Structural defects in amyloid-β fibrils drive secondary nucleation
Jing Hu, Tom Scheidt, Dev Thacker, Emil Axell, Elin Stemme, Urszula Łapińska, Stefan Wennmalm, Georg Meisl, Samo Curk, María Paz Andreasen, Michele Vendruscolo, Paolo Arosio, Anđela Šarić, Jeremy D. Schmit, Tuomas P. J. Knowles, , Alexander J. Dear
This study shows that structural defects in amyloid-β fibrils are key sites for secondary nucleation, suggesting new strategies for drug design to inhibit amyloid disorders.
Nature Communications · Feb 18, 2026Peer-reviewedBiophysics