| Abstract
| - A novel spacer consisting of a hexapeptide molecule with a high tendency to form a 310-helical structure,which terminates with a sulfydryl group for anchoring to a metal, was tailored for use as a tetheredhydrophilic spacer to be interposed between a metal support and a lipid bilayer. The thiol peptide has twotriethylenoxy side chains that impart it a satisfactory hydrophilicity and are intended to keep the anchoredthiol peptide chains sufficiently apart so as to accommodate water molecules and inorganic ions and tocreate a suitable environment for the incorporation of integral proteins. This thiol peptide was anchoredto a hanging mercury drop electrode. The formation of a phospholipid bilayer on top of the self-assembledthiol peptide was carried out by a novel procedure which exploits the spontaneous tendency of a lipid filmto form a bilayer when interposed between two hydrophilic phases. The resulting mercury-supported thiolpeptide/lipid bilayer system was characterized by ac voltammetry with phase resolution, chronocoulometry,and impedance spectroscopy. The suitability of this tethered film as a biomembrane model was tested byincorporating ubiquinone-10 and valinomycin.
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