Graphene-oxide surface chemistry governs protein adsorption: molecular docking insights

Graphene oxide (GO)–protein interactions are fundamental to the performance of GO-based biomaterials, yet the molecular determinants of binding affinity remain insufficiently understood. Here, molecular docking simulations were used to systematically investigate how GO’s intrinsic structural parameters force-field treatment, lattice size, and oxygen-to-carbon (O/C) ratio, govern noncovalent adsorption of bovine serum albumin (BSA). GO models optimized with the Universal Force Field exhibited higher conformational strain but stronger binding affinities, revealing that moderate lattice distortion enhances interfacial reactivity. Increasing GO lateral dimensions did not monotonically improve adsorption, indicating an optimal size that balances contact area with flexibility. Conversely, excessive oxidation diminished binding by disrupting π-conjugation and reducing hydrophobic character. Energy decomposition identified van der Waals, hydrogen-bonding, and hydrophobic forces as dominant contributors at the GO–BSA interface. These results clarify how atomic-scale surface chemistry modulates biomolecular adsorption on carbon nanomaterials, offering design principles for tailoring GO surfaces for biomedical and nanotechnological applications. • Smaller graphene oxide sheets show stronger protein binding affinity • Optimal oxidation level (O/C ≈ 0.2) maximizes GO–protein adsorption • Force-field analysis links conformational strain to binding strength • Controlled OFG distribution lowers strain and enhances adsorption • Molecular docking reveals induced-fit stabilization on GO surfaces