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@ARTICLE{Samantray:902427,
      author       = {Samantray, Suman and Strodel, Birgit},
      title        = {{T}he {E}ffects of {D}ifferent {G}lycosaminoglycans on the
                      {S}tructure and {A}ggregation of the {A}myloid-β (16–22)
                      {P}eptide},
      journal      = {The journal of physical chemistry / B},
      volume       = {125},
      number       = {21},
      issn         = {1089-5647},
      address      = {Washington, DC},
      publisher    = {Soc.},
      reportid     = {FZJ-2021-04249},
      pages        = {5511 - 5525},
      year         = {2021},
      note         = {Kein Post-print vorhanden!},
      abstract     = {Aggregates of the amyloid-β (Aβ) peptide are implicated
                      as a causative substance in Alzheimer’s disease. Molecular
                      dynamics simulations provide valuable contributions for
                      elucidating the conformational transitions of monomeric and
                      aggregated forms of Aβ be it in solution or in the presence
                      of other molecules. Here, we study the effects of four
                      different glycosaminoglycans (GAGs), three sulfated ones and
                      a nonsulfated one, on the aggregation of Aβ16–22. From
                      experiments, it has been suggested that GAGs, which belong
                      to the main components of the brain’s extracellular space,
                      favor amyloid fibril formation. Our simulation results
                      reveal that the binding of Aβ16–22 to the GAGs is driven
                      by electrostatic attraction between the negative GAG charges
                      and the positively charged K16 of Aβ16–22. While these
                      interactions have only minor effects on the GAG and
                      Aβ16–22 conformations at the 1 Aβ16–22/1 GAG ratio, at
                      the 2:2 stoichiometry the aggregation of Aβ16–22 is
                      considerably changed. In solution, the aggregation of
                      Aβ16–22 is strongly influenced by K16–E22 attraction,
                      leading to antiparallel β-sheets. In the presence of GAGs,
                      on the other hand, the interaction of K16 with the GAGs
                      increases the importance of the hydrophobic interactions
                      during Aβ16–22 aggregation, which in turn yields parallel
                      alignments. A templating and ordering effect of the GAGs on
                      the Aβ16–22 aggregates is observed. In summary, this
                      study provides new insight at the atomic level on
                      GAG–amyloid interactions, strengthening the view that
                      sulfation of the GAGs plays a major role in this context.},
      cin          = {IBI-7},
      ddc          = {530},
      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       = {34027669},
      UT           = {WOS:000661116600007},
      doi          = {10.1021/acs.jpcb.1c00868},
      url          = {https://juser.fz-juelich.de/record/902427},
}