▎ 摘　　要

A detailed understanding of the interaction mechanisms between pathogenic protein aggregates and nanomaterials is indispensable to the application and development in biomedical area. Here, all-atom molecular dynamics (MD) simulations were performed to characterize the interaction between a graphene nanosheet with amyloid fibrils domain, a mostly parallel beta-sheet model as a typical representative. It was found that graphene had strong capabilities to interact with A beta fibrils, which first demonstrated prominent impacts on the molecular structure of the outer side chains of A beta fibrils, then secondary structures of amyloid fibrils partially collapsed to varying degrees, indicating that the introduction of graphene nanosheets can cause severe structural disassociation and configuration change owing to adsorption of amyloid fibrils. As for the adhesion of A beta fibrils to graphene, van der Waals (vdW) interaction was mainly responsible for driving A beta fibrils binding to graphene, which effectively inhibited the self-association and aggregation of A beta fibrils. However, the solvent also collaboratively promoted graphene-mediated disruption on fibrils. Structural features and other effects, including polarization and spatial effects, acted synergistically on the adhesive strength to enable the interaction energy. Furthermore, the interaction mechanism between A beta fibrils domains and unconstrained graphene was also explored as comparison, and it was found that graphene tended to be faster but irregularly reduced the contents of beta-sheets to dissociate amyloid fibers. These observations provide some clues for understanding an underlying molecular mechanism of adsorption-induced destruction based on the graphene-amyloid interaction and an attack-direction dependence of graphene on amyloid fibril structure damage.