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@ARTICLE{Poojari:202185,
      author       = {Poojari, Chetan},
      title        = {{A}ggregation of {A}myloids at {B}iomembranes and its
                      {I}mplications in {A}lzheimers's {D}isease and {T}ype {II}
                      {D}iabetes},
      journal      = {Biophysical journal},
      volume       = {104},
      number       = {2},
      issn         = {0006-3495},
      address      = {New York, NY},
      publisher    = {Rockefeller Univ. Press},
      reportid     = {FZJ-2015-04474},
      pages        = {592a -},
      year         = {2013},
      abstract     = {The aggregation of the amyloid-β peptide (Aβ) into
                      neurotoxic oligomers on the neuronal membrane surface and
                      its insertion into the membrane is considered to be a
                      crucial event in the development of Alzheimer's disease
                      (AD). However, the mechanism of insertion, pore formation
                      and membrane disruption still needs to be uncovered. We used
                      atomistic molecular dynamics (MD) simulations to investigate
                      the behavior of Aβ in zwitterionic and anionic lipid
                      bilayers. We studied the effect of Aβ secondary structure,
                      oligomerization and mutation on its transmembrane stability
                      and membrane maintenance. Our main finding is that β
                      sheet-oligomerization is required for Aβto be stable in the
                      membrane and to induce membrane permeabilization.Aggregation
                      of human islet amyloid polypeptide (hIAPP) at beta-cell
                      membranes is associated with the onset of type II diabetes.
                      It is proposed that hIAPP aggregates induce cytotoxicity to
                      the pancreatic islets of langerhans cells by membrane
                      disruption. Chiral surface-specific vibrational sum
                      frequency generation (SFG) spectroscopy in conjunction with
                      ab initio simulations revealed a tilted orientation of hIAPP
                      β sheet-aggregates at lipid/aqueous interfaces. We used
                      this orientation for the starting structure of a hIAPP
                      trimer inserted into a lipid bilayer and followed its
                      effects on membrane maintenance using MD simulations. We
                      observe β barrel-formation, which allows massive water and
                      even ion flow across the membrane.},
      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:000316074305536},
      doi          = {10.1016/j.bpj.2012.11.3291},
      url          = {https://juser.fz-juelich.de/record/202185},
}