Molecular Dynamics Simulations of Collagen-like Peptide Adsorption on Titanium-Based Material Surfaces.

Classical molecular dynamics simulations were performed to investigate the early processes taking place in the interface region between titanium dioxide and a type I collagen triple helical segment, rich in hydroxyproline and proline residues, with special focus on intermolecular interactions and conformational stability. Possible binding modes were identified, and the analysis of the structural macroscopic and microscopic properties succeeded in elucidating the behavior of the helical bundle in contact with the TiO2 layer. The stability of the adsorbed molecules increased with the increasing number of coordinated atoms, and side-chain groups seemed to be primarily responsible of the adsorption process. However, a certain degree of disruption of the bundle was observed and quantified, considering the interchain distances and total solvent-exposed surface area. The results were consistent with previous studies and experimental data, which revealed that major changes in collagen conformation took place in water solution.