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    QCM-D and XPS study of protein adsorption on plasma polymers with sulfonate and phosphonate surface groups

    Year: 2019

    Journal: Colloid Surf. B-Biointerfaces, Volume 173, JAN 1, page 447–453

    Authors: Siow, Kim S.; Britcher, Leanne; Kumar, Sunil; Griesser, Hans J.

    Keywords: Biomaterial interfaces; Protein adsorption; Heptylamine plasma polymers; Michael-type addition; X-ray photoelectron spectroscopy; Quartz crystal microbalance; Sulfonate; Phosphonate; Aging

    As some proteins are known to interact with sulfated and phosphated biomolecules such as specific glycosa-minoglycans, this study derives from the hypothesis that sulfonate and phosphonate groups on solid polymer surfaces might cause specific interfacial interactions. Such surfaces were prepared by plasma polymerization of heptylamine (HA) and subsequent grafting of sulfonate or phosphonate groups via Michael-type addition of vinylic compounds. Adsorption of the proteins fibrinogen, albumin (HSA) and lysozyme on these functionalised plasma polymer surfaces was studied by XPS and quartz crystal microbalance with dissipation (QCM-D). It was also studied whether pre-adsorption with HSA would lead to a passivated surface against further adsorption of other proteins. XPS confirmed grafting of vinyl sulfonate and vinyl phosphonate onto the amine surface and showed that the proteins adsorbed to saturation at between 1 and 2 h. QCM-D showed rapid and irreversible adsorption of albumin on all three surfaces, while lysozyme could be desorbed with PBS to substantial extents from the sulfonated and phosphonated surfaces but not from the amine surface. Fibrinogen showed rapid initial adsorption followed by slower additional mass gain over hours. Passivation with albumin led to small and largely reversible subsequent adsorption of lysozyme, whereas with fibrinogen partial displacement yielded a mixed layer, regardless of the surface chemistry. Thus, protein adsorption onto these sulfonated and phosphonated surfaces is complex, and not dominated by electrostatic charge effects.
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