Self-Assembly of Au-Fe3O4 Hybrid Nanoparticles Using a Sol–Gel Pechini Method

The Pechini method has been used as a synthetic route for obtaining self-assembling magnetic and plasmonic nanoparticles in hybrid silica nanostructures. This manuscript evaluates the influence of shaking conditions, reaction time, and pH on the size and morphology of the nanostructures produced. The characterization of the nanomaterials was carried out by transmission electron microscopy (TEM) to evaluate the coating and size of the nanomaterials, Fourier-transform infrared spectroscopy (FT-IR) transmission spectra to evaluate the presence of the different coatings, and thermogravimetric analysis (TGA) curves to determine the amount of coating. The results obtained show that the best conditions to obtain core–satellite nanostructures with homogeneous silica shells and controlled sizes (<200 nm) include the use of slightly alkaline media, the ultrasound activation of silica condensation, and reaction times of around 2 h. These findings represent an important framework to establish a new general approach for the click chemistry assembling of inorganic nanostructures

Activation of the myosin motors in fast-twitch muscle of the mouse is controlled by mechano-sensing in the myosin filaments

ABSTRACT: Myosin motors in resting muscle are inactivated by folding against the backbone of the myosin filament in an ordered helical array and must be released from that conformation to engage in force generation. Time‐resolved X‐ray diffraction from single fibres of amphibian muscle showed that myosin filament activation could be inhibited by imposing unloaded shortening at the start of stimulation, suggesting that filaments were activated by mechanical stress. Here we improved the signal‐to‐noise ratio of that approach using whole extensor digitorum longus muscles of the mouse contracting tetanically at 28°C. Changes in X‐ray signals associated with myosin filament activation, including the decrease in the first‐order myosin layer line associated with the helical motor array, increase in the spacing of a myosin‐based reflection associated with packing of myosin tails in the filament backbone, and increase in the ratio of the 1,1 and 1,0 equatorial reflections associated with movement of motors away from the backbone, were delayed by imposing 10‐ms unloaded shortening at the start of stimulation. These results show that myosin filaments are predominantly activated by filament stress, as in amphibian muscle. However, a small component of filament activation at zero load was detected, implying an independent mechanism of partial filament activation. X‐ray interference measurements indicated a switch‐like change in myosin motor conformation at the start of force development, accompanied by transient disordering of motors in the regions of the myosin filament near its midpoint, suggesting that filament zonal dynamics also play a role in its activation. [Image: see text] KEY POINTS: Activation of myosin filaments in extensor digitorum longus muscles of the mouse is delayed by imposing rapid shortening from the start of stimulation. Stress is the major mechanism of myosin filament activation in these muscles, but there is a small component of filament activation during electrical stimulation at zero stress. Myosin motors switch rapidly from the folded inhibited conformation to the actin‐attached force‐generating conformation early in force development

Cooling intact and demembranated trabeculae from rat heart releases myosin motors from their inhibited conformation

Myosin filament–based regulation supplements actin filament–based regulation to control the strength and speed of contraction in heart muscle. In diastole, myosin motors form a folded helical array that inhibits actin interaction; during contraction, they are released from that array. A similar structural transition has been observed in mammalian skeletal muscle, in which cooling below physiological temperature has been shown to reproduce some of the structural features of the activation of myosin filaments during active contraction. Here, we used small-angle x-ray diffraction to characterize the structural changes in the myosin filaments associated with cooling of resting and relaxed trabeculae from the right ventricle of rat hearts from 39°C to 7°C. In intact quiescent trabeculae, cooling disrupted the folded helical conformation of the myosin motors and induced extension of the filament backbone, as observed in the transition from diastole to peak systolic force at 27°C. Demembranation of trabeculae in relaxing conditions induced expansion of the filament lattice, but the structure of the myosin filaments was mostly preserved at 39°C. Cooling of relaxed demembranated trabeculae induced changes in motor conformation and filament structure similar to those observed in intact quiescent trabeculae. Osmotic compression of the filament lattice to restore its spacing to that of intact trabeculae at 39°C stabilized the helical folded state against disruption by cooling. The myosin filament structure and motor conformation of intact trabeculae at 39°C were largely preserved in demembranated trabeculae at 27°C or above in the presence of Dextran, allowing the physiological mechanisms of myosin filament–based regulation to be studied in those conditions

Un asistente pedagógico digital para la reflexión, toma de decisiones y evaluación de la práctica docente

Desarrollo e Implementación de un Sistema de Soporte a la toma de Decisiones orientado a evaluar y fortalecer las competencias comunicativas de docentes y estudiantes con el objetivo de mejorar la motivación, la calidad y el rendimiento académico.Depto. de Psicobiología y Metodología en Ciencias del ComportamientoFac. de PsicologíaFALSEsubmitte