Contribución del aplanado de morteros de cal para restauración sobre muretes de mampostería

Los morteros con base cal, han sido materiales descritos en los tratados antiguos de arquitectura, permitidos en muchos documentos que rigen los trabajos de restauración de bienes inmuebles patrimoniales y actualmente son los materiales más empleados en la restauración y conservación del patrimonio de mampostería natural en muchos sitios del mundo. La cal puede ser normalizada o bien puede ser apagada en sitio como describe Vitrubio en sus Libros de Arquitectura; los áridos pueden ser ígneos, metamórficos o sedimentarios; para modificar las propiedades físicas y mecánicas básicas de los morteros de cal suelen agregarse aditivos orgánicos e inorgánicos. La restauración y conservación de los edificios de mampostería coloniales es un reto en México. Tenemos 9 ciudades coloniales cuyos centros históricos están en el listado de Patrimonio de la Humanidad de la Unesco. Todas edificadas con mamposterías de rocas naturales y aplanadas con morteros de cal y aditivos orgánicos. Inicialmente se recubrían las rocas que carecían de labrado, cánones dictados por la arquitectura en boga. Con la modernización y masificación del transporte, los residuos vertidos a la atmósfera han deteriorado la calidad del aire ambiental resultando en pátinas, costras negras, daño antropogénico en superficies expuestas, devitrificación de la matriz de las rocas. Del uso sugerido de emplear morteros como protección en los monumentos arquitectónicos coloniales, método relativamente simple y económico, se ha revisado también su efecto sobre la resistencia mecánica. Este trabajo hace una comparación entre pilas de mampostería de arcilla recocida adheridas con mortero de cal adicionado con fibras desecadas y pulverizadas de nopal cactus opuntia y pilas con las mismas características, pero recubiertas en ambas caras con el mortero mencionado.Tópico 4.- Morteros de cal, materiales cálcicos y cementíceos. Evaluación de propiedades y composición. Mampostería de ladrillos. Caracterización. Evaluación de patologías y Refuerzo

Capitulo 2. Ciencias Naturales y Ciencias Básicas, Ingeniería y Tecnología

La diseminación de la Levitación Magnética, a pesar de lo antiguo de su tecnología, ha sido limitada. Debido a sus inconvenientes prácticos de implementación, su uso es bastante restringido, comparado con otras tecnologías (SCMaglev japonés, Transrapid alemán, o productos comerciales para ocio y entretenimiento). Con el boom de las tecnologías limpias y amigables con el medio ambiente y en concordancia con los objetivos del milenio, es pertinente plantearse el objetivo de optimizar el proceso de Levitación Magnética para generar un aprovechamiento de las ventajas de esta tecnología a nivel mecánico, eléctrico, y ambiental.  Actualmente la UNAD adelanta un proyecto de investigación cuyo objetivo es generar un modelo físico matemático de levitación magnética para aplicaciones en ingeniería. De este proyecto se ha derivado una primera revisión sistemática de los principios físicos y los modelos vigentes en Levitación Magnética

Disulfiram as a novel inactivator of Giardia lamblia triosephosphate isomerase with antigiardial potential

Giardiasis, the infestation of the intestinal tract by Giardia lamblia, is one of the most prevalent parasitosis worldwide. Even though effective therapies exist for it, the problems associated with its use indicate that new therapeutic options are needed. It has been shown that disulfiram eradicates trophozoites in vitro and is effective in vivo in a murine model of giardiasis; disulfiram inactivation of carbamate kinase by chemical modification of an active site cysteine has been proposed as the drug mechanism of action. The triosephosphate isomerase from G. lamblia (GlTIM) has been proposed as a plausible target for the development of novel antigiardial pharmacotherapies, and chemical modification of its cysteine 222 (C222) by thiol-reactive compounds is evidenced to inactivate the enzyme. Since disulfiram is a cysteine modifying agent and GlTIM can be inactivated by modification of C222, in this work we tested the effect of disulfiram over the recombinant and trophozoite-endogenous GlTIM. The results show that disulfiram inactivates GlTIM by modification of its C222. The inactivation is species-specific since disulfiram does not affect the human homologue enzyme. Disulfiram inactivation induces only minor conformational changes in the enzyme, but substantially decreases its stability. Recombinant and endogenous GlTIM inactivates similarly, indicating that the recombinant protein resembles the natural enzyme. Disulfiram induces loss of trophozoites viability and inactivation of intracellular GlTIM at similar rates, suggesting that both processes may be related. It is plausible that the giardicidal effect of disulfiram involves the inactivation of more than a single enzyme, thus increasing its potential for repurposing it as an antigiardial drug. Keywords: Giardiasis, Drug repurposing, Neglected disease, Recombinant protein, Enzyme inactivatio

