title: The Molecular Structure of Human Red Blood Cell Membranes from Highly Oriented, Solid Supported Multi-Lamellar Membranes.
abstract: We prepared highly oriented, multi-lamellar stacks of human red blood cell (RBC) membranes applied on silicon wafers. RBC ghosts were prepared by hemolysis and applied onto functionalized silicon chips and annealed into multi-lamellar RBC membranes. High resolution X-ray diffraction was used to determine the molecular structure of the stacked membranes. We present direct experimental evidence that these RBC membranes consist of nanometer sized domains of integral coiled-coil peptides, as well as liquid ordered (lo) and liquid disordered (ld) lipids. Lamellar spacings, membrane and hydration water layer thicknesses, areas per lipid tail and domain sizes were determined. The common drug aspirin was added to the RBC membranes and found to interact with RBC membranes and preferably partition in the head group region of the lodomain leading to a fluidification of the membranes, i.e., a thinning of the bilayers and an increase in lipid tail spacing. Our results further support current models of RBC membranes as patchy structures and provide unprecedented structural details of the molecular organization in the different domains.
authors.affiliation: Department of Physics and Astronomy, McMaster University, Hamilton, ON, Canada.|Department of Experimental Physics, Saarland University, Saarbrücken, Germany.
authors.forename: Sebastian
authors.initials: S
authors.lastname: Himbert
authors.affiliation: Department of Physics and Astronomy, McMaster University, Hamilton, ON, Canada.
authors.forename: Richard J
authors.initials: RJ
authors.lastname: Alsop
authors.affiliation: Department of Physics and Astronomy, McMaster University, Hamilton, ON, Canada.
authors.forename: Markus
authors.initials: M
authors.lastname: Rose
authors.affiliation: Research Center for Molecular Imaging and Screening, Saarland University, Homburg/Saar, Germany.
authors.forename: Laura
authors.initials: L
authors.lastname: Hertz
authors.affiliation: Department of Physics and Astronomy, McMaster University, Hamilton, ON, Canada.
authors.forename: Alexander
authors.initials: A
authors.lastname: Dhaliwal
authors.affiliation: Department of Chemistry and Chemical Biology, McMaster University, Hamilton, ON, Canada.
authors.forename: Jose M
authors.initials: JM
authors.lastname: Moran-Mirabal
authors.affiliation: Department of Pathology and Molecular Medicine, McMaster University, Hamilton, Canada.|McMaster Immunology Research Center, McMaster University, Hamilton, Canada.|Michael G. DeGroote Institute for Infectious Disease Research, McMaster University, Hamilton, Canada.
authors.forename: Chris P
authors.initials: CP
authors.lastname: Verschoor
authors.affiliation: Department of Pathology and Molecular Medicine, McMaster University, Hamilton, Canada.|McMaster Immunology Research Center, McMaster University, Hamilton, Canada.|Michael G. DeGroote Institute for Infectious Disease Research, McMaster University, Hamilton, Canada.
authors.forename: Dawn M E
authors.initials: DM
authors.lastname: Bowdish
authors.affiliation: Research Center for Molecular Imaging and Screening, Saarland University, Homburg/Saar, Germany.|Department of Experimental Physics, Saarland University, Saarbrücken, Germany.
authors.forename: Lars
authors.initials: L
authors.lastname: Kaestner
authors.affiliation: Department of Experimental Physics, Saarland University, Saarbrücken, Germany.
authors.forename: Christian
authors.initials: C
authors.lastname: Wagner
authors.affiliation: Department of Physics and Astronomy, McMaster University, Hamilton, ON, Canada.
authors.forename: Maikel C
authors.initials: MC
authors.lastname: Rheinstädter
mesh_terms: D001241:Aspirin / Q000008:administration & dosage; D004910:Erythrocyte Membrane / Q000737:chemistry* / Q000187:drug effects; D006801:Humans; D015394:Molecular Structure; D012825:Silicon / Q000737:chemistry; D014961:X-Ray Diffraction
chemical_list: D001241:Aspirin; D012825:Silicon