% IMPORTANT: The following is UTF-8 encoded.  This means that in the presence
% of non-ASCII characters, it will not work with BibTeX 0.99 or older.
% Instead, you should use an up-to-date BibTeX implementation like “bibtex8” or
% “biber”.

@ARTICLE{Olubiyi:153348,
      author       = {Olubiyi, Olujide and Frenzel, Daniel and Bartnik, Dirk and
                      Glück, Julian and Brener, O. and Nagel-Steger, Luitgard and
                      Funke, S. A. and Willbold, Dieter and Strodel, Birgit},
      title        = {{A}myloid {A}ggregation {I}nhibitory {M}echanism of
                      {A}rginine-rich {D}-peptides},
      journal      = {Current medicinal chemistry},
      volume       = {21},
      issn         = {1875-533X},
      address      = {Hilversum [u.a.]},
      publisher    = {Bentham Science Publ.},
      reportid     = {FZJ-2014-02980},
      pages        = {1448-1457},
      year         = {2014},
      note         = {Campus-weite Veröffentlichung erwünschtD. Willbold und B.
                      Strodel sind beide "Corresponding Authors".},
      abstract     = {It is widely believed that Alzheimer's disease pathogenesis
                      is driven by the production and deposition of the amyloid-β
                      peptide (Aβ) in the brain. In this study, we employ a
                      combination of in silico and in vitro approaches to
                      investigate the inhibitory properties of selected
                      arginine-rich D-enantiomeric peptides (D-peptides) against
                      amyloid aggregation. The D-peptides include D3, a 12-residue
                      peptide with anti-amyloid potencies demonstrated in vitro
                      and in vivo, RD2, a scrambled sequence of D3, as well as
                      truncated RD2 variants. Using a global optimization method
                      together with binding free energy calculations followed by
                      molecular dynamics simulations, we perform a detailed
                      analysis of D-peptide binding to Aβ monomer and a fibrillar
                      Aβ structure. Results obtained from both molecular
                      simulations and surface plasmon resonance experiments reveal
                      a strong binding of D3 and RD2 to Aβ, leading to a
                      significant reduction in the amount of β structures in both
                      monomer and fibril, which was also demonstrated in
                      Thioflavin T assays. The binding of the D-peptides to Aβ is
                      driven by electrostatic interactions, mostly involving the
                      D-arginine residues and Glu11, Glu22 and Asp23 of Aβ.
                      Furthermore, we show that the anti-amyloid activities of the
                      D-peptides depend on the length and sequence of the
                      Dpeptide, its ability to form multiple weak hydrophobic
                      interactions with Aβ, as well as the Aβ oligomer size.},
      cin          = {ICS-6},
      ddc          = {540},
      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:000333274400005},
      url          = {https://juser.fz-juelich.de/record/153348},
}