Peptide/TiO2 surface interaction in solution by ab-initio and molecular dynamics simulations

Ab initio periodic calculations and classical molecular dynamics (MD) simulations were performed to investigate the adsorption mode of alanine and a number of short peptides, in particular two peptides, alanine-glutamic acid and alanine-lysine, taken as model systems for the ionic self-complementary oligopeptide EAK16-II, onto TiO2 (110) rutile surface, and their conformational characteristics upon adsorption. The atomistic description of the rutile surface and its interactions with water and peptide molecules were based on ab initio calculations, the TIP3P water model, the AMBER force field, and available parameters. By comparison with ab initio calculations, it is shown that MD simulations of reasonable duration can describe the main characteristics of the peptide-TiO2 surface interaction in solution, at least on a short time scale. Atom-atom radial distribution functions, atom-surface distances, backbone and side chain dihedral angle distributions, and peptide-surface interaction energies have been analyzed. Once adsorbed onto the TiO2 rutile surface by a bidentate interaction of both carboxyl oxygens with two adiacent Ti atoms, the small peptide studied showed a clear propensity to remain there and undergo relatively limited hinge-bending motions.