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The self-assembling of the amyloid β (Aβ) peptide into neurotoxic aggregates is considered a central event in the pathogenesis of Alzheimer’s disease (AD). Based on the “amyloid hypothesis”, many efforts have been devoted to designing molecules able to halt disease progression by inhibiting Aβ self-assembly. Here, we combine biophysical (ThT assays, TEM and AFM imaging), biochemical (WB and ESI-MS), and computational (all-atom molecular dynamics) techniques to investigate the capacity of four optically pure components of the natural product silymarin (silybin A, silybin B, 2,3-dehydrosilybin A, 2,3-dehydrosilybin B) to inhibit Aβ aggregation. Despite TEM analysis demonstrated that all the four investigated flavonoids prevent the formation of mature fibrils, ThT assays, WB and AFM investigations showed that only silybin B was able to halt the growth of small-sized protofibrils thus promoting the formation of …
American Chemical Society
Publication date: 
16 Aug 2017

Michele FM Sciacca, Valeria Romanucci, Armando Zarrelli, Irene Monaco, Fabio Lolicato, Natalia Spinella, Clelia Galati, Giuseppe Grasso, Luisa D’Urso, Margherita Romeo, Luisa Diomede, Mario Salmona, Corrado Bongiorno, Giovanni Di Fabio, Carmelo La Rosa, Danilo Milardi

Biblio References: 
Volume: 8 Issue: 8 Pages: 1767-1778
ACS chemical neuroscience