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@ARTICLE{Thomaier:823945,
      author       = {Thomaier, Maren and Gremer, Lothar and Dammers, Christina
                      and Fabig, Judith and Neudecker, Philipp and Willbold,
                      Dieter},
      title        = {{H}igh-{A}ffinity {B}inding of {M}onomeric but {N}ot
                      {O}ligomeric {A}myloid-β to {G}anglioside {GM}1
                      {C}ontaining {N}anodiscs},
      journal      = {Biochemistry},
      volume       = {55},
      number       = {48},
      issn         = {1520-4995},
      address      = {Columbus, Ohio},
      publisher    = {American Chemical Society},
      reportid     = {FZJ-2016-06573},
      pages        = {6662-6672},
      year         = {2016},
      abstract     = {The interaction of the amyloid-β protein (Aβ) with
                      neuronal cell membranes plays a crucial role in
                      Alzheimer’s disease. Aβ undergoes structural changes upon
                      binding to ganglioside GM1 containing membranes leading to
                      altered molecular characteristics of the protein. The
                      physiological role of the Aβ interaction with the
                      ganglioside GM1 is still unclear. In order to further
                      elucidate the molecular requirements of Aβ membrane
                      binding, we tested different nanodiscs varying in their
                      lipid composition, regarding the charge of the headgroups as
                      well as ganglioside GM1 concentration. Nanodiscs are
                      excellent model membrane systems for studying protein
                      membrane interactions, and we show here their suitability to
                      investigate the membrane interaction of Aβ. In particular,
                      we set out to investigate whether the binding activity of
                      GM1 to Aβ is specific for the assembly state of Aβ and
                      compared the binding affinities of monomeric with oligomeric
                      Aβ. Using fluorescence titration experiments, we
                      demonstrate high-affinity binding of Aβ(1−40) to GM1
                      containing nanodiscs, with dissociation constants, KD, in
                      the range from 25 to 41 nM, in a GM1 concentration-dependent
                      manner. Biolayer interferometry experiments confirmed the
                      high-affinity binding of monomeric Aβ(1−40) (KD of 24 nM
                      to 49 nM) as well as of Aβ(1−42) (KD of 30 nM) to GM1
                      containing nanodiscs, and no binding to phospholipid
                      containing nanodiscs. Interestingly, and in contrast to
                      monomeric Aβ, neither oligomeric Aβ(1−40) nor oligomeric
                      Aβ(1−42) binds to GM1 nanodiscs. To the best of our
                      knowledge, this is the first report of a loss of function
                      for monomeric Aβ upon aggregation.},
      cin          = {ICS-6},
      ddc          = {570},
      cid          = {I:(DE-Juel1)ICS-6-20110106},
      pnm          = {553 - Physical Basis of Diseases (POF3-553)},
      pid          = {G:(DE-HGF)POF3-553},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000389557300008},
      pubmed       = {pmid:27933798},
      doi          = {10.1021/acs.biochem.6b00829},
      url          = {https://juser.fz-juelich.de/record/823945},
}