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    The effect of charged groups on protein interactions with poly(HEMA) hydrogels

    Year: 2005

    Journal: Biomaterials 27 (2006) 567-575, 20100827

    Authors: Lord M.S., Stenzel M.H., Simmons A., Milthorpe B.K.

    Last authors: Bruce K. Milthorpe

    Organizations: Graduate School of Biomedical Engineering, The University of New South Wales, Sydney NSW 2052, Australia, Centre for Advanced Macromolecular Design, School of Chemical Engineering and Industrial Chemistry, The University of New South Wales, Sydney NSW 2052, Australia

    Country: Australia

    Proteins, lipids and other biomolecules interact strongly with the acrylic-based biomaterials used for contact lenses. Although hydrogels are nominally resistant to protein fouling, many studies have reported considerable amounts of protein bound to poly(2-hydroxyethylmethacrylate) (PHEMA) lenses. This study examined the binding of a series of biomolecules (tear protein analogues, mucin and cholesterol) to poly(methylmethacrylate) (PMMA) and three HEMA-based hydrogels (PHEMA, HEMA plus methacrylic acid (P(HEMA-MAA)), HEMA plus methacrylic acid plus N-vinylpyrrolidone (P(HEMA-MAA-NVP))) by use of a quartz crystal microbalance with dissipation (QCM-D) monitoring. The QCM-D estimates changes in the mass and viscous constant for the adsorbed layer through measurements of frequency and dissipation. Protein interaction with each of the test materials caused a net increase in mass of the material indicating protein binding except for lysozyme interacting with P(HEMA-MAA). A net decrease in mass was observed for lysozyme interacting with P(HEMA-MAA) which may be ascribed to lysozyme collapsing the hydrogel by expelling water. A net mass decrease was observed for cholesterol interacting with each of the hydrogel materials, while a mass increase was observed on PMMA.