OpenLB
Open Library of Bioscience

The interactions of the antibiotic polymyxin B1 and its enzymatic cleavage product polymyxin B1 nonapeptide with phosphatidic acid monolayers and with bilayer membranes were investigated. Temperature-dependent pressure-area analysis of the monolayer reveals a linear increase of the lipid mean molecular area in the liquid condensed state for polymyxin concentrations between 10(-8) and 4 x 10(-7) M. Depending on the surface pressure, the area increase amounts to 30-70 A2. A linear dependence was also observed in the liquid expanded state but saturation is reached already at 10(-7) M polymyxin. The adsorption of polymyxin to phosphatidic acid bilayers is also linear and of a Langmuir type. Saturation is reached at a 1:4 polymyxin/lipid molar ratio. Polymyxin induces a phase separation in phosphatidic acid monolayers which was concluded from the thermotropic phase transition curves. In agreement with earlier bilayer experiments a second lowered phase transition appears in the presence of polymyxin. These fluidized domains again exhibit a linear polymyxin uptake comparable to the one of the liquid expanded monolayer at a temperature, where the undisturbed lipid is still in the condensed state. Polymyxin nonapeptide also causes an expansion of phosphatidic acid monolayers but only by maximally 10 A2. The thermotropic phase transition of the monolayer is reduced and considerably broadened by the nonapeptide. In phosphatidic acid bilayers we observed a decrease of the lipid phase transition temperature by 24 degrees C. The lateral chain packing is considerably disturbed by the peptide part of polymyxin.(ABSTRACT TRUNCATED AT 250 WORDS)