The effect of long‐term disinfection procedures on hardness property of resin denture teeth

doi: 10.1111/j.1741‐2358.2011.00520.x The effect of long‐term disinfection procedures on hardness property of resin denture teeth Objective: The aim of the study was to evaluate the effect of long‐term disinfection procedures on the Vickers hardness (VHN) of acrylic resin denture teeth. Material and methods: Five acrylic resin denture teeth (Vipi Dent Plus‐V, Trilux–T, Biolux‐B, Postaris‐P and Artiplus‐A) and one composite resin denture teeth (SR‐Orthosit‐O) were embedded in heat‐polymerised acrylic resin within polyvinylchloride tubes. Specimens were stored in distilled water at 37°C for 48 h. Measurements of hardness were taken after the following disinfection procedures: immersion for 7 days in 4% chlorhexidine gluconate or in 1% sodium hypochlorite (CIm and HIm group, respectively) and seven daily cycles of microwave sterilisation at 650 W for 6 min (MwS group). In the WIm group, specimens were maintained in water during the time used to perform the disinfection procedures (7 days). Data were analysed with anova followed by the Bonferroni procedure (α = 0.01). Results: Microwave disinfection decreased the hardness of all acrylic resin denture teeth (p < 0.001). Immersion for 7 days in 4% chlorhexidine gluconate or distilled water had significant effect on the hardness of the acrylic resin denture teeth A (p < 0.01), and 1% sodium hypochlorite on teeth T (p < 0.01). All disinfection procedures decrease the hardness of the composite resin denture teeth (p < 0.01). Teeth O exhibited the highest and teeth V the lowest hardness values in the control group (p < 0.01). Conclusions: Disinfection procedures changed the hardness of resin denture teeth.     

Structural analysis of the interaction of the pyrimidine tract-binding protein with the internal ribosomal entry site of encephalomyocarditis virus and foot-and-mouth disease virus RNAs.

Initiation of translation of a subset of eukaryotic mRNAs results from internal ribosomal entry. This process is exemplified by encephalomyocarditis virus (EMCV), which contains an internal ribosomal entry site (IRES) within its 5' nontranslated region that is approximately 450-nt long and consists of a series of stem-loops designated H-L. We have previously identified a cellular 58-kDa polypeptide that binds specifically to this IRES and that is implicated in its function as the pyrimidine tract-binding protein PTB. We have now mapped PTB binding sites directly on the IRES elements of EMCV and the related foot-and-mouth disease virus (FMDV) using structure-specific enzymatic probes and base-specific chemical probes. PTB bound to six sites on the EMCV IRES: site 1 (UCUU401) is upstream of domain H, site 2 is the basal helix of domain H (nt 407-410 and 440-443), site 3 (UCUUU423) is the apical loop of domain H, site 4 is the apical helix and adjacent internal bulged loop of domain K, site 5 (CUUUA750) is the apical loop of domain K, and site 6 (CCUUU815) is downstream of domain L. PTB bound to sites on the FMDV IRES that correspond precisely to EMCV sites 3, 5, and 6. These sites have the consensus sequence CUUU and form two groups that are located near to the 5' and 3' borders of these IRES elements. Their position, and the effects of mutation of them on IRES function are consistent with PTB's role in IRES-mediated initiation being to bind to multiple sites in the IRES, thereby stabilizing a specific active conformation.