Abstract
Multiblock copolymers of hydrophiiic polyethylene oxide and hydrophobic polystyrene were synthesized in order to study the influence of various surface properties on the adsorption of albumin from solution. These model surfaces display microphase separated structure and have the ability to be altered on a molecular scale to change surface characteristics. Compositional changes were shown to influence hydrophilicity/hydrophobicity, surface mobility, domain morphology, albumin adsorption values, binding constants, and adsorbed albumin surface stability. Changes in surface and interfacial energies as measured by Wilhelmy plate contact angle analysis could be correlated to hydrophilic/hydrophobic compositional ratios. In addition, adsorption isotherms, binding constants, and protein surface exchange rates could be similarly correlated to the same compositional trends. Increasing the hydrophilic ratios of the copolymer caused increased surface mobility (increased hysteresis), decreased receding contact angle, decreasing albumin adsorption, decreased binding constants, and increased adsorption protein stability over time. These results are attributed to unique surface behavior induced by the formation of microdomain surface morphology.
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© 1987 Plenum Press, New York
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Grainger, D., Okano, T., Kim, S.W. (1987). Surface Characteristics of Polyethylene Oxide-Polystyrene Multiblock Copolymers. In: Gebelein, C.G. (eds) Advances in Biomedical Polymers. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-1829-3_21
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DOI: https://doi.org/10.1007/978-1-4613-1829-3_21
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