Peptide/protein-membrane interactions can destabilise and damage the membrane which can lead to cell death. Characterisation of the molecular details of these binding-mediated membrane destabilisation processes is therefore central to understanding cellular events such as antimicrobial action, membrane-mediated amyloid aggregation, and apoptotic protein induced mitochondrial membrane permeabilization. We have used optical biosensor and imaging techniques to allow biophysical analysis of membrane structure changes during peptide and protein binding. It is now evident that membrane interactions involve multiple kinetically distinct stages through measurement of birefringence in a real-time format. The combination of these biosensors with other biophysical techniques now opens the door to redefining molecular mechanism of biomolecular interactions in which the membrane bilayer is a key player. This has further expanded our capacity to pose novel questions around membrane structure changes that accompany peptide and protein binding.
Lee TH, Hirst DJ, Kulkarni K, Del Borgo MP and Aguilar MI, ‘Exploring Molecular-Biomembrane Interactions with Surface Plasmon Resonance and Dual Polarization Interferometry Technology: Expanding the Spotlight onto Biomembrane Structure’, Chemical Reviews, 118 (2018) 5392-5487.