Studies into the mechanism of cell lytic peptide action seek to define the structure of the final membrane disruption entity. While this provides very important information in terms of the mechanism of disruption, we still have limited capacity to rationalise differences in the activity of closely-related peptides. In order to provide a more detailed dissection of membrane binding and disruption, more specific information on the molecular changes that occur from the point at which the peptide firsts interacts with the membrane surface through to the final dissociation from, or disruption of the membrane is required. This process can include multiple steps associated with changes in the peptide and membrane structure and the insertion/re-orientation of the peptide, and the ability to measure these steps would clearly allow a more detailed redefinition of peptide-membrane interactions.

The application of optical biosensors to the measurement of peptide binding AND analysis of membrane bilayer structure in terms of changes in birefringence provides new understanding of the molecular events throughout the peptide binding process. However, this new insight opens up new challenges in the analysis of these multi-facetted pathways, especially given the dynamic and complex nature of biomembrane compositions. In this presentation the use of optical biosensors together with other biophysical techniques to analyse biomembrane interactions will be described and how this new understanding is a platform for both lipidomic analysis and high-resolution imaging of biomembrane structure and function.