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