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Engineering Lipid Bilayer Membranes for Protein Studies
AbstractLipid membranes regulate the flow of nutrients and communication signaling between cells and protect the sub-cellular structures. Recent attempts to fabricate artificial systems using nanostructures that mimic the physiological properties of natural lipid bilayer membranes (LBM) fused with transmembrane proteins have helped demonstrate the importance of temperature, pH, ionic strength, adsorption behavior, conformational reorientation and surface density in cellular membranes which all affect the incorporation of proteins on solid surfaces. Much of this work is performed on artificial templates made of polymer sponges or porous materials based on alumina, mica, and porous silicon (PSi) surfaces. For example, porous silicon materials have high biocompatibility, biodegradability, and photoluminescence, which allow them to be used both as a support structure for lipid bilayers or a template to measure the electrochemical functionality of living cells grown over the surface as in vivo. The variety of these media, coupled with the complex physiological conditions present in living systems, warrant a summary and prospectus detailing which artificial systems provide the most promise for different biological conditions. This study summarizes the use of electrochemical impedance spectroscopy (EIS) data on artificial biological membranes that are closely matched with previously published biological systems using both black lipid membrane and patch clamp techniques.
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Khan, M.S.; Dosoky, N.S.; Williams, J.D. Engineering Lipid Bilayer Membranes for Protein Studies. Int. J. Mol. Sci. 2013, 14, 21561-21597.View more citation formats
Khan MS, Dosoky NS, Williams JD. Engineering Lipid Bilayer Membranes for Protein Studies. International Journal of Molecular Sciences. 2013; 14(11):21561-21597.Chicago/Turabian Style
Khan, Muhammad S.; Dosoky, Noura S.; Williams, John D. 2013. "Engineering Lipid Bilayer Membranes for Protein Studies." Int. J. Mol. Sci. 14, no. 11: 21561-21597.