One of the most accepted engineering construction concepts of underground repositories for high radioactive waste considers the use of low-pH cementitious materials. This paper deals with the design of those based on Ordinary Portland Cements with high contents of silica fume and/or fly ashes that modify most of the concrete "standard" properties, the pore fluid composition and the microstructure of the hydrated products. Their resistance to long-term groundwater aggression is also evaluated. The results show that the use of OPC cement binders with high silica content produces low-pH pore waters and the microstructure of these cement pastes is different from the conventional OPC ones, generating C-S-H gels with lower CaO/Si0 2 ratios that possibly bind alkali ions. Leaching tests show a good resistance of low-pH concretes against groundwater aggression although an altered front can be observed.
This study aims to analyze the effects of supercritical carbonation (CO2 at 20 MPa and 318 K) on the
physicochemical properties of ordinary Portland cement pastes. The evolution of the main crystalline phases
of the cement pastes during carbonation was determined by means of X-ray diffraction and thermogravimetric
analysis. The pore structure was analyzed by low-temperature N2 adsorption−desorption and mercury intrusion
porosimetry techniques. Finally, the microstructure of the samples was observed by using scanning electron
microscopy coupled with energy-dispersive X-ray detection for chemical analysis. For a natural carbonation
process, diffusion of CO2 into the pores of the cement paste is considered as the rate-controlling step. Instead,
the accelerated reaction kinetics of calcium carbonate precipitation in the supercritical process was chemically
controlled by the detachment of calcium ions from solid portlandite or CSH gel. The total pore volume of the
studied cement pastes decreased with carbonation, which was associated with the deposition of the formed
CaCO3. Samples carbonated under the supercritical conditions developed a higher volume of gel pores than
those obtained by natural carbonation.
The emergence of bacterial resistance to the major classes of antibiotics has become a serious problem over recent years. For aminoglycosides, the major biochemical mechanism for bacterial resistance is the enzymatic modification of the drug. Interestingly, in several cases, the oligosaccharide conformation recognized by the ribosomic RNA and the enzymes responsible for the antibiotic inactivation is remarkably different. This observation suggests a possible structure-based chemical strategy to overcome bacterial resistance; in principle, it should be possible to design a conformationally locked oligosaccharide that still retains antibiotic activity but that is not susceptible to enzymatic inactivation. To explore the scope and limitations of this strategy, we have synthesized several aminoglycoside derivatives locked in the ribosome-bound "bioactive" conformation. The effect of the structural preorganization on RNA binding, together with its influence on the aminoglycoside inactivation by several enzymes involved in bacterial resistance, has been studied. Our results indicate that the conformational constraint has a modest effect on their interaction with ribosomal RNA. In contrast, it may display a large impact on their enzymatic inactivation. Thus, the work presented herein provides a key example of how the conformational differences exhibited by these ligands within the binding pockets of the ribosome and of those enzymes involved in bacterial resistance can, in favorable cases, be exploited for designing new antibiotic derivatives with improved activity in resistant strains.
Herein, we describe how the conformational differences exhibited by aminoglycosides in the binding pockets of the ribosome and those enzymes involved in bacterial resistance can be exploited in the design of new antibiotic derivatives with improved activity in resistant strains. The simple modification shown in the figure, leading to the conformationally restricted 5, provides an effective protection against aminoglycoside inactivation by Staphylococcus aureus ANT4, both in vivo and in vitro.
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