Fig. 7
Effects of taxifolin treatment on amyloid-β assembly. Efficient inhibition of amyloid-β1–40 assembly by taxifolin was shown both in vitro and in vivo. a Amyloid-β1–40 gradually formed aggregation bound with thioflavin-T in the absence of taxifolin (open circle). However, taxifolin treatment inhibited amyloid-β1-40 assembly (addition of 3 μM of taxifolin: filled triangle, 30 μM of taxifolin: filled square, 300 μM of taxifolin: filled circle). The mean fluorescence of triply prepared samples was expressed. b TEM images of fibrils after 6-hour incubation of amyloid-β1-40 alone (left) and amyloid-β1-40 with 300 μM of taxifolin (right). c–f The results of filter trap assay show taxifolin-treated Tg-SwDI mice have lower levels of amyloid-β oligomer than vehicle-treated Tg-SwDI mice. (c and d) The blot images of amyloid-β in the TBS soluble fractions extracted from the brains of 9-month-old Tg-SwDI mice receiving vehicle or taxifolin for 8 months (n = 4 each). The amyloid-β oligomers (c) and total amyloid-β (d) was detected by anti-amyloid-β oligomer antibody (A11) and anti-amyloid-β1-16 antibody (6E10). The duplicate samples were prepared independently. (e and f) Densitometric analysis of amyloid-β oligomer (e) and total amyloid-β (f). Scale bars indicate 500 nm. Error bars indicate ± SD. *p < 0.05