Monitoring molecular assembly of biofilms using quartz crystal microbalance with dissipation

Date
2022
Advisor
Instructor
Source Title
Bacterial amyloids: Methods and protocols
Print ISSN
1064-3745
Electronic ISSN
Publisher
Springer
Volume
2538
Issue
Pages
25 - 33
Language
English
Type
Book Chapter
Journal Title
Journal ISSN
Volume Title
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.

Course
Other identifiers
Book Title
Bacterial amyloids: Methods and protocols
Keywords
Adsorption, Amyloid, Binding, Biofilm, Dissipation, Kinetics, Protein, QCM-D, Quartz sensor, Surface
Citation
Published Version (Please cite this version)