% IMPORTANT: The following is UTF-8 encoded.  This means that in the presence
% of non-ASCII characters, it will not work with BibTeX 0.99 or older.
% Instead, you should use an up-to-date BibTeX implementation like “bibtex8” or
% “biber”.

@ARTICLE{Fatafta:902425,
      author       = {Fatafta, Hebah and Kav, Batuhan and Bundschuh, Bastian F.
                      and Loschwitz, Jennifer and Strodel, Birgit},
      title        = {{D}isorder-to-order transition of the amyloid-β peptide
                      upon lipid binding},
      journal      = {Biophysical chemistry},
      volume       = {280},
      issn         = {0301-4622},
      address      = {Amsterdam [u.a.]},
      publisher    = {Elsevier Science},
      reportid     = {FZJ-2021-04247},
      pages        = {106700 -},
      year         = {2022},
      abstract     = {There is mounting evidence that Alzheimer's disease
                      progression and severity are linked to neuronal membrane
                      damage caused by aggregates of the amyloid- (A) peptide.
                      However, the detailed mechanism behind the membrane damage
                      is not well understood yet. Recently, the lipid-chaperone
                      hypothesis has been put forward, based on which the
                      formation of complexes between A and free lipids enables an
                      easy insertion of A into membranes. In order to test this
                      hypothesis, we performed numerous all-atom molecular
                      dynamics simulations. We studied the complex formation
                      between individual lipids, considering both POPC and DPPC,
                      and A and examined whether the resulting complexes would be
                      able to insert into lipid membranes. Complex formation at a
                      one-to-one ratio was readily observed, yet with minimal
                      effects on A's characteristics. Most importantly, the
                      peptide remains largely disordered in 1:1 complexes, and the
                      complex does not insert into the membrane; instead, it is
                      adsorbed to the membrane surface. The results change
                      considerably once A forms a complex with a POPC cluster
                      composed of three lipid molecules. The hydrophobic
                      interactions between A and the lipid tails cause the peptide
                      to fold into either a helical or a -sheet structure. These
                      observations provide atomic insight into the
                      disorder-to-order transition that is needed for membrane
                      insertion or amyloid aggregation to proceed.},
      cin          = {IBI-7},
      ddc          = {540},
      cid          = {I:(DE-Juel1)IBI-7-20200312},
      pnm          = {5244 - Information Processing in Neuronal Networks
                      (POF4-524)},
      pid          = {G:(DE-HGF)POF4-5244},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {34784548},
      UT           = {WOS:000722063800001},
      doi          = {10.1016/j.bpc.2021.106700},
      url          = {https://juser.fz-juelich.de/record/902425},
}