The interface hydrophilic-hydrophobic integration of fluorinated defective graphene towards biomedical applications

In biomedical fields, rational design of novel two-dimensional (2D) biomedical nanomaterials aims to precisely manipulate biomolecules, including efficient capture, structural-functional transformation, directional movement, and self-assembly. In this work, we innovatively proposed new graphene nanosheets and selected two representative proteins to explore their binding mechanisms, structural-functional transformation of proteins, and biological effects of the materials. Fluorinated defective graphene (FDG) exhibited highly efficient capture and structural-functional transformation for the receptor binding domain (RBD), and we observed its collapse phenomenon in 2D materials for the first time. For the main protease (M^pro), FDG achieved an optimal balance between efficient capture, immobilization, and structural disruption. Further studies showed that fluorination on oxygen-containing defect graphene significantly enhanced variances in water distribution, surface properties, and hydrogen bond networks on the material surface. This allowed amino acids to be confined to specific areas, achieving efficient capture and directional movement. Additionally, the adsorption behavior and interaction strength of peptides and deoxynucleotides on FDG further validated the possibility of self-assembly. In summary, we highlight FDG as an excellent biomedical material with hydrophilic-hydrophobic integration.