A series of polymeric "sanidic" materials were investigated and a number of criteria developed which must be fulfilled in order to classify these materials as liquid crystalline. By a combination of electron diffraction and high-resolution imaging, the biaxial phase is shown to consist of poorly developed microcrystals embedded in a liquid-like amorphous matrix. Only some materials are able to form a liquid crystalline phase at higher temperatures, but this phase is uniaxial.

Cellulases are efficient enzymes for the conversion of cellulose into glucose. Their use in immobilized form enables them to be reused in successive cycles in many biotechnological processes. Unlike conventional methods of immobilization by covalent bonding, in miniemulsion polymerization the immobilization of enzyme and the synthesis of polymer nanoparticles (support) occur simultaneously. Based on these aspects, the immobilization of cellulose on poly(methyl methacrylate) (PMMA) nanoparticles by miniemulsion polymerization was studied. The surfactant type (non-ionic and ionic) and latex pH showed great influence on cellulase activity. High activity values were obtained only when non-ionic surfactant (Lutensol AT50) and buffering agent (NaHCO 3 ) were used simultaneously. MMA polymerization rate and final monomer conversion were not affected by the presence of cellulase. The maximum immobilization efficiency (60%) was obtained when 6 wt.% of cellulase was used and stable PMMA nanoparticles (133 nm) were obtained. The relative activity profile of immobilized cellulase, for pH as well as temperature, was similar to that reported for the free form. Immobilized enzyme keeps its activity throughout seven days when stored at 4 ºC and phosphate buffer pH 6.0. Based on the results obtained in this work, miniemulsion polymerization as a method for cellulase immobilization on PMMA nanoparticles showed to be a promising technique with high possibility of industrial application.

We investigated the effects of LASSBio-998 (L-998), a compound designed to be a p38 MAPK (mitogen-activated protein kinase) inhibitor, on lipopolysaccharide (LPS)-induced acute lung inflammation in vivo. BALB/c mice were challenged with aerosolized LPS inhalation (0.5 mg/ml) 4 h after oral administration of L-998. Three hours after LPS inhalation, bronchoalveolar lavage fluid was obtained to measure the levels of the proinflammatory cytokines TNF-α (tumor necrosis factor-α) and IL-1 (interleukin-1) and the chemokines MCP-1 (monocyte chemoattractant protein-1) and KC (keratinocyte chemoattractant). In addition, neutrophil infiltration and p38 MAPK phosphorylation was measured. L-998 inhibited LPS-induced production of TNF-α and IL-1β and did not alter KC and MCP-1 levels. Furthermore, L-998 also significantly decreased neutrophil accumulation in lung tissues. As expected, L-998 diminished p38 MAPK phosphorylation and reduced acute lung inflammation. Inhibition of p38 MAPK phosphorylation by L-998 was also demonstrated in LPS-challenged murine C57BL/6 peritoneal macrophages in vitro, with concentration-dependent effects. L-998 suppressed LPS-induced lung inflammation, most likely by inhibition of the cytokine-p38 MAPK pathway, and we postulate that L-998 could be a clinically relevant anti-inflammatory drug candidate.

No abstract