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@ARTICLE{Krugmann:885825,
      author       = {Krugmann, Benjamin and Radulescu, Aurel and Appavou,
                      Marie-Sousai and Koutsioumpas, Alexandros and Stingaciu,
                      Laura R. and Dulle, Martin and Förster, Stephan and
                      Stadler, Andreas M.},
      title        = {{M}embrane stiffness and myelin basic protein binding
                      strength as molecular origin of multiple sclerosis},
      journal      = {Scientific reports},
      volume       = {10},
      number       = {1},
      issn         = {2045-2322},
      address      = {[London]},
      publisher    = {Macmillan Publishers Limited, part of Springer Nature},
      reportid     = {FZJ-2020-04116},
      pages        = {16691},
      year         = {2020},
      abstract     = {Myelin basic protein (MBP) and its interaction with lipids
                      of the myelin sheath plays an important part in the
                      pathology of multiple sclerosis (MS). Previous studies
                      observed that changes in the myelin lipid composition lead
                      to instabilities and enhanced local curvature of MBP-lipid
                      multilayer structures. We investigated the molecular origin
                      of the instability and found that the diseased lipid
                      membrane has a $25\%$ lower bending rigidity, thus
                      destabilizing smooth >1µm curvature radius structures such
                      as in giant unilamellar vesicles. MBP-mediated assembling of
                      lipid bilayers proceeds in two steps, with a slow second
                      step occurring over many days where native lipid membranes
                      assemble into well-defined multilayer structures, whereas
                      diseased lipid membranes form folded assemblies with high
                      local curvature. For both native and diseased lipid mixtures
                      we find that MBP forms dense liquid phases on top of the
                      lipid membranes mediating attractive membrane interactions.
                      Furthermore, we observe MBP to insert into its bilayer
                      leaflet side in case of the diseased lipid mixture, whereas
                      there is no insertion for the native mixture. Insertion
                      increases the local membrane curvature, and could be caused
                      by a decrease of the sphingomyelin content of the diseased
                      lipid mixture. These findings can help to open a pathway to
                      remyelination strategies.},
      cin          = {JCNS-FRM-II / JCNS-1 / MLZ},
      ddc          = {600},
      cid          = {I:(DE-Juel1)JCNS-FRM-II-20110218 /
                      I:(DE-Juel1)JCNS-1-20110106 / I:(DE-588b)4597118-3},
      pnm          = {6G4 - Jülich Centre for Neutron Research (JCNS) (POF3-623)
                      / 6G15 - FRM II / MLZ (POF3-6G15) / 6215 - Soft Matter,
                      Health and Life Sciences (POF3-621)},
      pid          = {G:(DE-HGF)POF3-6G4 / G:(DE-HGF)POF3-6G15 /
                      G:(DE-HGF)POF3-6215},
      experiment   = {EXP:(DE-MLZ)KWS2-20140101 / EXP:(DE-MLZ)MARIA-20140101 /
                      EXP:(DE-Juel1)SNS-NSE-20150203 /
                      EXP:(DE-MLZ)TEM-MLZ-20151210},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:33028889},
      UT           = {WOS:000577449800036},
      doi          = {10.1038/s41598-020-73671-3},
      url          = {https://juser.fz-juelich.de/record/885825},
}