Daniel J. Hirst

TL;DR: A review of the application of surface plasmon resonance and dual polarization interferometry-based biosensors to the study of biomembrane-based systems using both planar mono- or bilayers or liposomes is presented.

TL;DR: It is demonstrated that more disordered unsaturated bilayers are more susceptible to further disorganisation and have a lower capacity to recover from peptide-induced structural changes than saturated ordered bilayers.

TL;DR: A theoretical and practical overview of the application of biosensor technology with a specific focus on DPI, PWR and OWLS to study biomembrane-mediated events and the mechanism of biomemBRane disruption is provided.

TL;DR: The results demonstrate the importance of the difference in membrane fluidity between the gel phase DMPC and the liquid crystal phase POPC for peptide-membrane interactions and establish the combination of DPI and kinetic modeling as a powerful tool for revealing features of peptide and membrane interaction mechanisms, including intermediate states between initial binding and full membrane disruption.

TL;DR: Dual polarisation interferometry suggests that Helix 8 can respond to the presence of PI(4)P by withdrawing from the bilayer, resulting in a functional conformational change in the receptor.