Molecular docking and molecular dynamics simulation studies on the adsorption/desorption behavior of bone...

The adsorption/desorption behavior, and conformational and orientational changes of proteins on the surface of biomaterials are significant parameters for understanding how biomaterials perform their biological functions. In this study, for the first time, the interactions between BMP-7 and β-TCP (001) surface models with different ion-rich terminations (Ca-rich and P-rich) were investigated by molecular dynamics simulation (MD) and steered molecular dynamics simulation (SMD). The results indicated that BMP-7 preferentially interacts with both Ca-rich and P-rich β-TCP (001) surfaces at its wrist epitope residues with certain conformational changes, which led to more exposure of BMP-7 knuckle epitope residues to the environment and facilitation for binding to the type II receptor. Compared to the P-rich surface, it is speculated that the Ca-rich surface was more conducive to BMP-7 signal transduction since the upright orientation of the protein adsorption would lead to smaller hindrance for receptor binding. This study provided more atomistic and molecular information for better understanding the process of Ca-P surfaces affecting BMP-7 biological properties and further interpreted the osteoinductive mechanism from the perspective of growth factor adsorption. Moreover, the docking screening method adopted in this study is of guiding significance to the design and development of bioactive materials.