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We developed an integrated device comprising a quartz crystal microbalance (QCM) and a field-effect transistor (FET) with a single common gold electrode in a flow chamber. An alternating current inducing oscillations in the piezoelectric quartz of the QCM sensor is electrically independent of the circuit for the FET output so that the two sensors in different detection mechanisms simultaneously record binding kinetics from a single protein solution on the same electrode. A conjunction of adsorbed mass from QCM with electric nature of bound protein from FET provided deeper understanding on a complex process of nonspecific protein adsorption and subsequent conformational changes at a solid/liquid interface. Lower apparent kon values obtained by FET than those obtained by QCM on hydrophobic surfaces are interpreted as preferred binding of protein molecules facing uncharged domains to the electrode surface, whereas higher koff values by FET than those by QCM imply active macromolecular rearrangements on the surfaces mainly driven by hydrophobic association in an aqueous medium. The advanced features of the combined sensor including in situ, label-free, and real-time monitoring provide information on structural dynamics, beyond measurements of affinities and kinetics in biological binding reactions.

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This page is a summary of: Simultaneous Monitoring of Protein Adsorption Kinetics Using a Quartz Crystal Microbalance and Field-Effect Transistor Integrated Device, Analytical Chemistry, August 2012, American Chemical Society (ACS),
DOI: 10.1021/ac3015092.
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