TCA [BSA]

Poly(methyl methacrylate) (PMMA)/nanobarium titanate (NBT) composite has potential application in denture base materials. The denture base materials should be stable in the wet environment and exhibit good mechanical properties. This study aimed to evaluate the effectiveness of titanate coupling agent (TCA) on NBT behavior after soaking in the simulated body fluid (SBF) and to determine the effect of SBF exposure on fracture toughness of the PMMA nanocomposites. Silanated (Si-NBT), titanated (Ti-NBT), and pure NBT (Un-NBT) at 5% concentration (by mass) were incorporated in the PMMA matrix. NBT was sonicated in MMA prior to mixing with PMMA. SBF absorption, solubility, and leaching were measured, and fracture toughness of the PMMA nanocomposites was evaluated after soaking. The results showed that Titanated samples displayed lower SBF absorption capability and solubility values than the silanated ones. Moreover, the leachability of filler elements (Ba and Ti) was substantially reduced by titanation (54% and 61%, respectively), whereas the Si-NBT/PMMA revealed values of 12.3% and 7% respectively. Significant differences in fracture toughness were observed among the tested samples after 6 weeks of aging in SBF (p< 0.05). Although no notable changes in theK(IC)of pure PMMA and Un-NBT/PMMA samples were detected,K(IC)was improved by 20% after titanation. In addition, the fracture toughness of the titanated samples was higher than that of the silanated ones by 26%. In conclusion, TCA exhibited better stability in moisture than silane. Degradation resistance to moisture obtained with titanated NBT could lead to the promotion of clinical longevity of the composites.

The alternative oxidase (AOX) is a monotopic di-iron carboxylate protein which acts as a terminal respiratory chain oxidase in a variety of plants, fungi and protists. Of particular importance is the finding that both emerging infectious diseases caused by human and plant fungal pathogens, the majority of which are multi-drug resistant, appear to be dependent upon AOX activity for survival. Since AOX is absent in mammalian cells, AOX is considered a viable therapeutic target for the design of specific fungicidal and anti-parasitic drugs. In this work, we have mutated conserved residues within the hydrophobic channel (R96, D100, R118, L122, L212, E215 and T219), which crystallography has indicated leads to the active site. Our data shows that all mutations result in a drastic reduction in V-max and catalytic efficiency whilst some also affected the K-m for quinol and oxygen. The extent to which mutation effects inhibitor sensitivity was also investigated, with mutation of R118 and T219 leading to a complete loss of inhibitor potency. However, only a slight reduction in IC50 values was observed when R96 was mutated, implying that this residue is less important in inhibitor binding. In silico modelling has been used to provide insight into the reason for such changes, which we suggest is due to disruptions in the proton transfer network, resulting in a reduction in overall reaction kinetics. We discuss our results in terms of the structural features of the ubiquinol binding site and consider the implications of such findings on the nature of the catalytic cycle. Significance: The alternative oxidase is a ubiquinol oxidoreductase enzyme that catalyses the oxidation of ubiquinol and the reduction of oxygen to water. It is widely distributed amongst the plant, fungal and parasitic kingdoms and plays a central role in metabolism through facilitating the turnover of the TCA cycle whilst reducing ROS production.