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@ARTICLE{Dammers:279274,
      author       = {Dammers, Christina and Gremer, Lothar and Reiß, Kerstin
                      and Klein, Antonia N. and Neudecker, Philipp and Hartmann,
                      Rudolf and Sun, Na and Demuth, Hans-Ulrich and Schwarten,
                      Melanie and Willbold, Dieter},
      title        = {{S}tructural {A}nalysis and {A}ggregation {P}ropensity of
                      {P}yroglutamate {A}β(3-40) in {A}queous {T}rifluoroethanol},
      journal      = {PLoS one},
      volume       = {10},
      number       = {11},
      issn         = {1932-6203},
      address      = {Lawrence, Kan.},
      publisher    = {PLoS},
      reportid     = {FZJ-2015-07289},
      pages        = {e0143647},
      year         = {2015},
      abstract     = {A hallmark of Alzheimer’s disease (AD) is the
                      accumulation of extracellular amyloid-β (Aβ) plaques in
                      the brains of patients. N-terminally truncated
                      pyroglutamate-modified Aβ (pEAβ) has been described as a
                      major compound of Aβ species in senile plaques. pEAβ is
                      more resistant to degradation, shows higher toxicity and has
                      increased aggregation propensity and β-sheet stabilization
                      compared to non-modified Aβ. Here we characterized
                      recombinant pEAβ(3–40) in aqueous trifluoroethanol (TFE)
                      solution regarding its aggregation propensity and structural
                      changes in comparison to its non-pyroglutamate-modified
                      variant Aβ(1–40). Secondary structure analysis by
                      circular dichroism spectroscopy suggests that pEAβ(3–40)
                      shows an increased tendency to form β-sheet-rich structures
                      in $20\%$ TFE containing solutions where Aβ(1–40) forms
                      α-helices. Aggregation kinetics of pEAβ(3–40) in the
                      presence of $20\%$ TFE monitored by thioflavin-T (ThT) assay
                      showed a typical sigmoidal aggregation in contrast to
                      Aβ(1–40), which lacks ThT positive structures under the
                      same conditions. Transmission electron microscopy confirms
                      that pEAβ(3–40) aggregated to large fibrils and high
                      molecular weight aggregates in spite of the presence of the
                      helix stabilizing co-solvent TFE. High resolution NMR
                      spectroscopy of recombinantly produced and uniformly isotope
                      labeled [U-15N]-pEAβ(3–40) in TFE containing solutions
                      indicates that the pyroglutamate formation affects
                      significantly the N-terminal region, which in turn leads to
                      decreased monomer stability and increased aggregation
                      propensity.},
      cin          = {ICS-6},
      ddc          = {500},
      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:000365853900151},
      pubmed       = {pmid:26600248},
      doi          = {10.1371/journal.pone.0143647},
      url          = {https://juser.fz-juelich.de/record/279274},
}