Fig. 1: C3N nanodots inhibit Aβ42 fibrillization in vitro.
From: C3N nanodots inhibits Aβ peptides aggregation pathogenic path in Alzheimer’s disease
a Transmission electron microscopy (TEM) image, crystal structure (top right corner, HRTEM image), and lateral size distribution (bottom right corner, histogram) of C3N nanodots. The image is representative of three independent experiments. b The influence of C3N nanodots on Aβ42 peptides (50 μM) aggregation was detected by ThT fluorescence. Data are presented as mean ± SD, n = 3 biological replicates and signals were normalized by setting the maximal ThT signals to 100%. c The formation levels of amyloid fiber under different conditions were detected by dot blot assay using Aβ fibrils conformation specific antibody (mOC87), at time = 24 h. Immunoblots are from one experiment representative of three independent experiments with similar results. d Representative AFM images of Aβ peptides untreated/treated with C3N nanodots (0, 100, 300, and 500 μg/mL) for 24 h. n = 3 independent experiments. e Time evolutions of the secondary structure of each residue in two Aβ42 peptides. The secondary structures of residues were assigned using the DSSP definition72. f The proportions of each structural component in the peptides. g CD spectra of Aβ peptides at 0 and 24 h in the absence of C3N nanodots and after incubation with C3N nanodots for 24 h. h The nonbonded interaction energies (including electrostatic (elec), van der Waals (vdW) interactions, and a total of them) between C3N nanodots and peptides and key binding configurations during the process. Green dashed lines indicate hydrogen bonds, and the hydrophobic and hydrophilic (polar/charged) residues are shown with silver and green, respectively. Source data are provided as a Source data file.
