Fig. 8
Attenuation of spontaneous Aβ1–42 aggregation by PLGA vs PCL and PEG-PLGA. ThT kinetic assays (A, D, G) and DLS analysis (B, C, E, F, H, I) showing effects of PLGA (25 µM; green) compared to PEG-PLGA (5 µM; blue) and PCL (100 nM; red) on spontaneous aggregation of 10 µM Aβ1–42 (black) over 24 h incubation at 27 °C (A–C), 37 °C (D–F) and 40 °C (G–I). DLS analysis revealing diameter and average size histograms of Aβ1–42 in the presence of PLGA (green), PEG-PLGA (blue) and PCL (red) at 27 °C (B, C), 37 °C (E, F) and 40 °C (H, I) compared to control Aβ1–42 (black). Note that PLGA is more potent in suppressing spontaneous Aβ1–42 aggregation than PEG-PLGA and PCL at the studied concentrations. Filter-trap assay and respective quantification data revealing specificty of oligomeric and fibrillar Aβ1–42 conformers and their interactions in the presence or absence of 25 µM PLGA nanoparticles as detected using oligomeric specific A11 antobody (J) and fibrillar specific OC antibody (K). Note that presence of PLGA attenauted the detection of both Aβ1–42 conformers but the interaction is somewhat more evident with Aβ aggregates than with Aβ oligomers