Dual polarization interferometry: An optical biosensor which allows new insights into peptide-induced changes in biomembrane structure

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The interactions between peptides and membranes mediate awide variety of biological processes and characterization of the molecular details of these interactions is central to our understanding of cellular events such as protein trafficking, cellular signalling, and ion-channel formation. Optical techniques have played an important role in the study of the mechanisms and kinetics of peptide-membrane, with instruments utilizing for example, surface plasmon resonance (SPR) to monitor molecular events occurring within the first few hundred nanometres of a sensor surface.[1,2] However, an important limitation is their inability to differentiate between changes in sample layer thickness and density, i.e. the molecular orientation of molecules at the surface. This limitation is a particular impediment to understanding membrane interactions and molecular aggregation. To address this problem, dual polarization interferometry (DPI) can be used to analyze thin films to obtain unique combinations of several opto-geometrical properties including refractive index (RI), density, thickness, mass, and birefringence to be measured in real time for the formation of biomolecule layers.[3-7]
Original languageEnglish
Pages (from-to)844 - 845
Number of pages2
JournalAustralian Journal of Chemistry
Issue number6
Publication statusPublished - 2011

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