Structural Effects of Protein Aging: Terminal Marking by Deamidation in Human Triosephosphate Isomerase

<div><p>Deamidation, the loss of the ammonium group of asparagine and glutamine to form aspartic and glutamic acid, is one of the most commonly occurring post-translational modifications in proteins. Since deamidation rates are encoded in the protein structure, it has been proposed that they can serve as molecular clocks for the timing of biological processes such as protein turnover, development and aging. Despite the importance of this process, there is a lack of detailed structural information explaining the effects of deamidation on the structure of proteins. Here, we studied the effects of deamidation on human triosephosphate isomerase (HsTIM), an enzyme for which deamidation of N15 and N71 has been long recognized as the signal for terminal marking of the protein. Deamidation was mimicked by site directed mutagenesis; thus, three mutants of HsTIM (N15D, N71D and N15D/N71D) were characterized. The results show that the N71D mutant resembles, structurally and functionally, the wild type enzyme. In contrast, the N15D mutant displays all the detrimental effects related to deamidation. The N15D/N71D mutant shows only minor additional effects when compared with the N15D mutation, supporting that deamidation of N71 induces negligible effects. The crystal structures show that, in contrast to the N71D mutant, where minimal alterations are observed, the N15D mutation forms new interactions that perturb the structure of loop 1 and loop 3, both critical components of the catalytic site and the interface of HsTIM. Based on a phylogenetic analysis of TIM sequences, we propose the conservation of this mechanism for mammalian TIMs.</p></div

Structural and Functional Perturbation of <i>Giardia lamblia</i> Triosephosphate Isomerase by Modification of a Non-Catalytic, Non-Conserved Region

<div><p>Background</p><p>We have previously proposed triosephosphate isomerase of <i>Giardia lamblia</i> (GlTIM) as a target for rational drug design against giardiasis, one of the most common parasitic infections in humans. Since the enzyme exists in the parasite and the host, selective inhibition is a major challenge because essential regions that could be considered molecular targets are highly conserved. Previous biochemical evidence showed that chemical modification of the non-conserved non-catalytic cysteine 222 (C222) inactivates specifically GlTIM. The inactivation correlates with the physicochemical properties of the modifying agent: addition of a non-polar, small chemical group at C222 reduces the enzyme activity by one half, whereas negatively charged, large chemical groups cause full inactivation.</p><p>Results</p><p>In this work we used mutagenesis to extend our understanding of the functional and structural effects triggered by modification of C222. To this end, six GlTIM C222 mutants with side chains having diverse physicochemical characteristics were characterized. We found that the polarity, charge and volume of the side chain in the mutant amino acid differentially alter the activity, the affinity, the stability and the structure of the enzyme. The data show that mutagenesis of C222 mimics the effects of chemical modification. The crystallographic structure of C222D GlTIM shows the disruptive effects of introducing a negative charge at position 222: the mutation perturbs loop 7, a region of the enzyme whose interactions with the catalytic loop 6 are essential for TIM stability, ligand binding and catalysis. The amino acid sequence of TIM in phylogenetic diverse groups indicates that C222 and its surrounding residues are poorly conserved, supporting the proposal that this region is a good target for specific drug design.</p><p>Conclusions</p><p>The results demonstrate that it is possible to inhibit species-specifically a ubiquitous, structurally highly conserved enzyme by modification of a non-conserved, non-catalytic residue through long-range perturbation of essential regions.</p></div

Structural analysis of GlTIM C222D^C.

<p>(A) Structural superposition of the 20 monomers in the crystallographic structure of GlTIM C222D^C; each chain is shown in different color. (B) Close-up of the superposed loop 6 and 7 regions in GlTIM C222D^C, which show the major conformational differences between the different chains; the orientation is the same as in panel A. (C) <i>Per</i> residue Cα RMSD values of the 20 monomers present in the crystallographic structure of GlTIM C222D^C; each chain is shown in a different color.</p