Comparison of Adsorption of Proteins at Di erent Sizes on Pristine Graphene and Graphene Oxide

Using all-atom molecular dynamics (MD) simulations, we have investigated the adsorption stability and conformation change of different proteins on the surface of pristine graphene (PG) and graphene oxide (GO). We find that: (ⅰ) with the cooperation of the electrostatic interactions between proteins and oxygen-containing groups, GO shows better adsorption stability than PG; (ⅱ) the peptide loses its secondary structure on both PG and GO surface, and the α-helix structure of the protein fragment is partially broken on PG surface, but is well preserved on GO surface, while the secondary structure of globular protein has no distinct change on both PG and GO surface. In general, GO presents better biocompatibility than PG. Our results are of significant importance to understand the interactions between proteins and PG/GO and the applications of PG/GO in biotechnology and biomedicine.