The lipid cubic phase (LCP) is a nanomaterial composed of water channels surrounded by lipid bilayers. LCPs are stable at room temperature and are biocompatible. These features make the lipid cubic phases similar to biological membranes, and hence, are favorable for embedding membrane proteins. We show that the monoolein cubic phase deposited on the electrode forms a 3D lipid bilayer film convenient for electrochemical investigations of membrane proteins. In this research, we studied the effect of embedding an ionophoric peptide, gramicidin A (gA), on the structure and properties of the LCP film. The phase identity and structural parameters of the gramicidin-doped phase were characterized by small-angle X-ray scattering (SAXS). The potassium ion transport through the film were studied by electroanalytical methods: alternating current voltammetry (ACV), chronoamperometry (CA) and electrochemical impedance spectroscopy (EIS). Increased values for the current of the gramicidin-doped cubic phase compared to the empty cubic phase and changes of the EIS parameters confirmed that the peptide remained in the film in its active dimeric form. Our results show that the LCP can be considered a suitable 3D biomimetic film for the investigation of ion channels and other transporting membrane proteins, and for their application in electrochemical sensors.
Keywords: Alternating current voltammetry; Chronoamperometry; Electrochemical impedance spectroscopy; Gramicidin; Hexagonal phase; Lipid cubic phase.
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