An Electromagnetic Tracker System for the design of a dental superstructure

Nowadays, different techniques are available for manufacturing full-arch implant-supported prosthesis, many of them based on an impression procedure. Nevertheless, the long-term success of the prosthesis is highly influenced by the accuracy during such process, being affected by factors such as the impression material, implant position, angulation and depth. This paper investigates the feasibility of a 3D electromagnetic motion tracking system as an acquisition method for modeling such prosthesis. To this extent, we propose an implant acquisition method at the patient mouth, using a specific prototyped tool coupled with a tracker sensor, and a set of calibration procedures (for distortion correction and tool calibration), that ultimately obtains combined measurements of the implant’s position and angulation, and eliminating the use of any impression material. However, in the particular case of the evaluated tracking system, the order of magnitude of the obtained errors invalidates its use for this specific application.

Electromagnetic tracker feasibility in the design of a dental superstructure for edentulous patients

The success of the osseointegration concept and the Brånemark protocol is highly associated to the accuracy in the production of an implant-supported prosthesis. One of most critical steps for long-term success of these prosthesis is the accuracy obtained during the impression procedure, which is affected by factors such as the impression material, implant position, angulation and depth. This paper investigates the feasibility of 3D electromagnetic motion tracking systems as an acquisition method for modeling full-arch implant-supported prosthesis. To this extent, we propose an implant acquisition method at the patient mouth and a calibration procedure, based on a 3D electromagnetic tracker that obtains combined measurements of implant’s position and angulation, eliminating the use of any impression material. Three calibration algorithms (namely linear interpolation, higher-order polynomial and Hardy multiquadric) were tested to compensate for the electromagnetic tracker distortions introduced by the presence of nearby metals. Moreover, implants from different suppliers were also tested to study its impact on tracking accuracy. The calibration methodology and the algorithms employed proved to implement a suitable strategy for the evaluation of novel dental impression techniques. However, in the particular case of the evaluated electromagnetic tracking system, the order of magnitude of the obtained errors invalidates its use for the full-arch modeling of implant-supported prosthesis.

Surface plasmon resonance as a tool in the functional analisys of an immunodominant site in foot-and-mouth disease virus

A fast and direct surface plasmon resonance (SPR) method for the kinetic analysis of the interactions between peptide antigens and immobilised monoclonal antibodies (mAb) has been established. Protocols have been developed to overcome the problems posed by the small size of the analytes (< 1600 Da). The interactions were well described by a simple 1:1 bimolecular interaction and the rate constants were self-consistent and reproducible. The key features for the accuracy of the kinetic constants measured were high buffer flow rates, medium antibody surface densities and high peptide concentrations. The method was applied to an extensive analysis of over 40 peptide analogues towards two distinct anti-FMDV antibodies, providing data in total agreement with previous competition ELISA experiments. Eleven linear 15-residue synthetic peptides, reproducing all possible combinations of the four replacements found in foot-and-mouth disease virus (FMDV) field isolate C-S30, were evaluated. The direct kinetic SPR analysis of the interactions between these peptides and three anti-site A mAbs suggested additivity in all combinations of the four relevant mutations, which was confirmed by parallel ELISA analysis. The four-point mutant peptide (A15S30) reproducing site A from the C-S30 strain was the least antigenic of the set, in disagreement with previously reported studies with the virus isolate. Increasing peptide size from 15 to 21 residues did not significantly improve antigenicity. Overnight incubation of A15S30 with mAb 4C4 in solution showed a marked increase in peptide antigenicity not observed for other peptide analogues, suggesting that conformational rearrangement could lead to a stable peptide-antibody complex. In fact, peptide cyclization clearly improved antigenicity, confirming an antigenic reversion in a multiply substituted peptide. Solution NMR studies of both linear and cyclic versions of the antigenic loop of FMDV C-S30 showed that structural features previously correlated with antigenicity were more pronounced in the cyclic peptide. Twenty-six synthetic peptides, corresponding to all possible combinations of five single-point antigenicity-enhancing replacements in the GH loop of FMDV C-S8c1, were also studied. SPR kinetic screening of these peptides was not possible due to problems mainly related to the high mAb affinities displayed by these synthetic antigens. Solution affinity SPR analysis was employed and affinities displayed were generally comparable to or even higher than those corresponding to the C-S8c1 reference peptide A15. The NMR characterisation of one of these multiple mutants in solution showed that it had a conformational behaviour quite similar to that of the native sequence A15 and the X-ray diffraction crystallographic analysis of the peptide ? mAb 4C4 complex showed paratope ? epitope interactions identical to all FMDV peptide ? mAb complexes studied so far. Key residues for these interactions are those directly involved in epitope ? paratope contacts (141Arg, 143Asp, 146His) as well as residues able to stabilise a particular peptide global folding. A quasi-cyclic conformation is held up by a hydrophobic cavity defined by residues 138, 144 and 147 and by other key intrapeptide hydrogen bonds, delineating an open turn at positions 141, 142 and 143 (corresponding to the Arg-Gly-Asp motif).