Abstract
The one-sided addition of fengycin (FE) to planar lipid bilayers mimicking target fungal cell membranes up to 0.1 to 0.5 μM in the membrane bathing solution leads to the formation of well-defined and well-reproducible single-ion channels of various conductances in the picosiemens range. FE channels were characterized by asymmetric conductance-voltage characteristic. Membranes treated with FE showed nonideal cationic selectivity in potassium chloride bathing solutions. The membrane conductance induced by FE increased with the second power of the lipopeptide aqueous concentration, suggesting that at least FE dimers are involved in the formation of conductive subunits. The pore formation ability of FE was not distinctly affected by the molecular shape of membrane lipids but strongly depended on the presence of negatively charged species in the bilayer. FE channels were characterized by weakly pronounced voltage gating. Small molecules known to modify the transmembrane distribution of electrical potential and the lateral pressure profile were used to modulate the channel-forming activity of FE. The observed effects of membrane modifiers were attributed to changes in lipid packing and lipopeptide oligomerization in the membrane.
Highlights
The one-sided addition of fengycin (FE) to planar lipid bilayers mimicking target fungal cell membranes up to 0.1 to 0.5 μM in the membrane bathing solution leads to the formation of well-defined and wellreproducible single-ion channels of various conductances in the picosiemens range
The mirror difference in the g(V) characteristics of syringomycin and FE channels is due to the opposite charges of lipopeptide molecules
Using the model lipid membranes, we demonstrated that the lipopeptide from Bacillus subtilis FE forms ion channels of weak cation selectivity in lipid bilayers mimicking the composition of target fungal cell membranes
Summary
The one-sided addition of fengycin (FE) to planar lipid bilayers mimicking target fungal cell membranes up to 0.1 to 0.5 μM in the membrane bathing solution leads to the formation of well-defined and wellreproducible single-ion channels of various conductances in the picosiemens range. Two general models have been proposed to explain lipopeptide membrane activity: functioning in a detergent-like manner via solubilization of the lipid bilayer[12,13] and formation of transmembrane pores that lead to permeability changes[14,15]. The selectivity of FE has been significantly influenced by the environmental lipid composition of target cell membranes. It has been confirmed by microbiological tests[19] and studies performed using model systems[20]. The www.nature.com/scientificreports a c 0 b g, pS
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