Protein binding to implants is governed by the physicochemical properties of the biomaterial surface. The adhesion of a protein onto a solid surface is nonspecific. The aim of this study was to assess the adsorption process of fibrinogen at two different dental implants. The first biomaterial has a sand-blasted titanium surface, whereas the second one is covered by a calcium phosphate coating. After scanning electron microscopy and atomic force microscopy characterization of the implant surfaces, force spectroscopy has been used to determine the unbinding force of fibrinogen adsorbed at the two different substrates. Force-measurement findings indicate that the detachment force of fibrinogen adsorbed onto both surfaces varies as a function of the interaction time. The mean strength of the unbinding forces increases with the interaction time (100 and 1,000 ms, respectively). However, experimental data suggest that fibrinogen fixes to the two studied biomaterials by different mechanisms. Moreover, it appears that, after an interaction time of 1,000 ms, the detachment force of the adsorbed protein is quite larger for the titanium surface than for the calcium phosphate coating.
The interaction of proteins with solid surfaces is a fundamental phenomenon in the biomaterials field. We investigated, using atomic force microscopy (AFM), the interactions of a recombinant amelogenin with titanium, a biphasic calcium phosphate (BCP) and mica. The unbinding processes were compared to those of an earlier studied protein, namely fibrinogen. Force spectroscopy (AFM) experiments were carried out at 0 ms, 10 2 ms, 10 3 ms and 10 4 ms of contact time. In general, the rupture forces increased as a function of interaction time. The unbinding forces of amelogenin interacting with the BCP surface were always stronger than those of the amelogenin-titanium system. The unbinding forces of fibrinogen interacting with the BCP surface were always much stronger than those of the fibrinogen-titanium system.For the most part, this study provides direct evidence that recombinant amelogenin binds more strongly than fibrinogen on the studied substrates.
The aim of the present study was to investigate an inorganic bovine-derived hydroxyapatite bone substitute (Osteograph ® ) mixed with the same biomaterial coated with a synthetic peptide (P-15) analogue of collagen ). This blend of bone replacement materials was used for sinus floor augmentation. Assessments were carried out by using histology methods, transmission electron microscopy (TEM) and microanalysis (EDX). Ultrastructural and analytical features of the interfaces between the graft material and the peri-biomaterial tissues were evaluated six months after implantation. Our findings clearly show that newly-formed crystallites first develop at the surface of implanted crystals. Histological investigations revealed new bone tissue linking biomaterial particles together. TEM assessments pointed out that lamellar bone was generally separated from the graft material by a layer of woven bone measuring between 1 and 1.5 µm in thickness. Although calcified bone tissue was observed in direct contact with bone filling particles, the presence of mineralized granular material around implanted particles was also noticed. No characteristic periodic striation of mineralized collagen was evident within that mineralized structure. Chemical analyses (TEM-EDX) realized at different locations of newly formed mineralized granular substance along the interface revealed average Ca/P ratios ranging between 1.02 and 1.63. The different, concomitantly occurring, aforementioned structural features of the interfaces strongly suggested that the host responses to the used biomaterial blend resulted from dynamic osseointegration phenomena related to various interfacial mechanisms. Nevertheless, the biological response to the bone graft material appeared clinically and histologically satisfactory.
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