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@ARTICLE{Rafiei:916056,
      author       = {Rafiei, Yasin and Salmani, Bahram and Mirzaei-Behbahani,
                      Behnaz and Taleb, Mahshid and Meratan, Ali Akbar and
                      Ramezani, Mohammad and Nikfarjam, Nasser and Becker, Stefan
                      and Rezaie Ghaleh, Nasrollah},
      title        = {{P}olyphenols-{B}ased {N}anosheets of {P}ropolis {M}odulate
                      {C}ytotoxic {A}myloid {F}ibril {A}ssembly of α-{S}ynuclein},
      journal      = {ACS chemical neuroscience},
      volume       = {13},
      number       = {22},
      issn         = {1948-7193},
      address      = {Washington, DC},
      publisher    = {ACS Publ.},
      reportid     = {FZJ-2022-05902},
      pages        = {3168 - 3179},
      year         = {2022},
      abstract     = {Natural compounds with anti-aggregation capacity are
                      increasingly recognized as viable candidates against
                      neurodegenerative diseases. Recently, the polyphenolic
                      fraction of propolis (PFP), a complex bee product, has been
                      shown to inhibit amyloid aggregation of a model protein
                      especially in the nanosheet form. Here, we examine the
                      aggregation-modulating effects of the PFP nanosheets on
                      α-synuclein (α-syn), an intrinsically disordered protein
                      involved in the pathogenesis of Parkinson's disease. Based
                      on a range of biophysical data including intrinsic and
                      extrinsic fluorescence, circular dichroism (CD) data, and
                      nuclear magnetic resonance spectroscopy, we propose a model
                      for the interaction of α-syn with PFP nanosheets, where the
                      positively charged N-terminal and the middle non-amyloid
                      component regions of α-syn act as the main binding sites
                      with the negatively charged PFP nanosheets. The Thioflavin T
                      (ThT) fluorescence, Congo red absorbance, and CD data reveal
                      a prominent dose-dependent inhibitory effect of PFP
                      nanosheets on α-syn amyloid aggregation, and the microscopy
                      images and MTT assay data suggest that the PFP nanosheets
                      redirect α-syn aggregation toward nontoxic off-pathway
                      oligomers. When preformed α-syn amyloid fibrils are
                      present, fluorescence images show co-localization of PFP
                      nanosheets and ThT, further confirming the binding of PFP
                      nanosheets with α-syn amyloid fibrils. Taken together, our
                      results demonstrate the binding and anti-aggregation
                      activity of PFP nanosheets in a disease-related protein
                      system and propose them as potential nature-based tools for
                      probing and targeting pathological protein aggregates in
                      neurodegenerative diseases.},
      cin          = {IBI-7},
      ddc          = {540},
      cid          = {I:(DE-Juel1)IBI-7-20200312},
      pnm          = {5241 - Molecular Information Processing in Cellular Systems
                      (POF4-524)},
      pid          = {G:(DE-HGF)POF4-5241},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {36314062},
      UT           = {WOS:000879961600001},
      doi          = {10.1021/acschemneuro.2c00465},
      url          = {https://juser.fz-juelich.de/record/916056},
}