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@ARTICLE{Camargo:1029094,
      author       = {Camargo, Luana Cristina and Gering, Ian and Mastalipour,
                      Mohammadamin and Kraemer-Schulien, Victoria and Bujnicki,
                      Tuyen and Willbold, Dieter and Coronado, Mônika A. and
                      Eberle, Raphael J.},
      title        = {{A} {S}nake {V}enom {P}eptide and {I}ts {D}erivatives
                      {P}revent {A}β 42 {A}ggregation and {E}liminate {T}oxic
                      {A}β 42 {A}ggregates {I}n {V}itro},
      journal      = {ACS chemical neuroscience},
      volume       = {15},
      number       = {14},
      issn         = {1948-7193},
      address      = {Washington, DC},
      publisher    = {ACS Publ.},
      reportid     = {FZJ-2024-04954},
      pages        = {2600 - 2611},
      year         = {2024},
      abstract     = {Over a century has passed since Alois Alzheimer first
                      described Alzheimer's disease (AD), and since then,
                      researchers have made significant strides in understanding
                      its pathology. One key feature of AD is the presence of
                      amyloid-β (Aβ) peptides, which form amyloid plaques, and
                      therefore, it is a primary target for treatment studies.
                      Naturally occurring peptides have garnered attention for
                      their potential pharmacological benefits, particularly in
                      the central nervous system. In this study, nine peptide
                      derivatives of Crotamine, a polypeptide from Crotalus
                      durissus terrificus Rattlesnake venom, as well as one
                      d-enantiomer, were evaluated for their ability to modulate
                      Aβ42 aggregation through various assays such as ThT, QIAD,
                      SPR, and sFIDA. All tested peptides were able to decrease
                      Aβ42 aggregation and eliminate Aβ42 aggregates.
                      Additionally, all of the peptides showed an affinity for
                      Aβ42. This study is the first to describe the potential of
                      crotamine derivative peptides against Aβ42 aggregation and
                      to identify a promising d-peptide that could be used as an
                      effective pharmacological tool against AD in the future.},
      cin          = {IBI-7},
      ddc          = {540},
      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       = {38957957},
      UT           = {WOS:001263163500001},
      doi          = {10.1021/acschemneuro.4c00089},
      url          = {https://juser.fz-juelich.de/record/1029094},
}