| AVS 54th International Symposium | |
| Biomaterial Interfaces | Thursday Sessions |
| Session BI-ThM |
| Session: | Biomimetic Phospholipid Interfaces |
| Presenter: | H. Zhang, University of Arizona |
| Authors: | H. Zhang, University of Arizona V. Subramaniam, Univeristy of Arizona S. Burnside, University of Arizona G. D'Ambruoso, University of Arizona M. Brown, University of Arizona S. Saavedra, University of Arizona |
| Correspondent: | Click to Email |
Membrane-associated proteins are of great importance in transport and signal transduction cascades and therefore are crucial pharmacological targets. With the goal of developing biosensors to screen pharmaceutical candidates, numerous research groups have reconstituted transmembrane proteins into lipid membranes, which provide a biocompatible environment. Our group has been investigating the use of synthetic lipids that can be polymerized to form a highly stable bilayer. Absorbance spectroscopy and plasmon waveguide spectroscopy (PWR) are being utilized to monitor the photoactivity of a G-protein coupled receptor (GPCR), bovine rhodopsin, in both polymerized liposomes and planar supported lipid bilayers (PLSBs), respectively. The photoactivity of rhodopsin is largely retained in some types of poly(lipid) membranes. However, the lipid structure and bilayer polymerization clearly affect the retention of protein activity. PWR is used to probe conformational changes accompanying rhodopsin photoactivation in PSLBs, whereas absorbance spectroscopy is used to directly measure formation of the rhodopsin activated state. Studies are also being performed to investigate the effect of lipid structure on the activity of other types of GPCRs, e.g. the human delta opioid receptor.