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@ARTICLE{Nath:1025423,
      author       = {Nath, Soumav and Buell, Alexander K. and Barz, Bogdan},
      title        = {{P}yroglutamate-modified amyloid β(3–42) monomer has
                      more β-sheet content than the amyloid β(1–42) monomer},
      journal      = {Physical chemistry, chemical physics},
      volume       = {25},
      number       = {24},
      issn         = {1463-9076},
      address      = {Cambridge},
      publisher    = {RSC Publ.},
      reportid     = {FZJ-2024-02882},
      pages        = {16483 - 16491},
      year         = {2023},
      abstract     = {The aggregation of the amyloid β (Aβ) peptide is a major
                      hallmark of Alzheimer's disease. This peptide can aggregate
                      into oligomers, proto-fibrils and mature fibrils, which
                      eventually assemble into amyloid plaques in vivo. Several
                      post-translational modifications lead to the presence of
                      different forms of the Aβ peptide in the amyloid plaques
                      with different biophysical and biochemical properties. While
                      the canonical forms Aβ(1–40) and Aβ(1–42) have been
                      found to be the major components of amyloid plaques,
                      N-terminally pyroglutamate-modified variants, specifically
                      pE-Aβ(3–42), amount to a significant fraction of the
                      total Aβ plaque content of AD brains. With increased
                      hydrophobicity, these variants display a more pronounced
                      aggregation behaviour in vitro which, together with their
                      higher stability against degradation in vivo is thought to
                      make them crucial molecular players in the aetiology of AD.
                      The peptide monomers are the smallest assembly units, and
                      play an important role in most of the individual molecular
                      processes involved in amyloid fibril formation, such as
                      primary and secondary nucleation and elongation.
                      Understanding the monomeric conformational ensembles of the
                      isoforms is important in unraveling observed differences in
                      their bio-physico-chemical properties. Here we use enhanced
                      and extensive molecular dynamics simulations to study the
                      structural flexibility of the N-terminally truncated
                      Pyroglutamate modified isomer of Aβ, pE-Aβ(3–42)
                      monomer, and compared it with simulations of the Aβ(1–42)
                      peptide monomer under the same conditions. We find
                      significant differences, especially in the secondary
                      structure and hydrophobic exposure, which might be
                      responsible for their different behaviour in biophysical
                      experiments.},
      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       = {37306611},
      UT           = {WOS:001004437400001},
      doi          = {10.1039/D2CP05961D},
      url          = {https://juser.fz-juelich.de/record/1025423},
}