Shear Bond Strength of Self-etching Adhesive Systems with Different pH Values to Bleached and/or CPP-ACP-treated Enamel

Purpose: To compare shear bond strengths of three different self-etching adhesive systems of different pH values to enamel bleached with carbamide peroxide, treated with casein phosphopeptide-amorphous calcium phosphate (CPP-ACP), or treated with CPP-ACP subsequent to bleaching with carbamide peroxide. Materials and Methods: Thirty-six human third molars were cut into 4 sections and randomly assigned to 4 groups (n = 36): group I: no treatment; group II: bleaching; group III: CPP-ACP; group IV: bleaching and CPP-ACP. After surface treatments, the samples of each group were further divided into three subgroups (n = 12) based on the adhesive used. The adhesives Clearfil SE Bond (CSE), AdhesE (ADE), and Adper SE Plus (ADP) were applied, and resin composite cylinders with a diameter of 2 mm and a height of 4 mm were bonded to the enamel. Then the specimens were subjected to shear bond strength testing. Two-way ANOVA and a post-hoc Tukey's test were used for statistical analysis (α = 0.05). Results: There were significant differences between the adhesive systems (p < 0.001) and surface treatments (p < 0.001), but no significant interactions were observed between these variables (p = 0.78). The CSE adhesive system showed the highest bond strength, and the bleaching procedure reduced bond strengths (p = 0.001). Furthermore, there were no significant differences in shear bond strength values between the control and CPP groups. However, the differences between other groups were statistically significant (p < 0.05). Conclusion: Bleaching reduced shear bond strength to enamel, but CPP-ACP application did not affect the bond strength to intact and previously bleached enamel. The bond strength of adhesives with different pH values to enamel was material dependant.     

Finite Element Model of Ocular Adduction by Active Extraocular Muscle Contraction

PurposeIn order to clarify the role of the optic nerve (ON) as a load on ocular rotation, we developed a finite element model (FEM) of incremental adduction induced by active contractility of extraocular muscles (EOMs), with and without tethering by the ON.MethodsThree-dimensional (3-D) horizontal rectus EOM geometries were obtained from magnetic resonance imaging of five healthy adults, and measured constitutive tissue properties were used. Active and passive strain energies of EOMs were defined using ABAQUS (Dassault Systemes) software. All deformations were assumed to be caused by EOM twitch activation that rotated the eye about a fixed center. The medial rectus (MR) muscle was commanded to additionally contract starting from 26 degrees adducted position, and the lateral rectus (LR) to relax, further adducting the eye either with or without loading by the ON. Tridimensional heat maps were generated to represent the stress and strain distributions.ResultsTensions in the EOMs were physiologically plausible during incremental adduction. Force in the MR increased from 10 gm at 26 degrees adduction to approximately 28 gm at 32 degrees adduction. Under identical MR contraction, adduction with ON loading reached 32 degrees but 36 degrees without it. Maximum and minimum principal strains within the MR were 16% and 22%, respectively, but when ON loading was included, resulting stress and strain were concentrated at the optic disc.ConclusionsThis physiologically plausible method of simulating EOM activation can provide realistic input to model biomechanical behavior of active and passive tissues in the orbit to clarify biomechanical consequences of ON traction during adduction.     

Displacement of the Hip Center of Rotation After Arthroplasty of Crowe III and IV Dysplasia: A Radiological and Biomechanical Study

To study the direction and biomechanical consequences of hip center of rotation (HCOR) migration in Crowe type III and VI hips after total hip arthroplasty, post-operative radiographs and CT scans of several unilaterally affected hips were evaluated. Using a three-dimensional model of the human hip, the HCOR was moved in all directions, and joint reaction force (JRF) and abductor muscle force (AMF) were calculated for single-leg stance configuration. Comparing to the normal side, HCOR had displaced medially and inferiorly by an average of 23.4% and 20.8%, respectively, of the normal femoral head diameter. Significant decreases in JRF (13%) and AMF (46.13%) were observed in a presumptive case with that amount of displacement. Isolated inferior displacement had a small, increasing effect on these forces. In Crowe type III and IV hips, the HCOR migrates inferiorly and medially after THA, resulting in a decrease in JRF, AMF, and abductor muscle contraction force.     

Functional mapping and single chain construction of the anti-cytokeratin 8 monoclonal antibody TS1

The anti-cytokeratin (CK) 8 monoclonal antibody (mab) TS1 has been shown to efficiently bind to CK8 expressed in carcinomas in vivo. The anti-idiotypic antibody of TS1, alphaTS1, can be used to regulate the tumor:non-tumor ratio of TS1 by clearing non-tumor binding TS1 from the circulation. If the interaction of TS1 to CK8 and alphaTS1 is fully understood, mutations can be used to improve the tumor:non-tumor ratio. A scFv was made of the mab TS1 and residues earlier identified by Erlandsson et al. as important for the interaction with both its antigen CK8 and its anti-idiotype alphaTS1, were mutated to alanine or amides and expressed in E. coli. The effects of the mutations were studied by ELISA and residues important for the interactions to both CK8 and alphaTS1 were identified as mainly tyrosines, charged residues, a serine and a tryptophan. Altogether, nine amino acid residues in TS1 were found to be important in the interaction to alphaTS1 and six residues for the interaction to CK8. Important residues, clustered together in the modelled protein, were identified as residues from CDR 3 of the heavy chain and the unexpected participation of a residue in CDR 2 of the light chain. Some of the important residues are likely to be hotspots. Hotspots constitute a few residues in an interaction that contribute most to the binding, energetically. Amino acid residues in hotspots often cluster together in the center of the interaction interface, but can also be spread out to the periphery. The hotspots are often surrounded by hydrophobic patches, which are seen in the modelled TS1 protein used in this study. Amino acid residues that increased the affinity when mutated were also identified for both interactions. These residues are likely to be located outside the interacting interface. It can from this study be concluded that it is wise to precede the mutational procedure with experiments that can give guidelines for the selection of which amino acid residues to mutate. If the guidelines from the chemical modifications from Erlandsson et al. not had been used, this study would have left some residues unmutated and thereby missed important information.