Adenosine triphosphate induces amorphous aggregation of amyloid b by increasing Aβ dynamics aggregation of amyloid b by increasing Aβ dynamics aggregation of amyloid b by increasing Aβ dynamics aggregation of amyloid b by increasing Aβ dynamics

Fig. 2. The Aβ monomer was prepared from 26-O-acyliso-Aβ42 (iso-Aβ), which starts aggregating immediately after dissolving in an aqueous solution. Formation of Aβ aggregates in the presence of 10 mM ATP, ADP or AMP, and the absence were monitored by ThT fluorescence. The aggregation proceeded in a final concentration of 10 % v/v DMSO. The fluorescence of 10 μM ThT in the presence or absence of 2.2 μM Aβ42 was monitored at an excitation wavelength of 444 nm and emission wavelength of 485 nm. Figure S6. CD spectra of Aβ. The iso-Aβ was dissolved in acetonitrile and the aggregation was started by dissolving in PBS. The aggregation proceeded at 37℃ in a final concentration of 2.2 μM Aβ in 10 v/v% acetonitrile. The positive and negative peaks at 200 and 220 nm, respectively, are typical for β-sheet structure. Figure S9. FT-IR spectra of Aβ aggregates. The spectrum in the presence of ADP after 1 day of incubation showed a distinct peak (cyan arrow) from those in the absence. These peaks of 1631 cm-1 with the sub-band 1685 cm-1 (black arrows) show a high content of β-sheets. The main peak positions of spectra after 4 days of incubation were similar to each other.