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    A Comparative Study of Protein Adsorption on Titanium Oxide Surfaces using in situ Ellipsometry, Optical Waveguide Lightmode Spectroscopy, and Quartz Crystal Microbalance/Dissipation

    Year: 2002

    Journal: Colloids and Surfaces B: Biointerfaces 24 (2002) 155–170, 20100827

    Authors: Höök F., Vörös J., Rodahl M., Kurrat R., Böni P., Ramsden J.J., Textor M., Spencer N.D., Tengvall P., Gold J., Kasemo B.

    Last authors: B. Kasemo

    Organizations: Department of Applied Physics, Chalmers Institute of Technology, SE-412 96 Göteborg, Sweden Laboratory for Surface Science and Technology, Department of Materials, Swiss Federal Institute of Technology, CH-8092 Zürich, Switzerland Department of Physics and Measurement Technology, Laboratory of Applied Physics, Linköping University, SE-581 83 Linköping, Sweden Paul Scherrer Institut, CH-5232 Villigen PSI, Switzerland Department of Biophysical Chemistry, Biocenter of the University, CH-4056 Basel, Switzerland

    Country: Sweden

    The adsorption kinetics of three model proteins -human serum albumin, fibrinogen and hemoglobin- has been measured and compared using three different experimental techniques: optical waveguide lightmode spectroscopy (OWLS), ellipsometry (ELM) and quartz crystal microbalance (QCM). The studies were complemented by also monitoring the corresponding antibody interactions with the pre-adsorbed protein layer. All measurements were performed with identically prepared titanium-oxide coated substrates. All three techniques are suitable to follow in-situ kinetics of protein-surface and protein-antibody interactions, and provide quantitative values of the adsorbed adlayer mass. The results have, however, different physical contents. The optical techniques OWLS and ELM provide in most cases consistent and comparable results, which can be straightforwardly converted to adsorbed protein molar ("dry") mass. QCM, on the other hand, produces measured values that are generally higher in terms of mass. This, in turn, provides valuable, complementary information in two respects: (i) the mass calculated from the resonance frequency shift includes both protein mass and water that binds or hydrodynamically couples to the protein adlayer and (ii) analysis of the energy dissipation in the adlayer and its magnitude in relation to the frequency shift (c.f. adsorbed mass) provides insight about the mechanical/structural properties such as viscoelasticity.