Famotidine, an antiulcer drug belonging to the H₂ antagonists class of pharmacological agents, was recently shown to potently inhibit human (h) and bacterial carbonic anhydrases (CAs, EC 4.2.1.1). We investigated the inhibitory effects of famotidine against all classes of CAs from the pathogenic bacteria Vibrio cholerae, Burkholderia pseudomallei and Mycobacterium tuberculosis Rv3273 β-CA, as well as the CAs from the nonpathogenic bacteria/cyanobacteria Sulfurihydrogenibium yellowstonensis, S. azorense, Pseudoalteromonas haloplanktis, Colwellia psychrerythraea and Nostoc commune. The δ- and ζ-CAs from the diatom Thalassiosira weissflogii, the fungal enzymes from Cryptococcus neoformans, Candida glabrata and Malassezia globosa, as well as the protozoan enzymes from Trypanosoma cruzi and Plasmodium falciparum, were also investigated. Anopheles gambiae β-CA was also investigated. All these enzymes were effectively inhibited by famotidine, with affinities between the low nanomolar to the micromolar range. The best inhibition was observed against C. glabrata β-CA and TweCAζ, with K_Is ranging between 13.6 and 22.1 nM.

The synthesis of the β-cyclodextrin/propiconazole nitrate inclusion complex and the advantages of the encapsulation of this drug were recently reported, but the experimental data only partially revealed the structure of the supramolecular complex due to the limitations in understanding the intermolecular association mechanism. The present work describes the equilibrium molecular geometries of β-cyclodextrin/propiconazole and β-cyclodextrin/protonated propiconazole, established by the AM1 and PM3 semi-empirical methods. The affinity between different parts of the guest molecule and the cyclodextrin cavity was studied considering that propiconazole possesses three residues able to be included into the host cavity through primary or secondary hydroxyl rims. The results have revealed that the most stable complex is formed when the azole residue of the propiconazole enters the cavity of the cyclodextrin through the narrow hydroxyl’s rim.

C60-PEI and C60-PEG-PEI as efficient binders of dsDNA, with good transfection up to 25%, high cytocompatibility and cell proliferation up to 200%.

The nontoxicity, worldwide availability and low production cost of cuttlefish bone products qualify them an excellent biocoagulant to treat food industry wastewater. In this study, cuttlefish bone liquid waste from the deproteinization step was used as a biocoagulant to treat food industry wastewater. This work concerns a waste that has never before been investigated. The objectives of this work were: the recovery of waste resulting from cuttlefish bone deproteinization, the replacementof chemical coagulants with natural ones to preserve the environment, and the enhancement ofthe value of fishery byproducts. A quantitative characterization of the industrial effluents of a Moroccan food processing plant was performed. The physicochemical properties of the raw cuttlefish bone powder and the deproteinization liquid extract were determined using specific analysis techniques: SEM/EDX, FTIR, XRD and ¹H-NMR. The protein content of the deproteinization liquid was determined by OPA fluorescent assay. The zeta potential of the liquid extract was also determined. The obtained analytical results showed that the deproteinization liquid waste contained an adequate amount of soluble chitin fractions that could be used in food wastewater treatment. The effects of the coagulant dose and pH on the food industrial effluents were studied to confirm the effectiveness of the deproteinization liquid extract. Under optimal conditions, the coagulant showed satisfactory results. Process optimization was performed using the Box–Behnken design and response surface methodology. Thus, the optimal removal efficiencies predicted using this model for turbidity (99.68%), BOD₅ (97.76%), and COD (82.92%) were obtained at a dosage of 8 mL biocoagulant in 0.5 L of food processing wastewater at an alkaline pH of 11.

A series of benzenesulfonamides incorporating selenazoles with diverse substitution patterns were investigated as inhibitors of six bacterial carbonic anhydrases (CAs, EC 4.2.1.1) from bacterial pathogens, such as Helicobacter pylori (hpCAα was the investigated enzyme), Vibrio cholerae (all the three CAs from this pathogen were considered, VchCAα, VchCAβ and VchCAγ) and Burkholderia pseudomallei (with its two CAs, BpsCAβ and BpsCAγ). All these sulfonamides were effective CA inhibitors, with potencies in the low micromolar or submicromolar range, making them attractive as lead compounds for designing antibacterials with a novel mechanism of action, which could counteract the extensive resistance problem observed with many clinically used antibiotics.