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    Protein Adsorption on Supported Phospholipid Bilayers

    Year: 2002

    Journal: Journal of Colloid and Interface Science 246, 40–47 (2002), 20100827

    Authors: Glasmästar K., Larsson C., Höök F., Kasemo B.

    Last authors: Bengt Kasemo

    Organizations: Department of Applied Physics, Chalmers University of Technology and Göteborg University, SE-412 96 Göteborg, Sweden; and Department of Cell and Molecular Biology, Göteborg University, SE-412 96 Göteborg, Sweden

    Country: Sweden

    Quartz crystal microbalance with dissipation (QCM-D) measurements were used to investigate the adsorption of human fibrinogen, human serum albumin, bovine hemoglobin, horse heart cytochrome c, human immunoglobulin (hIgG), and 10% fetal bovine serum on supported bilayers of egg-phosphatidylcholine (eggPC) lipids. For comparison the adsorption of fibrinogen and hIgG to eggPC bi-layers was also studied with surface plasmon resonance (SPR). The supported bilayers were formed in situ by vesicle adhesion and spon-taneous fusion onto a SiO2 surface. The supported lipid bilayer is highly protein resistant: The irreversible adsorption measured with the QCM-Dtechnique was below the detection level, while reversible protein adsorption was detected for all the proteins in the range 0.3– 4% of the saturation coverage on a hydrophobic thiol monolayer on gold. The adsorbed amounts were slightly higher for the SPR measurements. Possible mechanisms for the protein resistance of eggPC bilayers are briefly discussed.