In this work, we present the first characterization of the cell lysing mechanism of MSI-78, an antimicrobial peptide. MSI-78 is an amphipathic alpha-helical peptide designed by Genaera Corporation as a synthetic analog to peptides from the magainin family. (31)P-NMR of mechanically aligned samples and differential scanning calorimetry (DSC) were used to study peptide-containing lipid bilayers. ...

We investigate using Monte Carlo simulations in the NPT ensemble the self-assembly of disk-coil macromolecules with stacking interactions. The disk-coil molecules are composed of a planar disk that is covalently bonded to a single coil. In addition to commonly used amphiphilic interactions between the disk and coil portion of the molecules, we employ an attractive interaction between central mo...

Tapping mode atomic force microscopy was used to investigate the lamellar morphology of poly(l-lactide) and two poly(l-lactide-co-meso-lactide) random copolymers containing 3% and 6% meso-lactide. Samples were isothermally crystallized at selected temperatures, and qualitative and quantitative analyses of lamellar structure were performed using height and phase images. This is the first study o...

In a diblock copolymer system the free energy field depends non-locally on the monomerdensity field. In addition there are two positive parameters in the constitutive relation. One ofthem is small with respect to which we do singular perturbation analysis. The second one isof order 1 with respect to which we do bifurcation analysis. Combining the two techniques wefind wriggl...

Typical SAXS profiles and lamellar spacing d as a function of shear rate for the system with B/H=0.30 at T=25◦C are shown in fig. 1. This systems shows the orientation transition at γ̇c/a=300s −1 (see Fig. 6 in the main text). Lamellar spacing d at B/H=0.30 slightly decreases with increase in the shear rate, while at B/H=0.32 it slightly reduces at low shear rate and stays almost constant at hig...

phosphatidate phosphohydrolase (pap2b, fraction b) was purified from the plasma membrane ofrat liver cells. the km for the surface concentration of phosphatidic acid was 0.43 mol%. the subunit of theenzyme had an m.w. of 33.8 kda using sodium dodecyl sulfate polyacrylamide gel electrophoresis. thenative enzyme shows a molecular weight of 182 kda in a gel filtration column packed with sephacryl ...