% 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{Ziehm:848211,
      author       = {Ziehm, Tamar and Buell, Alexander K. and Willbold, Dieter},
      title        = {{T}he role of hydrophobicity and charge of amyloid-beta
                      oligomer eliminating {D}-peptides in the interaction with
                      amyloid-beta monomers},
      journal      = {ACS chemical neuroscience},
      volume       = {9},
      number       = {11},
      issn         = {1948-7193},
      address      = {Washington, DC},
      publisher    = {ACS Publ.},
      reportid     = {FZJ-2018-03473},
      pages        = {2679-2688},
      year         = {2018},
      abstract     = {Inhibition of the self-assembly process of amyloid-beta and
                      even more the removal of already existing toxic amyloid-beta
                      assemblies represent promising therapeutic strategies
                      against Alzheimer´s disease. To approach this aim, we
                      selected a D-enantiomeric peptide by phage-display based on
                      the interaction with amyloid-beta monomers. This lead
                      compound was successfully optimized by peptide microarrays
                      with respect to its affinity and specificity to the target
                      resulting in D-peptides with both increased hydrophobicity
                      and net charge. Here, we present a detailed biophysical
                      characterization of the interactions between these optimized
                      D peptides and amyloid-beta monomers in comparison to the
                      original lead compound in order to obtain a more thorough
                      understanding of the physico-chemical determinants of the
                      interactions. Kinetics and apparent stoichiometry of complex
                      formation were studied using surface plasmon resonance.
                      Potential modes of binding to amyloid-beta were identified
                      and the influences of ionic strength on complex stability,
                      as well as on the inhibitory effect on amyloid-beta
                      aggregation were investigated. The results reveal a very
                      different mode of interaction of the optimized D-peptides
                      based on a combination of electrostatic and hydrophobic
                      interactions as compared to the mostly electrostatically
                      driven interaction of the lead compound. These conclusions
                      were supported by the thermodynamic profiles of the
                      interaction between optimized D-peptides and Aβ monomers,
                      which indicate an increase in binding entropy with respect
                      to the lead compound.},
      cin          = {ICS-6},
      ddc          = {540},
      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},
      pubmed       = {pmid:29893543},
      UT           = {WOS:000451496200018},
      doi          = {10.1021/acschemneuro.8b00132},
      url          = {https://juser.fz-juelich.de/record/848211},
}