▎ 摘　　要

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) (A beta 42) by monitoring the assembly morphologies in the A beta 42/N, F-GQDs systems. Our results indicate that the N, F-GQDs functionalized with multiple surface groups effectively inhibits the fibrillization of amyloid A beta 42. The strong adsorption of A beta 42 on N, F-GQDs significantly reduces the generation of beta-sheet structures and the cytotoxicity of A beta 42/N, F-GQDs aggregates. Accordingly, a morpho-logical evolution from the long fibrils of A beta 42 to the spherical particles and unique closed-loop structures of A beta 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 A beta 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.