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@ARTICLE{Streich:826950,
      author       = {Streich, Carmen and Akkari, Laura and Decker, Christina and
                      Bormann, Jenny and Rehbock, Christoph and
                      Müller-Schiffmann, Andreas and Niemeyer, Felix Carlsson and
                      Nagel-Steger, Luitgard and Willbold, Dieter and Sacca,
                      Barbara and Korth, Carsten and Schrader, Thomas and
                      Barcikowski, Stephan},
      title        = {{C}haracterizing the {E}ffect of {M}ultivalent {C}onjugates
                      {C}omposed of {A}β-{S}pecific {L}igands and {M}etal
                      {N}anoparticles on {N}eurotoxic {F}ibrillar {A}ggregation},
      journal      = {ACS nano},
      volume       = {10},
      number       = {8},
      issn         = {1936-0851},
      address      = {Washington, DC},
      publisher    = {Soc.},
      reportid     = {FZJ-2017-01157},
      pages        = {7582-7597},
      year         = {2016},
      abstract     = {Therapeutically active small molecules represent promising
                      nonimmunogenic alternatives to antibodies for specifically
                      targeting disease-relevant receptors. However, a potential
                      drawback compared to antibody–antigen interactions may be
                      the lower affinity of small molecules toward receptors.
                      Here, we overcome this low-affinity problem by coating the
                      surface of nanoparticles (NPs) with multiple ligands.
                      Specifically, we explored the use of gold and platinum
                      nanoparticles to increase the binding affinity of
                      Aβ-specific small molecules to inhibit Aβ peptide
                      aggregation into fibrils in vitro. The interactions of bare
                      NPs, free ligands, and NP-bound ligands with Aβ are
                      comprehensively studied via physicochemical methods
                      (spectroscopy, microscopy, immunologic tests) and cell
                      assays. Reduction of thioflavin T fluorescence, as an
                      indicator for β-sheet content, and inhibition of cellular
                      Aβ excretion are even more effective with NP-bound ligands
                      than with the free ligands. The results from this study may
                      have implications in the development of therapeutics for
                      treating Alzheimer’s disease.},
      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},
      UT           = {WOS:000381959100041},
      pubmed       = {pmid:27404114},
      doi          = {10.1021/acsnano.6b02627},
      url          = {https://juser.fz-juelich.de/record/826950},
}