Fig. 2
Development of fibril amyloid beta (fAβ) and the effect of NPs on Aβ fibrilization kinetics. a Representative transmission electron microscope (TEM) images of fAβ and oligomeric Aβ (oAβ). fAβ or oAβ (both 5 μl) was loaded on a formvar-coated, carbon-stabilized copper grid. Scale bar, 200 nm. b Thioflavin-T (Th-T) assay for fAβ and oAβ to validate the aggregation of β sheets. Protein or PBS (control) was mixed with 40 µM Th-T in a black-bottom 96-well microplate. Data are presented as mean ± SEM; n = 3; **P = 0.003 for student’s t test. c Th-T kinetic assay conducted with Aβ monomer over 65 h at 37 °C. Samples containing monomeric Aβ only or in the presence of NPs were loaded with 20 µM Th-T into a 96-well clear-bottomed non-binding half-area plate. d Endpoint Th-T fluorescence at 63 h. Data are presented as mean ± SEM; n = 3–4; ****P < 0.0001 for T12P5(PS) versus fAβ488 and ***P = 0.0007 for M12P5(PS) versus fAβ488 for Dunnett’s multiple comparisons shown on graph by one-way ANOVA. e TEM images of preformed fAβ mixed with AM-NPs or distilled water for 2 h. Scale bar, 500 nm