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@ARTICLE{PeraltaReyes:1044126,
      author       = {Peralta Reyes, Fernanda S. and Sommerhage, Simon and
                      Willbold, Dieter and Schröder, Gunnar F. and Gremer,
                      Lothar},
      title        = {{L}ecanemab {B}inds to {T}ransgenic {M}ouse
                      {M}odel‐{D}erived {A}myloid‐β {F}ibril {S}tructures
                      {R}esembling {A}lzheimer's {D}isease {T}ype {I}, {T}ype {II}
                      and {A}rctic {F}olds},
      journal      = {Neuropathology $\&$ applied neurobiology},
      volume       = {51},
      number       = {3},
      issn         = {0305-1846},
      address      = {Oxford [u.a.]},
      publisher    = {Wiley-Blackwell},
      reportid     = {FZJ-2025-03033},
      pages        = {e70022},
      year         = {2025},
      abstract     = {Aims:Lecanemab, an Alzheimer’s disease US Food and Drug
                      Administration-approved monoclonal antibody, was previously
                      reported to have a high affinity against intermediately
                      sized amyloid-β aggregates. Subsequently, it was observed
                      by immunogold labelling that lecanemab can also bind to
                      human type I amyloid-β fibrils. To determine whether
                      lecanemab binds to amyloid-β fibril structures other than
                      type I, we analysed its binding capacity to various
                      structurally defined and pathologically relevant amyloid-β
                      fibrils.Methods:We performed immunogold labelling with
                      lecanemab on extracted amyloid-β fibril preparations from
                      six different Alzheimer´s disease mouse models whose
                      structures were previously solved by cryo-EM and quantified
                      the relative binding affinities of lecanemab to the
                      different fibril polymorphs.Results:Our results show that
                      lecanemab exhibits high binding affinity to amyloid-β
                      fibril structures that have a flexible N-terminus in common,
                      as is the case for type I, type II and murine type III
                      amyloid-β fibril polymorphs, which resemble or are
                      identical to human structures observed in sporadic and
                      familial cases of Alzheimer’s disease, including a case
                      with the Arctic (E22G) mutation. In contrast, only weak
                      lecanemab binding was observed for murine amyloid-β fibrils
                      with a fixed and ordered N-terminus.Conclusions:These
                      findings may also explain the low incidence of ARIA-E with
                      lecanemab in clinical trials. This is because human
                      meningeal amyloid-β fibrils derived from cerebral amyloid
                      angiopathy affected brain tissue also contain a fixed and
                      ordered N-terminus, most likely preventing lecanemab
                      binding.},
      cin          = {IBI-7},
      ddc          = {610},
      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       = {40495448},
      UT           = {WOS:001507890600001},
      doi          = {10.1111/nan.70022},
      url          = {https://juser.fz-juelich.de/record/1044126},
}