No abstract

Small fluorescent atomic copper clusters, stabilized by tetrabutylammonium nitrate, have been synthesized by a simple electrochemical technique. These small clusters (Cu N , N < ≈14) show photoluminescence in the visible range with unusual high quantum yields (13%) and were characterized by UV−vis and fluorescence spectroscopies, LDI-TOF (laser desorption/ionization time-of-flight) mass spectroscopy, XPS (X-ray photoelectron spectroscopy), and TEM/HRTEM (high-resolution/transmission electron microscopy). Cu clusters are very stable and can be dispersed in both apolar and polar solvents, which makes them useful as very small building blocks, bringing new possibilities to construct novel nano/microstructures, with potential applications in fields such as biosensors, biomedicine, etc.

In this work, we aimed to characterize the surface and the internal structure of mannitol microspheres containing chitosan/tripolyphosphate nanoparticles, which were prepared by spray-drying. These microspheres were recently proposed as valuable candidates to transport therapeutic protein-loaded nanoparticles to the lungs owing to their favorable aerodynamic properties. To observe the distribution of chitosan nanoparticles and mannitol in the microspheres, specific characterization techniques, such as confocal laser scanning microscopy, X-ray photoelectron spectroscopy, and time-of-flight secondary ion mass spectrometry, were used. Results showed that mannitol is distributed in the whole particle and nanoparticles are homogeneously mixed with mannitol. Moreover, both components were detected in the microsphere surface, mannitol being present to a higher extent, which is in agreement with the theoretical mannitol/nanoparticle ratio of microspheres (80/20). Therefore, this work confirmed that chitosan nanoparticles were successfully encapsulated in mannitol microspheres, providing a homogeneous distribution of the nanoparticles and, hence, of the nanoencapsulated therapeutic macromolecule.

This work was undertaken to provide further insight into the role of mammalian target of rapamycin complex 1 (mTORC1) in skeletal muscle regeneration, focusing on myofiber size recovery. Rats were treated or not with rapamycin, an mTORC1 inhibitor. Soleus muscles were then subjected to cryolesion and analyzed 1, 10, and 21 days later. A decrease in soleus myofiber cross-section area on post-cryolesion days 10 and 21 was accentuated by rapamycin, which was also effective in reducing protein synthesis in these freeze-injured muscles. The incidence of proliferating satellite cells during regeneration was unaltered by rapamycin, although immunolabeling for neonatal myosin heavy chain (MHC) was weaker in cryolesion+rapamycin muscles than in cryolesion-only muscles. In addition, the decline in tetanic contraction of freeze-injured muscles was accentuated by rapamycin. This study indicates that mTORC1 plays a key role in the recovery of muscle mass and the differentiation of regenerating myofibers, independently of necrosis and satellite cell proliferation mechanisms.