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The fruit of Randia monantha is traditionally and empirically used in the preparation of a beverage as antivenom and for the treatment of various diseases, but to date there is little scientific evidence regarding its antimicrobiological properties and toxicity. The objective of this study was to evaluar the effect of the administration of the aqueous extract of the Randia monantha pulp on acute toxicity in male Wistar rats and evaluate antimicrobial activity at different concentrations against pathogenic bacteria. The results of acute oral toxicity revealed no deaths in doses up to 5000 mg / kg body weight. The experimental animals showed no significant changes in the weight and behavior parameters evaluated with respect to the control treatment. Rats did not show significant changes in the hematological parameters, but dosis of 5000 mg/kg body weight rats exhibited the appearance of yellow spots on kidney. The aqueous extract did not show antimicrobial activity against test pathogenic bacteria. These results suggest that the aqueous extract of the Randia monantha fruit can be used with some degree of safety by oral administration but should not be taken in high doses.

El estudio pretende conocer el perfil sociodemográfico y de consumo de sustancias de los casos admitidos al programa de prevención indicada Proyecto JOVEN de Fundación Aldaba – Proyecto Hombre de Valladolid. La muestra está formada por 125 adolescentes y jóvenes que acudieron al Proyecto JOVEN en 2016 (varones 81.6%, menores 77.6%, españoles, 83.2% y con 16.4 años (DT = 2.07) de edad). La mayoría convive con su familia, bien con ambos cónyuges (41.6%) o bien con el padre/madre separados o divorciados (32.8%). En un 4.8% convivían en centros residenciales. La droga principal que motivó la inclusión en los programas y la intervención con ellos y sus familias es el cannabis (75.2%). El consumo fue menor entre los mayores de 18 años (64.3%) que entre los menores (78.4%), y mayor entre hombres (78.4%), que entre mujeres (60.9%).

Black pepper oleoresin was encapsulated by spray drying using gum arabic (GA) and whey protein concentrate (WPC) as wall materials. The physical surface features were examined using low-temperature adsorption of nitrogen at 77 K. Clustering function and spreading pressure were evaluated to predict optimal storage conditions of the microcapsules, through analyzing the data from the water adsorption isotherms determined using a gravimetric method at 25, 35, and 45 °C. Kinetic studies of the color changes and loss of piperine of the microcapsules stored at different water activities at 35 °C were carried out. It was found that the GAB, BET and Condon models adequately describe the sorption characteristics. The monolayers calculated with the clustering function and minimum change in spreading pressure (MCSP) were close to those obtained by the adsorption models. The isotherms local from the Condon model coincided with the levels of stability of the microcapsules. Two local isotherms were found for GA microcapsules, which exhibited two regions of chemical stability during storage. One region with high stability in the range of 0.108–0.515 a w , and the other with poor stability of 0.515–0.821 a w . Conversely, WPC microcapsules showed one isotherm local, which had high stability in the entire water activity range studied. For both microcapsules, the lowest values of color changes were of 1.5–4, while the degradation rate constants were −0.017 day−1 and -0.002 day−1 for GA and WPC, respectively. The water activities where occurred the optimal stability fall within of the MCSP zone.

Pulmonary surfactant is a lipoprotein complex that reduces surface tension to prevent alveolar collapse and contributes to the protection of the respiratory surface from the entry of pathogens. Surfactant protein A (SP-A) is a hydrophilic glycoprotein of the collectin family, and its main function is related to host defense. However, previous studies have shown that SP-A also aids in the formation and biophysical properties of pulmonary surfactant films at the air-water interface. Humans, unlike rodents, have two genes, SFTPA1 and SFTPA2. The encoded proteins, SP-A1 and SP-A2, differ quantitatively or qualitatively in function. It has been shown that both gene products are necessary for tubular myelin formation, an extracellular structural form of lung surfactant. The goal of this study was to investigate potential differences in the biophysical properties of surfactants containing human SP-A1, SP-A2, or both. For this purpose, we have studied for the first time, to our knowledge, the biophysical properties of pulmonary surfactant from individual humanized transgenic mice expressing human SP-A1, SP-A2, or both SP-A1 and SP-A2, in the captive bubble surfactometer. We observed that pulmonary surfactant containing SP-A1 reaches lower surface tension after postexpansion interfacial adsorption than surfactants containing no SP-A or only SP-A2. Under interfacial compression-expansion cycling conditions, surfactant films containing SP-A1 also performed better, particularly with respect to the reorganization of the films that takes place during compression. On the other hand, addition of recombinant SP-A1 to a surfactant preparation reconstituted from the hydrophobic fraction of a porcine surfactant made it more resistant to inhibition by serum than the addition of equivalent amounts of SP-A2. We conclude that the presence of SP-A1 allows pulmonary surfactant to adopt a particularly favorable structure with optimal biophysical properties.

