The adsorption kinetics of three model proteins—human serumalbumin, fibrinogen and hemoglobin—has been
measured and compared using three different experimentaltechniques: optical waveguide lightmode spectroscopy
(OWLS), ellipsometry (ELM) and quartz crystal microbalance (QCM-D).The studies were complemented by also
monitoring the corresponding antibody interactions with thepre-adsorbed protein layer. All measurements were
performed with identically prepared titanium oxide coatedsubstrates. All three techniques are suitable to follow
in-situ kinetics of protein–surface and protein–antibodyinteractions, and provide quantitative values of the adsorbed
adlayer mass. The results have, however, different physicalcontents. The optical techniques OWLS and ELM provide
in most cases consistent and comparable results, which can bestraightforwardly converted to adsorbed protein molar
(‘dry’) mass. QCM-D, on the other hand, produces measured valuesthat are generally higher in terms of mass. This,
in turn, provides valuable, complementary information in tworespects: (i) the mass calculated from the resonance
frequency shift includes both protein mass and water that binds orhydrodynamically couples to the protein adlayer;
ａnd (ii) analysis of the energy dissipation in the adlayer and itsmagnitude in relation to the frequency shift (c.f.
adsorbed mass) provides insight about the mechanical/structuralproperties such as viscoelasticity. ? 2002 Elsevier
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