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The interaction between amyloid peptides and membrane is a broad research topic due to the variety of biological events occurring, such as the membrane disruption related pathogenesis of amyloid diseases or the toxicity of peptide materials. Amyloid peptides have many structural forms, it is therefore important to explore the interactions between the membrane and assemblies of amyloid peptides, and to find ways to control these interactions. Herein, we utilized atomic force microscopy (AFM) and circular dichroism spectra to explore the modulating effect of Graphene Oxide (GO) on amyloid peptide assembly. In addition, the interaction between liposome samples and amyloid peptide assembly modulated by GO was investigated. It is achieved that the membrane disruption of amyloid peptide aggregates can be fine-tuned by tweaking the GO concentration. The findings in this work provide a better understanding of amyloid peptide and membrane interactions and how it can be tuned.

AFM study on amyloid peptide - graphene oxide assembly and its interaction with liposome