Abstract
A set of water-swollen core-shell particles was synthesized by emulsion polymerization of a 1,3-dioxolane functional monomer in water. After removal of the 1,3-dioxolane group, the particles' shells were shown to swell in aqueous media. Upon hydrolysis, the particles increased in size from around 70 to 100-130 nm. A bicinchoninic acid assay and ζ-potential measurements were used to investigate the adsorption of lysozyme, albumin, or fibrinogen. Each of the core-shell particles adsorbed significantly less protein than the noncoated core (polystyrene) particles. Differences were observed as both the amount of difunctional, cross-linking monomer and the amount of shell monomer in the feed were changed. The core-shell particles were shown to be resistant to protein adsorption, and the degree to which the three proteins adsorbed was dependent on the formulation of the shell.
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