Adsorption properties of albumin and fibrinogen on hydrophilic/hydrophobic TiO2 surfaces: A molecular dynamics study

In serval experimental researches, UV-induced hydrophilicity enabled better hemocompatibility in the TiO2 surface, which was considered to be caused by the removal of the carboxylic acid contamination from the surface. In this paper, we altered the surface wetting property by applying the formate contamination on the rutile (110) surface, and systematically investigated the adsorption properties of albumin and fibrinogen on hydrophilic/hydrophobic TiO2 surface. Unique contacts were found between the charged residues and the hydrophilic surface, anchoring the protein on the surface. The small size and the heart shape of albumin make it easy to cross the stable water layers near the surface. Besides, albumin has a higher proportion of charged residues, so it can form more unique contacts on the hydrophilic surface. Therefore, the albumin tends to adsorb on the hydrophilic surface. For the hydrophobic surface, the water layers near the surface are weakened, which helps the fibrinogen diffusing to the surface and adjusting its orientation. Although the hydrophobic surface cannot form the unique contacts, the larger size of fibrinogen can provide more residues to form enough ordinary contacts after adjusting, and then achieves stable adsorption. Therefore, fibrinogen tends to adsorb on the hydrophobic surface.

Automated summary

The study investigates the adsorption properties of albumin and fibrinogen on different TiO2 surfaces by altering the surface wetting property. The findings suggest that albumin tends to adsorb on hydrophilic surfaces, while fibrinogen tends to adsorb on hydrophobic surfaces.