A model biomimetic system for the study of protein reconstitution or drug interactions should include lipid rafts in the mixed lipid monolayer, since they are usually the domains embedding membrane proteins and peptides. Four model lipid films composed of three components: 1,2-dioleoyl-sn-glycero-3-phosphocholine (DOPC), cholesterol (Chol) and sphingomyelin (SM) mixed in different molar ratios were proposed and investigated using surface pressure measurements and thermodynamic analysis of the monolayers at the air–water interface and imaged by Brewster angle microscopy. The ternary monolayers were transferred from the air–water onto the gold electrodes to form bilayer films and were studied for the first time by electrochemical methods: alternative current voltammetry and electrochemical impedance spectroscopy and imaged by atomic force microscopy. In excess of DOPC, the ternary systems remained too liquid for the raft region to be stable, while in the excess of cholesterol the layers were too solid. The layers with SM in excess lead to the formation of Chol:SM complexes but the amount of the fluid matrix was very low. The equimolar content of the three components lead to the formation of a stable and well-organized assembly with well-developed raft microdomains of larger thickness, surrounded by the more fluid part of the bilayer. The latter is proposed as a convenient raft model membrane for further physicochemical studies of interactions with drugs or pollutants or incorporation of membrane proteins.

Supported lipid membranes are widely used platforms which serve as simplified models of cell membranes. Among numerous methods used for preparation of planar lipid films, self-assembly of bicelles appears to be promising strategy. Therefore, in this paper we have examined the mechanism of formation and the electrochemical properties of lipid films deposited onto thioglucose-modified gold electrodes from bicellar mixtures. It was found that adsorption of the bicelles occurs by replacement of interfacial water and it leads to formation of a double bilayer structure on the electrode surface. The resulting lipid assembly contains numerous defects and pinholes which affect the permeability of the membrane for ions and water. Significant improvement in morphology and electrochemical characteristics is achieved upon freeze–thaw treatment of the deposited membrane. The lipid assembly is rearranged to single bilayer configuration with locally occurring patches of the second bilayer, and the number of pinholes is substantially decreased. Electrochemical characterization of the lipid membrane after freeze–thaw treatment demonstrated that its permeability for ions and water is significantly reduced, which was manifested by the relatively high value of the membrane resistance.

Sparsely tethered bilayer lipid membrane (stBLM) is a popular model considered to mimic biological membranes. The advantage of this system is the molecular architecture that provides a water environment on both sides of the lipid membrane. In this work, we have coupled electrochemical measurements with surface enhanced infrared absorption spectroscopy and atomic force microscopy to evaluate the effect of the electric field on the physicochemical properties of stBLM composed of 1,2‐dimyristoyl‐sn‐glycero‐3‐phosphocholine and cholesterol. More specifically, we have focused on the structure of the submembrane water and nanomechanical properties of the membrane. Our experimental results revealed that stBLM composed of DMPC/Cholesterol offers good nanomechanical stability and low permeability within a relatively wide potential window. Importantly, it also covers biologically relevant range corresponding to transmembrane potentials occurring in natural cell membranes, which makes them suitable platform for bioinspired sensing devices.

Many biochemical processes related to proper homeostasis take place in cell membranes. The key molecules involved in these processes are proteins, including transmembrane proteins. These macromolecules still challenge the understanding of their function within the membrane. Biomimetic models that mimic the properties of the cell membrane can help understand their functionality. Unfortunately, preserving the native protein structure in such systems is problematic. A possible solution to this problem involves the use of bicelles. Their unique properties make integrating bicelles with transmembrane proteins manageable while preserving their native structure. Hitherto, bicelles have not been used as precursors for protein-hosting lipid membranes deposited on solid substrates like pre-modified gold. Here, we demonstrated that bicelles can be self-assembled to form sparsely tethered bilayer lipid membranes and the properties of the resulting membrane satisfy the conditions suitable for transmembrane protein insertion. We showed that the incorporation of α-hemolysin toxin in the lipid membrane leads to a decrease in membrane resistance due to pore formation. Simultaneously, the insertion of the protein causes a drop in the capacitance of the membrane-modified electrode, which can be explained by the dehydration of the polar region of the lipid bilayer and the loss of water from the submembrane region.

This concept paper elucidates the possible influence of the electrical double layer (EDL) and the polyelectrolytic nature of bacterial cell walls on the behavior of antimicrobial peptides (AMPs) and lipopeptides. It proposes that the presence of EDL adjacent to lipid membranes may play a crucial role in inducing peptide aggregation and conformational changes, thus affecting their antimicrobial activity. Furthermore, it emphasizes that the negatively charged components in both Gram‐positive and Gram‐negative bacterial cell walls may act as polyelectrolytes, effectively reducing the critical micellization concentration (CMC) of positively charged peptides and lipopeptides. This reduction is expected to facilitate their aggregation, potentially enhancing their accumulation at the bacterial membrane and increasing their effectiveness in disrupting membrane integrity and exerting antimicrobial activity. Therefore, understanding the interplay between EDL effects, polyelectrolytic properties of bacterial cell walls, and the behavior of antimicrobial peptides is essential for elucidating their mechanisms of action and optimizing their therapeutic potential.