The emission intensities in the range of 2000–8000 Å of CF, CF2, O, F, CO, CO+, and CO2 produced in CF4/O2 radio-frequency discharges, operated at 1 Torr of pressure and 50 W of power input, have been used to follow the etching process of Si and SiO2, as a function of the CF4/O2 feed composition. The addition of small amounts of nitrogen or argon to the plasma mixtures has permitted the determination of the effect of the oxygen addition to the gas feed on the electron densities of the plasma for a wide range of electron energies. The relative concentration profiles of F and O, as well as of CO and CO2, have been determined with this technique, as a function of the oxygen content in the feed. The important role played by atomic F as active etchant for both Si and SiO2 substrates has been confirmed.

The Zr4+ complexes with desferrioxamine (H3DFO) and its derivatives are the only 89Zr-based imaging agents for proton emission tomography (PET) that have been used so far in clinical trials. Nevertheless, a complete speciation of the Zr4+/H3DFO system in solution has never been performed and the stability constants of the relevant complexes are still unknown. Here we report, for the first time, the speciation of this system in water, performed by potentiometric titrations, and the determination of the stability constants of all complexes formed in the pH range 2.5–11.5. Surprisingly, although desferrioxamine gives rise to very stable 1:1 complexes with Zr4+ (logK = 36.14 for Zr4+ + DFO3− = [ZrDFO]+), 2:2 and 2:3 ones are also formed in solution. Depending on the conditions, these binuclear complexes can be main species in solution. These results were corroborated by small-angle X-ray scattering (SAXS) and MALDI mass spectrometry analyses of complex solutions. Information on complex structures was obtained by means of density functional theory (DFT) calculations.

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AL amyloidosis is characterized by widespread deposition of immunoglobulin light chains (LCs) as amyloid fibrils. Cardiac involvement is frequent and leads to life-threatening cardiomyopathy.Besides the tissue alteration caused by fibrils, clinical and experimental evidence indicates that cardiac damage is also caused by proteotoxicity of prefibrillar amyloidogenic species. As in other amyloidoses, the damage mechanisms at cellular level are complex and largely undefined. We have characterized the molecular changes in primary human cardiac fibroblasts (hCFs) exposed in vitro to soluble amyloidogenic cardiotoxic LCs from AL cardiomyopathy patients. To evaluate proteome alterations caused by a representative cardiotropic LC, we combined gel-based with label-free shotgun analysis and performed bioinformatics and data validation studies. To assess the generalizability of our results we explored the effects of multiple LCs on hCF viability and on levels of a subset of cellular proteins. Our results indicate that exposure of hCFs to cardiotropic LCs translates into proteome remodeling, associated with apoptosis activation and oxidative stress. The proteome alterations affect proteins involved in cytoskeletal organization, protein synthesis and quality control, mitochondrial activity and metabolism, signal transduction and molecular trafficking. These results support and expand the concept that soluble amyloidogenic cardiotropic LCs exert toxic effects on cardiac cells.Amyloidoses are protein misfolding diseases defined by the presence of extracellular protein aggregates as cross-β-sheet amyloid fibrils. The ability to form amyloid fibrils in vivo is a common feature of at least 36 distinct human proteins, which are otherwise different in terms of sequence, native structure, function and localization 1 . Light chain amyloidosis (AL amyloidosis) is the most frequent systemic form, and is characterized by widespread fibril deposition in target tissues 2,3 . Causal agents of this form are misfolding-prone immunoglobulin