Co-Inheritance of alpha-thalassemia and sickle cell disease in a cohort of Angolan pediatric patients

Molecular Biology Reports - The aim of this study was to explore the association between alpha-thalassemia, fetal hemoglobin, hematological indices, and clinical adverse events in Angolan sickle...     

Purification and properties of a coagulant thrombin-like enzyme from the venom of Bothrops leucurus

A thrombin-like enzyme from Bothrops leucurus venom, named leucurobin (leuc), was purified by gel filtration, affinity and ion exchange chromatographies. Physicochemical studies indicated that the purified enzyme is a 35 kDa monomeric glycoprotein on SDS-PAGE under reducing conditions, which decreased to 29 kDa after deglycosylation with N-glycosidase F (PNGase F). The amino acid sequence of leuc was determined by automated sequencing of the intact native protein and peptides produced by digestion of the S-pyridyl-ethylated protein with trypsin. The protein sequence exhibits significant similarities with other serine proteases reported from snake venoms, and contains two potential sites of N-linked glycosylation. The proteinase split off fibrinopeptide A (FPA) rapidly from human fibrinogen; however, only negligible traces of fibrinopeptide B (FPB) were observed. In addition, the enzyme released the N-terminal peptide (Mr=4572) containing the first 42 residues from the Bbeta-chain. Leuc could neither activate factor XIII nor release kinins from heat-treated bovine plasma. Its specific clotting activity was equivalent to 198 NIH thrombin U/mg on human fibrinogen. Kinetic properties of leuc were determined using representative chromogenic substrates. The enzyme evoked the gyroxin syndrome when injected into the tail veins of mice at levels of 0.143 microg/g mouse. The inhibitory effects of PMSF and benzamidine on the amidolytic activity suggest that leuc is a serine proteinase, and inhibition by beta-mercaptoethanol revealed the important role of the disulfide bonds in the stabilization of the native structure. Antibothropic serum, SBTI and EDTA had little or no effect on its amidolytic activity. However, the clotting effect of the enzyme was strongly inhibited by antibothropic serum. A Dixon plot showed that the hydrolysis of Bz-L-Arg-pNA by leuc was competitively inhibited by benzamidine (Ki=1.61+/-0.25 mM).     

Successful Treatment of Canine Sporotrichosis with Terbinafine: Case Reports and Literature Review

Sporotrichosis occurs worldwide, and the metropolitan region of Rio de Janeiro, Brazil, is a main endemic area, with a large number of human and animal cases in the last 19 years. This mycosis is more frequently described in cats rather than in dogs. There are a limited number of oral antifungal agents for the treatment of sporotrichosis in animals. In this context, the effectiveness of terbinafine in the treatment of sporotrichosis in humans, as well as the promising results of in vitro susceptibility tests, inspired us to use this drug in the therapy of this mycosis in dogs. We reported for the first time the use of terbinafine in the treatment of two dogs with sporotrichosis caused by Sporothrix brasiliensis. Moreover, we provided an overview of therapeutic features of canine sporotrichosis cases reported since the 1960s. One of the dogs presented the fixed cutaneous form of the disease, while the other patient presented hyperemia of the nasal mucosa and respiratory signs only. Terbinafine showed high antifungal activity in vitro against the canine Sporothrix isolates. The dogs were successfully treated with terbinafine, with remission of all clinical signs initially presented. The current reports indicate that this drug can emerge as a therapeutic option for canine sporotrichosis.     

Antimicrobial efficacy of alcohol-based hand gels with a 30-s application

Aims: The objective of this study was to assess the antimicrobial efficacy of alcohol‐based hand gels according to European Norm 1500 (EN 1500). Methods and Results: We assessed the antimicrobial efficacy of 12 alcohol‐based hand gels produced in Brazil, containing 70% w/w or v/v ethyl alcohol as the active ingredient, according to EN 1500, with a 30‐s application. In addition, 70% w/w ethyl alcohol and three alcohol‐based hand rubs commonly used in Europe and effective according to EN 1500 were also tested. Eight of 12 (67%) alcohol‐based hand gels produced in Brazil failed by EN 1500. In contrast, 70% w/w ethyl alcohol and European alcohol‐based hand rubs were approved by EN 1500. Conclusions: In this study, the majority of Brazilian alcohol‐based hand gels showed limited efficacy on hand hygiene within 30 s. Significance and Impact of the Study: The findings of this study may be used as an important argument to motivate Brazilian manufacturers to improve the antimicrobial efficacy of alcohol‐based hand gels, because it is prudent to suppose that alcohol‐based hand gels can be recommended for use in healthcare settings only if they show antimicrobial activity at least similar to that of alcohol‐based liquid preparations, including the traditional 70% w/w ethyl alcohol.     

Inhibition of α-Glycosidase by Lippia dulcis Trevir. (Verbenaceae) Preparations,Quantification of Verbascoside,and Study of Its Molecular Docking

This study aimed to quantify verbascoside (VEB), perform molecular docking studies of VEB with the α-glucosidase (GL) of Bacillus stearothermophilus, and evaluate the inhibition of the enzyme by L. dulcis preparations. The substrate concentration and presence of reduced glutathione were evaluated for their effect on the in vitro inhibition of the GL enzyme. Assays were also performed in the presence and absence of simulated gastric fluid. The antidiabetic fractions 2 and 3 were the most inhibited GL, but their activity were significantly decreased in the presence of gastric fluid. Chromatographic analyses confirmed the predominant presence of VEB in the samples. The samples had VEB concentrations between 49.9 and 243.5 mg/g. Simulation of the molecular docking of VEB were consistent with its GL-inhibitory activity. It can conclude that the crude ethanol extract and fractions show inhibitory activity against the GL enzyme.