A comparative study of protein adsorption on titanium - Hook et al. Round robin - Colloids and Surfaces 2002_R3
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-D). 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-D, 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. © 2002 Elsevier
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