Quartz Crystal Microbalance as a Sensor to Characterize Macromolecular Assembly Dynamics
Figure 19
QCM-D analysis of AH peptide binding to a quartz crystal coated with POPC model lipid membrane and a cell-derived membrane. (a) AH peptide binding dynamics on a POPC model lipid bilayer. Frequency, , and dissipation, , changes detected by QCM-D as a function of time were recorded. (b) NH peptide binding dynamics to POPC model lipid bilayers. NH contains three mutations designed to disrupt the hydrophobic face of AH. (c) Binding of AH peptide to Huh7-derived microsome coated onto an SiO2 quartz crystal substrate. The data show that the microsomes saturated at a higher mass than the model POPC membrane, presumably due to the presence of proteinaceous components. They also show by the dissipation value that those proteinaceous components are associated with higher viscoelastic energy dissipation, as expected. (d) No binding of NH peptide to Huh7-derived membranes adsorbed on an SiO2 surface. Note that there are no changes in either the frequency or dissipation, which suggests that there is no binding to Huh7-derived membranes. Reprint from [34].
