Abstract
The structure and the functionality of biofilm proteins, the main components of the extracellular matrix, can be tuned by protein engineering. The use of binding kinetics data has been demonstrated in the characterization of recombinantly produced biofilm proteins to control their behavior on certain surfaces or under certain conditions. Quartz crystal microbalance with dissipation monitoring (QCM-D) allows measuring the change in resonance frequency and the energy loss and distribution upon the interaction of molecules with the surface. The characterization of the molecular assembly of curli biofilm proteins on different surfaces using QCM-D is presented here as a detailed protocol. The experimental procedure detailed in this chapter can be applied and modified for other biofilm proteins or subunits to determine their surface adsorption and kinetic binding characteristics.
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Yuca, E., Şeker, U.Ö.Ş. (2022). Monitoring Molecular Assembly of Biofilms Using Quartz Crystal Microbalance with Dissipation (QCM-D). In: Arluison, V., Wien, F., Marcoleta, A. (eds) Bacterial Amyloids. Methods in Molecular Biology, vol 2538. Humana, New York, NY. https://doi.org/10.1007/978-1-0716-2529-3_3
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DOI: https://doi.org/10.1007/978-1-0716-2529-3_3
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