Adsorption of GA module onto graphene and graphene oxide: A molecular dynamics simulation study

• We simulate the adsorption of protein onto GO and PG.
• PG will destroy protein’s secondary structure while GO not.
• Electrostatic interactions and hydrogen bonds play important roles in GO system.
• π–π stacking interaction exists in both protein–PG and protein–GO systems.
• GO shows better biocompatibility.

Using all-atom molecular dynamics (MD) simulation, we have investigated the adsorption of protein GA module (GA53) onto graphene oxide (GO), compared with similar adsorption onto pristine graphene (PG). We find that: (1) the protein GA53 can be easily and firmly adsorbed onto the surface of GO and PG, but the binding sites are not specific; the main difference is that the secondary structure of GA53 can be well preserved in protein–GO system, while GA53 will partially lose its secondary structure after adsorbed on PG. (2) in protein–GO system, hydroxyl and epoxy groups increase the distance between protein and GO, which weaken their vdW interactions, meanwhile, hydrogen bonds and electrostatic interactions enhance their binding affinity. In protein–PG system, strong vdW interactions between residues of GA53 and PG have destroyed its secondary structure. (3) π–π stacking interactions still exist between aromatic residues and both the basal plane of GO and PG. In comparison with PG, our results suggest that GO presents better biocompatibility to preserve protein secondary structure when simultaneously absorbing protein.