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@ARTICLE{Poojari:140001,
      author       = {Poojari, Chetan and Xiao, D. and Batista, V. S. and
                      Strodel, Birgit},
      title        = {{M}embrane {P}ermeation {I}nduced by {A}ggregates of
                      {H}uman {I}slet {A}myloid {P}olypeptides},
      journal      = {Biophysical journal},
      volume       = {105},
      issn         = {0006-3495},
      address      = {New York, NY},
      publisher    = {Rockefeller Univ. Press},
      reportid     = {FZJ-2013-05968},
      pages        = {2323-2332},
      year         = {2013},
      abstract     = {Several neurodegenerative diseases such as Alzheimer’s
                      and Parkinson’s diseases as well as nonneuropathic
                      diseases such as type II diabetes and atrial amyloidosis are
                      associated with aggregation of amyloid polypeptides into
                      fibrillar structures, or plaques. In this study, we use
                      molecular dynamics simulations to test the stability and
                      orientation of membrane-embedded aggregates of the human
                      islet amyloid polypeptide (hIAPP) implicated in type II
                      diabetes. We find that in both monolayers and bilayers of
                      dipalmitoylphosphatidylglycerol (DPPG) hIAPP trimers and
                      tetramers remain inside the membranes and preserve their
                      β-sheet secondary structure. Lipid bilayer-inserted hIAPP
                      trimers and tetramers orient inside DPPG at 60° relative to
                      the membrane/water interface and lead to water permeation
                      and Na+ intrusion, consistent with ion-toxicity in islet
                      β-cells. In particular, hIAPP trimers form a water-filled
                      β-sandwich that induce water permeability comparable with
                      channel-forming proteins, such as aquaporins and
                      gramicidin-A. The predicted disruptive orientation is
                      consistent with the amphiphilic properties of the hIAPP
                      aggregates and could be probed by chiral sum frequency
                      generation (SFG) spectroscopy, as predicted by the simulated
                      SFG spectra.},
      cin          = {ICS-6},
      ddc          = {570},
      cid          = {I:(DE-Juel1)ICS-6-20110106},
      pnm          = {452 - Structural Biology (POF2-452)},
      pid          = {G:(DE-HGF)POF2-452},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000327285100013},
      pubmed       = {pmid:24268144},
      doi          = {10.1016/j.bpj.2013.09.045},
      url          = {https://juser.fz-juelich.de/record/140001},
}