In this article density functional theory (DFT)-based calculations were employed to investigate the electrochemistry of the antitumor ruthenium complexes trans-tetrachloro(dimethylsulfoxide)imidazole ruthenate(III) (NAMI-A) and trans-[tetrachlorobis(1.-indazole)ruthenate(III)] (KP1019), their hydrolysis products as well as their interactions with biological S-donors and N-donors targets as cysteine, glutathione and guanine nucleobase. The compounds exhibit different electrochemical behavior upon hydrolysis. While the reduction potential of NAMI-A increases up to 0.8 V upon hydrolysis, the reduction potential of KP1019 remains almost constant after the first hydrolysis. NAMI-A and KP1019 complexes have thermodynamic preference to be reduced prior to undergoing hydrolysis and, strong preference to undergo successive hydrolysis instead of interacting with the S-donor and N-donor ligands. Interaction with S-donor ligands in the unprotonated form is highly unfavorable, with the free energy in solution (ΔGsol) ≥ 18 kcal mol-1. For both complexes, the interaction with the guanine and glutathione are of the same magnitude (ΔGsol ca. –0.6 kcal mol-1) meaning that these ligands can compete for binding to the metallodrug.

Abstract The thermal processing of iron ore pellets in pelletizing plants is a decisive stage regarding final product quality and knowledge of its characteristics has a fundamental importance in its process optimization. This study evaluated the variable sensitivity involved in pellet bed formations and their permeability using the artificial neural networks method. The model stated that standard diameter deviation, sphericity and pellet bed height mostly affect bed permeability. The computational model was able to predict pellet bed backpressure by means of pellet geometrical features, thus allowing improving green pellet generation, in order to ensure fuel and energy consumption reduction, final quality improvement and better productivity.

In this work, we used an aqueous two-phase system (ATPS) consisting of the ionic liquid [C4mim][Cl] and the salt K2HPO4 to partition α-lactalbumin, β-lactoglobulin, and lactoferrin whey proteins. Extraction efficiency values above 87% indicate that the proteins primarily migrated to the ionic liquid-rich phase (top phase). Partition coefficient values ranged from 6.17 to 8.93 for a-lactalbumin, from 22.80 to 34.55 for β-lactoglobulin, and from 26.46 to 40.06 for lactoferrin. Therefore, the saline ATPS with the ionic liquid examined in this study can be considered to be a promising alternative for extracting whey proteins.