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| Hauptseite > Publikationsdatenbank > Lecanemab Binds to Transgenic Mouse Model‐Derived Amyloid‐β Fibril Structures Resembling Alzheimer's Disease Type I, Type II and Arctic Folds > print |
| Hauptseite > Publikationsdatenbank > Lecanemab Binds to Transgenic Mouse Model‐Derived Amyloid‐β Fibril Structures Resembling Alzheimer's Disease Type I, Type II and Arctic Folds > print |
| 001 | 1044126 | ||
| 005 | 20250804115246.0 | ||
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| 100 | 1 | _ | |a Peralta Reyes, Fernanda S. |0 P:(DE-Juel1)201266 |b 0 |
| 245 | _ | _ | |a Lecanemab Binds to Transgenic Mouse Model‐Derived Amyloid‐β Fibril Structures Resembling Alzheimer's Disease Type I, Type II and Arctic Folds |
| 260 | _ | _ | |a Oxford [u.a.] |c 2025 |b Wiley-Blackwell |
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| 520 | _ | _ | |a 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. |
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| 700 | 1 | _ | |a Sommerhage, Simon |0 P:(DE-Juel1)186754 |b 1 |
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| 700 | 1 | _ | |a Schröder, Gunnar F. |0 P:(DE-Juel1)132018 |b 3 |e Corresponding author |
| 700 | 1 | _ | |a Gremer, Lothar |0 P:(DE-Juel1)145165 |b 4 |e Corresponding author |
| 773 | _ | _ | |a 10.1111/nan.70022 |g Vol. 51, no. 3, p. e70022 |0 PERI:(DE-600)2008293-9 |n 3 |p e70022 |t Neuropathology & applied neurobiology |v 51 |y 2025 |x 0305-1846 |
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