The physicochemical properties of honey from the stingless bee Scaptotrigona mexicana harvested at four, three, two, and actual years did not show significant differences in most of their physicochemical and antioxidant properties. Some properties, such as: color, pH, and titratable acidity were affected by storage temperature, being most affected at 45 °C. The concentration of polyphenols was correlated with the percentage of radical 2,2′-diphenyl-1-picrylhydrazyl scavenging activity (R2 = 0.930). Honey showed an antibacterial activity against gram (+) and gram (–) bacteria, not showing inhibition of yeast and mold tested. The sensory evaluation showed that this honey had a high level of preference by consumers. Honey from S. mexicana bee can be stored for at least three years without being significantly affected by their physicochemical and antioxidant properties, and this is acceptable for marketing.

Pulmonary surfactant is a lipid-protein complex secreted by type II alveolar cells. This surface-active agent prevents alveolar collapse by reducing surface tension at the respiratory air-liquid interface during expiration and contributes to the innate defense of the lung. Surfactant protein A (SP-A) is a hydrophilic collectin protein implicated mainly in the host defense. However, it has been shown that SP-A participates in the formation of surfactant films at the interface and helps to reestablish the biophysical properties of surfactant when this is impaired by the presence of some inhibitors. There are two SP-A genes in humans, SFTPA1 and SFTPA2, which products differ in structure and function. With the aim of investigating the differences in the biophysical properties of surfactant containing human SP-A1, SP-A2 or both, we have studied 1) pulmonary surfactant from individual humanized transgenic mice expressing human SP-A1, SP-A2, or both SP-A1/2, in a Captive Bubble Surfactometer (CBS), and 2) the capability of this two variants of the protein to restore the biophysical activity of a reconstituted organic extract (OE) from native porcine surfactant in the presence of serum as inhibitory agent, mimicking a situation of lung injury. The experiments revealed consistent functional differences in surfactant containing SP-A1 or SP-A2. In the presence of serum, surfactant from mice containing SP-A1 and the OE reconstituted upon addition of SP-A1, achieved lower surface tension after post-expansion interfacial adsorption and a more efficient reorganization of the film under interfacial compression-expansion cycling conditions, than surfactants containing no SP-A or only SP-A2. We conclude that the presence of hSP-A1 allows surfactant to adopt a particularly favorable structure with optimal biophysical properties and helps to restore a proper behavior in the presence of an inhibitory agent as serum.

Pulmonary surfactant is a lipoprotein complex which reduces surface tension to prevent alveolar collapse. At the same time, surfactant also contributes to the protection of the large respiratory surface from the entry of pathogens. It is composed of around 92% lipids and 8% of specific surfactant proteins by mass. One of these proteins is SP-A, a hydrophilic glycoprotein of the collectin family. The main function of this protein is related with host defense. However, previous studies showed that SP-A also aids in the formation and surface behavior of surfactant films at the air-water interface. Humans possess two SP-A genes expressing protein variants SP-A1 and SP-A2. Although their specific or combined activity is not well understood, it has been shown that both gene products are necessary for tubular myelin formation, an extracellular structural form of surfactant. The goal of the present study was to investigate potential differences in the biophysical behavior of surfactants containing human SP-A1, SP-A2, or both. For this purpose we have studied pulmonary surfactant from humanized transgenic mice expressing hSP-A1, hSP-A2, or both human SP-As instead of the endogenous murine protein, in the Captive Bubble Surfactometer (CBS), which simulates alveolar interfacial compression-expansion dynamics. We observed that surfactant containing both hSP-A1 and hSP-A2 reaches lower surface tension after initial and post-expansion interfacial adsorption than surfactants containing only hSP-A1 or hSP-A2. Under interfacial cycling conditions (Quasi-static or Dynamic compression-expansion regimes) surfactant films containing both hSP-A1 and hSP-A2 also showed better performance than surfactant containing only SP-A1 or SP-A2. We conclude that the simultaneous presence of hSP-A1 and hSP-A2 proteins permits surfactant to adopt a particularly favorable structure with optimal functional properties.NIH HL34788