The antimicrobial peptide protegrin-1 (PG-1) interacts with membranes in a manner that strongly depends on membrane lipid composition. In this research we use an approach representing the outer layers of bacterial and red blood cell membranes with lipid monolayers and using a combination of insertion assay, epifluorescence microscopy, and surface x-ray scattering to gain a better understanding of antimicrobial peptide's mechanism of action. We find that PG-1 inserts readily into anionic dipalmitoyl-phosphatidylglycerol, palmitoyl-oleoyl-phosphatidylglycerol, and lipid A films, but significantly less so into zwitterionic dipalmitoyl-phosphatidylcholine, palmitoyl-oleoyl-phosphatidylcholine, and dipalmitoyl-phosphatidylethanolamine monolayers under similar experimental conditions. Epifluorescence microscopy shows that the insertion of PG-1 into the lipid layer results in the disordering of lipid packing; this disordering effect is corroborated by grazing incidence x-ray diffraction data. X-ray reflectivity measurements further point to the location of the peptide in the lipid matrix. In a pathologically relevant example we show that PG-1 completely destabilizes monolayer composed of lipid A, the major component in the outer membrane of Gram-negative bacteria, which is likely to be the mechanism by which PG-1 disrupts the outer membrane, thus allowing it to reach the target inner membrane.
We present a high-resolution x-ray study of the effects of disorder induced by random cross-linking side-chain smectic elastomers. The influence of variation of the concentration and stiffness of the cross-link units on the disruption of the one-dimensional translational order is reported in detail. Precise analysis of the line shape of the quasi-Bragg peaks associated with the smectic layering indicates a transition from algebraic decaying ordering to disorder. The smectic line shapes can be described by the Caillé correlation function convoluted with a finite-size factor represented by a stretched Gaussian (compressed exponential). The transition to disorder is signaled by a change in the exponent of the stretched Gaussian from 1 (simple Gaussian describing finite-size domains) via 0.5 (Lorentzian describing exponentially decaying short-range correlations) to <0.5 (stretched exponential correlations). For a flexible cross linker the changeover occurs for concentration between 0.15 and 0.20, for a stiff cross linker below about 0.10. Broadening of the higher harmonics of the x-ray peak indicates strong nonuniform strain within finite-size domains and local deformations induced by randomly distributed dislocations.
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