2018 Volume 31 Issue 3 Pages 208-215
Laminin 332 (LN332) is an extracellular matrix that enhances the adhesion and migration of epithelial cells. The specific binding of LN332 on titanium (Ti) surfaces may serve to enhance the biological sealing at the epithelium-implant interface. Accordingly, it is important to analyze the response and application of LN332 on titanium implants. Superhydrophilic surface modification is reported to enhance the adsorption of proteins to titanium. This study aimed to evaluate the binding behavior of LN332 on surface-modified Ti with superhydrophilicity. In addition, the mechanism by which adsorption of LN332 is enhanced was examined by surface analyses.
Atmospheric-pressure plasma treatment (Ti-Plasma) and ultraviolet treatment (Ti-UV) as superhydrophilic treatments were performed on a titanium sensor that was designed for quartz crystal microbalance (QCM-D) apparatus. Untreated gold (Au-Air) or titanium sensor (Ti-Air) was used as a control. Adsorption properties of LN332 were assessed using a QCM-D method. In addition, surface characteristics were examined with X-ray photoelectron spectroscopy (XPS) and SEM observation using LN332-adsorbed specimens.
The amount of LN332 adsorption was increased on Ti-Air compared to Au-Air. In addition, the specific binding of LN332 was increased on the superhydrophilic treatment groups (Ti-Plasma and Ti-UV) compared with Ti-Air. Surface analyses of LN332-adsorbed surfaces revealed that carbon (C) and nitrogen (N) contents as well as carbonyl group, carboxyl group and peptide-related group were increased on the Ti-Plasma and Ti-UV specimens. Accordingly, peptide bonds seemed to play an important role on the specific binding of LN332 to surface-modified titanium with superhydrophilicity.
These results suggested that the superhydrophilic modifications may promote the adhesion of LN332 to titanium.
