School of Biotechnology
Department of
Theoretical Chemistry
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Royal Institute of Technology
School of Biotechnology Department of Theoretical Chemistry |
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Project of the month, May 2010Protein Adsorption onto Hydroxylated TiO2 Surfaces
Figure 1. Snapshots of the adsorbed residues on a hydroxylated rutile surface taken at 5 ns. Protein adsorption onto implant surfaces is of great importance for the regulation of implant bioactivity. Surface modification is a promising way in the molecular design of biocompatible materials against nonspecific adsorption of proteins. In this project we focus on the different behaviour of protein adsorption on hydroxylated and nonhydroxylated rutile TiO2 (110) surfaces through molecular dynamics simulations. Our investigation indicates that the distribution of the water molecules at the interface induced by the surface modification plays an important role in the protein adsorption. The surface with modified hydroxyl groups was observed to have much greater affinity to the protein, as reflected by the larger protein surface electrostatic interaction and by the larger amount of adsorbed residues. The highly ordered structure of the modified hydroxyl groups on the hydroxylated surface diminishes the possibility of hydrogen-bond formation between the surface and the water molecules above it, which in turn makes it more easy for the protein to move closer to the surface with hydroxyl modification.
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