Surface Characterisation of Human Serum Albumin Layers on Activated Ti6Al4V

Adpsortion of protein layers on biomaterials plays an important role in the interactions between implants and the bio-environment. In this context, human serum albumin (HSA) layers have been deposited on modified Ti6Al4V surfaces at different ultraviolet (UV-C) irradiation times to observe possible changes in the adsorbed protein layer. Protein adsorption was done from solutions at concentraions lower than the serum protein concentration, to follow the surface modifications at the beginning of the albumin adhesion process. For this purpose, the surface of the protein-coated samples has been characterized by time of flight secondary ion mass spectrometry (ToF-SIMS), contact angle and zeta potential measurements. The results obtained show a reduction in the total surface tension and zeta potential of samples treated with UV-C light when coated with a protein layer. Furthermore, the UV-C light treatment applied to titanium alloy surfaces is able to modify the conformation, orientation and packing of the proteins arranged in the adsorbed layer. Low irradiation time generates an unstable surface with the lowest protein adsorption and the highest hydrophobic/hydrophilic protein ratio, indicating a possible denaturalization of the protein on these surfaces. However, surface changes are stabilized after 15 h or UV-C irradiation, favoring the protein adsorption through electrical interactions.

Automated summary

Research shows that UV-C light treatment on Ti6Al4V surfaces can alter the conformation, orientation, and packing of protein layers, with low irradiation time leading to protein denaturation and 15 hours of irradiation stabilizing the surface changes favoring protein adsorption.