lanthiopeptin and 1-2-oleoylphosphatidylcholine

The interaction between the cinnamycin and the biomimetic membranes was studied using the atomic force microscope(AFM). The bilayer was composed of the monolayer tethered on the gold surface and the outer layer fused with the vesicles on the monolayer. The vesicles were prepared at the desired ratio of dioleoylphosphatidylethanolamine(DOPE) to dioleoylphosphatidylcholine(DOPC). On the bilayer, the surface force measurement was performed with the cinnamycin immobilized covalently on the tip surface. The immobilization led to the presence of the adhesion, which was found while the tip was retracted from the bilayer. In addition, the magnitude of the adhesive force was changed with respect to the composition of DOPE in the outer layer. The difference in the adhesion may be attributed to the mean-molecular-area of DOPE and the specific-binding density on the outer layer. Furthermore, the analysis of the rupture force with respect to the loading rate indicated that the rupture length was around 0.1∼0.13 nm, which was similar to that of a van der Waals bond.

Topics: Bacteriocins; Biomimetic Materials; Lipid Bilayers; Membranes, Artificial; Peptides, Cyclic; Phosphatidylcholines; Phosphatidylethanolamines

The binding of the cinnamycin on the biomimetic membrane was studied with respect to time using the surface plasmon resonance(SPR). The membrane was composed of the inner layer tethered on the gold surface and the outer layer formed on the inner layer, which was at the desired ratio of dioleoylphosphatidylethanolamine(DOPE) to dioleoylphosphatidyl- choline(DOPC). On the bilayer, the cinnamycin solution was injected and showed different behavior of the binding with respect to time up on its concentration. For kinetic analysis, the behavior was converted to the coverage fraction with respect to time, which was ratio to the saturated response of 5 μM cinnamycin solution. The fraction change with respect to time was function of the available-site, which was eventually the subtraction of the fraction from one. With the fitting of the first order of the available site, the rate constant was acquired into 6∼7 × 10

Topics: Adsorption; Bacteriocins; Kinetics; Membranes, Artificial; Peptides, Cyclic; Phosphatidylcholines; Phosphatidylethanolamines; Surface Plasmon Resonance; Thermodynamics

Asymmetric lipid giant vesicles have been used to model the biochemical reactions in cell membranes. However, methods for producing asymmetric giant vesicles lead to the inclusion of an organic solvent layer that affects the mechanical and physical characteristics of the membrane. Here we describe the formation of asymmetric giant vesicles that include little organic solvent, and use them to investigate the dynamic responses of lipid molecules in the vesicle membrane. We formed the giant vesicles via the inhomogeneous break-up of a lipid microtube generated by applying a jet flow to an asymmetric planar lipid bilayer. The asymmetric giant vesicles showed a lipid flip-flop behaviour in the membrane, superficially similar to the lipid flip-flop activity observed in apoptotic cells. In vitro synthesis of membrane proteins into the asymmetric giant vesicles revealed that the lipid asymmetry in bilayer membranes improves the reconstitution ratio of membrane proteins. Our asymmetric giant vesicles will be useful in elucidating lipid-lipid and lipid-membrane protein interactions involved in the regulation of cellular functions.

Topics: 1,2-Dipalmitoylphosphatidylcholine; Alkanes; Bacteriocins; Connexin 43; Fluorescent Dyes; Lipid Bilayers; Particle Size; Peptides, Cyclic; Phosphatidylcholines; Phosphatidylserines; Rhodamines; Unilamellar Liposomes