N, F-doped graphene quantum dots effectively inhibit the fibrillization of amyloid-beta peptide (1–42)

Developing novel inhibitors for the fibrillization of amyloid peptides and understanding the relevant assembly processes are essential for biomedical and biomaterial sciences. Herein, we have synthesized and characterized the nitrogen and fluorine co-doped graphene quantum dots (N, F-GQDs), and investigated their inhibition of the fibrillization of Amyloid-beta peptide (1–42) (Aβ 42 ) by monitoring the assembly morphologies in the Aβ 42 /N, F-GQDs systems. Our results indicate that the N, F-GQDs functionalized with multiple surface groups effectively inhibits the fibrillization of amyloid Aβ 42 . The strong adsorption of Aβ 42 on N, F-GQDs significantly reduces the generation of β-sheet structures and the cytotoxicity of Aβ 42 /N, F-GQDs aggregates. Accordingly, a morphological evolution from the long fibrils of Aβ 42 to the spherical particles and unique closed-loop structures of Aβ 42 /N, F-GQDs have been captured. A possible interpretation for the observed phenomena in the presence of N, F-GQDs has been proposed by combining the different inhibition effects of other GQDs on the fibrillization of Aβ 42 and the results from various control experiments. Moreover, the inhibition activity of N, F-GQDs demonstrates good adaptability to resist the fluctuation of pH value and the interference of divalent metal ions , facilitating their practical applications in the future.