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Atomic Force Microscopy Imaging and Force Spectroscopy of Supported Lipid Bilayers
Published on: July 22, 2015
Characterization of lipid chain order and dynamics in asymmetric membranes by solid-state NMR spectroscopy
Oskar Engberg1, Viola Döbel1, Kathrin M Engel1
1Institute of Medical Physics and Biophysics, University of Leipzig, Härtelstr. 16/18, D-4107 Leipzig, Germany. daniel.huster@medizin.uni-leipzig.de.
Abstract:
We studied the structure and dynamics of asymmetric POPCout/(POPE/POPG)in and POPSout/(POPE/POPG)in lipid membranes. To this end, the outer layer of multilamellar POPE/POPG (molar ratio 9 : 1) vesicles was exchanged (using methyl-β-cyclodextrin) by either chain deuterated POPC-d31 or POPS-d31, for which 2H NMR order parameters were measured. As controls, we prepared symmetric POPC-d31/POPE/POPG and POPS-d31/POPE/POPG membranes of the composition of just the outer membrane of the asymmetric multilamellar vesicles and pure POPC-d31 or POPS-d31 multilamellar vesicles. Compared to symmetric membranes of the same lipid composition, chain order parameters (S) of the asymmetric preparations were higher in the upper half of the chain and lower in the lower half. This reshuffling of acyl chain order is also expressed in higher 2H NMR Zeeman order relaxation rates (R1Z) of the chain segments in asymmetric membranes indicating alterations in the elastic properties of asymmetric bilayers as inferred from plots of R1Zvs. S2. Asymmetric membranes showed increased stiffness and rigidity although the lipid acyl chain composition between the inner and outer leaflets were identical. There were no indications for chain interdigitation between the two leaflets in the NMR spectra, which led us to speculate that the interleaflet coupling could be accomplished by sensing the differences in lipid packing densities between the two leaflets. These alterations in leaflet properties should have consequences for lipid protein interaction and ultimately protein function.
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