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@ARTICLE{Strodel:12607,
      author       = {Strodel, B. and Lee, J.W.L. and Whittleston, C.S. and
                      Wales, D.J.},
      title        = {{T}ransmembrane {S}tructures for {A}lzheimer’s {A}ß1-42
                      {O}ligomers},
      journal      = {Journal of the American Chemical Society},
      volume       = {132},
      issn         = {0002-7863},
      address      = {Washington, DC},
      publisher    = {American Chemical Society},
      reportid     = {PreJuSER-12607},
      pages        = {13300 - 13312},
      year         = {2010},
      note         = {B.S. gratefully acknowledges the Julich Supercomputing
                      Centre for providing and maintaining the computing resources
                      used in this work. C.S.W. thanks the EPSRC for financial
                      support.},
      abstract     = {We model oligomers of the Alzheimer's amyloid β-peptide
                      Aβ(1-42) in an implicit membrane to obtain insight into the
                      mechanism of amyloid toxicity. It has been suggested that
                      Aβ oligomers are the toxic species, causing membrane
                      disruption in neuronal cells due to pore formation. We use
                      basin-hopping global optimization to identify the most
                      stable structures for the Aβ(1-42) peptide monomer and
                      small oligomers up to the octamer inserted into a lipid
                      bilayer. To improve the efficacy of the basin-hopping
                      approach, we introduce a basin-hopping parallel tempering
                      scheme and an oligomer generation procedure. The most stable
                      membrane-spanning structure for the monomer is identified as
                      a β-sheet, which exhibits the typical strand-turn-strand
                      motif observed in NMR experiments. We find ordered β-sheets
                      for the dimer to the hexamer, whereas for the octamer, we
                      observe that the ordered structures separate into distinct
                      tetrameric units that are rotated or shifted with respect to
                      each other. This effect leads to an increase in favorable
                      peptide-peptide interactions, thereby stabilizing the
                      membrane-inserted octamer. On the basis of these results, we
                      suggest that Aβ pores may consist of tetrameric and
                      hexameric β-sheet subunits. These Aβ pore models are
                      consistent with the results of biophysical and biochemical
                      experiments.},
      keywords     = {Amyloid beta-Peptides: chemistry / Biopolymers: chemistry /
                      Models, Molecular / Nuclear Magnetic Resonance, Biomolecular
                      / Peptide Fragments: chemistry / Protein Conformation /
                      Thermodynamics / Amyloid beta-Peptides (NLM Chemicals) /
                      Biopolymers (NLM Chemicals) / Peptide Fragments (NLM
                      Chemicals) / amyloid beta-protein (1-42) (NLM Chemicals) / J
                      (WoSType)},
      cin          = {ISB-3},
      ddc          = {540},
      cid          = {I:(DE-Juel1)VDB942},
      pnm          = {Funktion und Dysfunktion des Nervensystems / BioSoft:
                      Makromolekulare Systeme und biologische
                      Informationsverarbeitung},
      pid          = {G:(DE-Juel1)FUEK409 / G:(DE-Juel1)FUEK505},
      shelfmark    = {Chemistry, Multidisciplinary},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:20822103},
      UT           = {WOS:000282304000055},
      doi          = {10.1021/ja103725c},
      url          = {https://juser.fz-juelich.de/record/12607},
}