The Molecular Structure of Human Red Blood Cell Membranes from Highly Oriented, Solid Supported Multi-Lamellar Membranes
Autor: | Richard J. Alsop, Laura Hertz, Lars Kaestner, Chris P. Verschoor, Sebastian Himbert, Dawn M. E. Bowdish, Maikel C. Rheinstädter, Markus Rose, Christian Wagner, Alexander Dhaliwal, Jose M. Moran-Mirabal |
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Jazyk: | angličtina |
Rok vydání: | 2019 |
Předmět: |
0301 basic medicine
Silicon Materials science chemistry.chemical_element 02 engineering and technology Article 03 medical and health sciences X-Ray Diffraction medicine Molecule Humans Lamellar structure Multidisciplinary Aspirin Molecular Structure Erythrocyte Membrane 021001 nanoscience & nanotechnology Red blood cell 030104 developmental biology medicine.anatomical_structure Membrane chemistry X-ray crystallography Biophysics Nanometre 0210 nano-technology Membrane biophysics |
Zdroj: | Scientific Reports |
DOI: | 10.22028/d291-29981 |
Popis: | 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 lo domain 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. |
Databáze: | OpenAIRE |
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