Members of oral bacterial communities form biofilms not only on tooth surfaces but also on the surface of dental implants that replace natural teeth. Prolonged interaction of host cells with biofilm-forming anaerobes frequently elicits peri-implantitis, a destructive inflammatory disease accompanied by alveolar bone loss leading to implant failure. Here we wish to overview how the deposition of bioactive peptides to dental implant surfaces could potentially inhibit bacterial colonization and the development of peri-implantisis. One preventive strategy is based on natural antimicrobial peptides (AMPs) immobilized on titanium surfaces. AMPs are capable to destroy both Gram positive and Gram negative bacteria directly. An alternative strategy aims at coating implant surfaces - especially the transmucosal part - with peptides facilitating the attachment of gingival epithelial cells and connective tissue cells. These cells produce AMPs and may form a soft tissue seal that prevents oral bacteria from accessing the apical part of the osseointegrated implant. Because a wide variety of titanium-bound peptides were studied in vitro, we wish to concentrate on bioactive peptides of human origin and some of their derivatives. Furthermore, special attention will be given to peptides effective under in vivo test conditions.

Dental implants are artificial dental roots anchoring prosthetic restorations to replace natural teeth. Dental implant systems may have different tapered conical connections. Our research focused on the mechanical examination of implant–superstructure connections. Thirty-five samples with 5 different cone angles (24°, 35°, 55°, 75°, and 90°) were tested for static and dynamic loads, carried out by a mechanical fatigue testing machine. Fixing screws were fixed with a torque of 35 Ncm before measurements. For static loading, samples were loaded with a force of 500 N in 20 s. For dynamic loading, the samples were loaded for 15,000 cycles with a force of 250 ± 150 N. In both cases, the compression resulting from load and reverse torque was examined. At the highest compression load of the static tests, a significant difference (p = 0.021) was found for each cone angle group. Following dynamic loading, significant differences (p < 0.001) for the reverse torques of the fixing screw were also shown. Static and dynamic results showed a similar trend: under the same loading conditions, changing the cone angle—which determines the relationship between the implant and the abutment—had led to significant differences in the loosening of the fixing screw. In conclusion, the greater the angle of the implant–superstructure connection, the smaller the screw loosening due to loading, which may have considerable effects on the long-term, safe operation of the dental prosthesis.

Solvent-free preparation types for cyclodextrin complexation, such as co-grinding, are technologies desired by the industry. However, in-depth analytical evaluation of the process and detailed characterization of intermediate states of the complexes are still lacking in areas. In our work, we aimed to apply the co-grinding technology and characterize the process. Fenofibrate was used as a model drug and dimethyl-β-cyclodextrin as a complexation excipient. The physical mixture of the two substances was ground for 60 min; meanwhile, samples were taken. A solvent product of the same composition was also prepared. The intermediate samples and the final products were characterized with instrumental analytical tools. The XRPD measurements showed a decrease in the crystallinity of the drug and the DSC results showed the appearance of a new crystal form. Correlation analysis of FTIR spectra suggests a three-step complexation process. In vitro dissolution studies were performed to compare the dissolution properties of the pure drug to the products. Using a solvent-free production method, we succeeded in producing a two-component system with superior solubility properties compared to both the active ingredient and the product prepared by the solvent method. The intermolecular description of complexation was achieved with a detailed analysis of FTIR spectra.

The adhesion of biomolecules to dental and orthopedic implants is a fundamental step in the process of osseointegration. Short peptide motifs, such as RGD or KRSR, carried by extracellular matrix proteins or coated onto implant surfaces, accelerate cell adhesion and tissue formation. For this reason, understanding the binding mechanisms of adhesive peptides to oxidized surfaces of titanium implants is of paramount importance. We performed molecular dynamics simulations to compare the adhesion properties of 6 peptides, including the tripeptide RGD, its variants KGD and LGD, as well as the tetrapeptide KRSR, its variant LRSR and its truncated version RSR, on anatase, rutile, and amorphous titanium dioxide (TiO₂) surfaces. The migration of these molecules from the water phase to the surface was simulated in an aqueous environment. Based on these simulations, we calculated the residence time of each peptide bound to the three different TiO₂ structures. It was found that the presence of an N-terminal lysine or arginine amino acid residue resulted in more efficient surface binding. A pulling simulation was performed to detach the adhered molecules. The maximum pulling force and the binding energy were determined from the results of these simulations. The tri- and tetrapeptides had slightly greater adhesion affinity to the amorphous and anatase structure than to rutile in general, however specific surface and peptide binding characters could be detected. The binding energies obtained from our simulations allowed us to rank the adhesion strengths of the studied peptides.