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Alamethicin Aggregation In Lipid Membranes., Jianjun Pan, Stephanie Tristram-Nagle, John Nagle
Alamethicin Aggregation In Lipid Membranes., Jianjun Pan, Stephanie Tristram-Nagle, John Nagle
Prof. Stephanie Tristram-Nagle Ph.D.
X-ray scattering features induced by aggregates of alamethicin (Alm) were obtained in oriented stacks of model membranes of DOPC(diC18:1PC) and diC22:1PC. The first feature obtained near full hydration was Bragg rod in-plane scattering near 0.11 A(-1) in DOPC and near 0.08 A(-1) in diC22:1PC at a 1:10 Alm:lipid ratio. This feature is interpreted as bundles consisting of n Alm monomers in a barrel-stave configuration surrounding a water pore. Fitting the scattering data to previously published molecular dynamics simulations indicates that the number of peptides per bundle is n = 6 in DOPC and n >or= 9 in diC22:1PC. The larger …
Alamethicin In Lipid Bilayers: Combined Use Of X-Ray Scattering And Md Simulations, Jianjun Pan, D. Peter Tieleman, John F. Nagle, Norbert Kučerka, Prof. Stephanie Tristram-Nagle Ph.D.
Alamethicin In Lipid Bilayers: Combined Use Of X-Ray Scattering And Md Simulations, Jianjun Pan, D. Peter Tieleman, John F. Nagle, Norbert Kučerka, Prof. Stephanie Tristram-Nagle Ph.D.
Prof. Stephanie Tristram-Nagle Ph.D.
We study fully hydrated bilayers of two di-monounsaturated phospholipids diC18:1PC (DOPC) and diC22:1PC with varying amounts of alamethicin (Alm). We combine the use of X-ray diffuse scattering and molecular dynamics simulations to determine the orientation of alamethicin in model lipids. Comparison of the experimental and simulated form factors shows that Alm helices are inserted transmembrane at high humidity and high concentrations, in agreement with earlier results. The X-ray scattering data and the MD simulations agree that membrane thickness changes very little up to 1/10 Alm/ DOPC. In contrast, the X-ray data indicate that the thicker diC22:1PC membrane thins with added …