Abstract
The interaction between bone morphogenetic protein-2 (BMP-2) and the surface of biomaterials is essential for the restoration of bone and cartilage tissue, inducing cellular differentiation and proliferation. The properties of the surface, including topology features, regulate the conformation and bioactivity of the protein. In this research, we investigated the influence of nanopatterned surfaces on the interaction of a homodimer BMP-2 with graphite material by combining molecular dynamics (MD) and steered molecular dynamics (SMD) simulations. The graphite substrates were patterned as flat, linear grating, square, and circular profiles in combination with BMP-2 conformation in the side-on configuration. Ramachandran plots for the wrist and knuckle epitopes indicated no steric hindrances and provided binding sites to type I and type II receptors. Results showed two optimal patterns that increased protein adsorption of the lower monomer while preserving the secondary structure and leaving the upper monomer free to interact with the cells. Charged residues arginine and lysine and polar residues histidine and tyrosine were the main residues responsible for the strong interaction with the graphite surface. This research provides new molecular-level insights to further understand the mechanisms underlying protein adsorption on nanoscale patterned substrates.