-characterized globular protein lysozyme was used. The...
Nonionic surfactants are commonly used to stabilize proteins during upstream and downstream processing and drug formulation. Surfactants stabilize the proteins through two major mechanisms: (i) their preferential location at nearby interfaces, in this way precluding protein adsorption; and/or (ii) their association with protein into "complexes" that prevent proteins from interacting...