Screening of the anticonvulsant activity of some plants from Fabaceae family in experimental seizure models in mice

Fabaceae is the third largest family of flowering plants. Lack of essential oils in the plants of this family can be an advantage in search for safe and effective medicines. In this study the anticonvulsant effect of the leaves of Albizzia julibrissin, Acacia juliflora, Acacia nubica and aerial parts of Astragalus obtusifolius was evaluated in pentylenetetrazole [PTZ] and maximal electroshock [MES] seizure tests. The hydroalcoholic extracts of the plants were obtained by percolation. Different doses of the extracts were injected to the mice intraperitoneally [i.p.] and occurrence of clonic seizures induced by PTZ [60 mg/kg, i.p.] or tonic seizures induced by MES [50 mA, 50Hz, 1sec] were monitored up to 30 min after administration. Acute toxicity of the extracts was also assessed. The safe and effective extract was then fractionated by dichloromethane and anticonvulsant activity of the fractions was determined. Finally, the constituents of the extract and the fractions were screened by thin layer chromatography. Among the extracts, only A. obtusifolius extract showed low toxicity and protective effect against clonic seizures with ED50 value of 3.97 g/kg. Fractionation of the extract led to increase in anticonvulsant activity and ED50 value of 2.86 g/kg was obtained for the aqueous fraction. Phytochemical screening revealed the presence of alkaloids, flavonoids, anthrones and saponins in the aqueous fraction. The presence of anticonvulsant compounds in A. obtusifolius suggests further activity-guided fractionation and analytical studies to find out the potential of this plant as a source of anticonvulsant agent

[Evaluation the immunogenesity structure of HIV recombinant protein gp41-p24]

HIV recombinant proteins can be used as immunogen and inducer of immune system. The gag and env proteins are among the most important ones that are located on internal and surface sections, respectively. In this study, we considered the immunogenisity structure of HIV recombinant protein gp41-p24, which has not yet been studied in detail before. In the present study, the HIV recombinant protein gp41-p24 was prepared by cloning methods and kept as unfolded. Using the dilution procedure, unfolded protein was changed to refolded state. The molecular weight and concentration of protein [refolded and unfolded] was measured by electrophoresis and spectrophotometer methods. The measurement of refolded protein can be estimated by native gel and circular dichroism method [CD] based on secondary structure of the protein. Immunological activity and immunogenic structure of these two proteins, based on protein type and optical density was recorded by ELISA and western blot methods. Our results showed that molecular weight of each protein was 32 KD and also they were pure. The refolded protein was observed by native gel method. In the above protein compared with the unfolded one, increased content of helix and beta strand structures and decreased random form was shown. Immune reaction with the antibodies in the serum of HIV positive control patients was observed in the standard and refolded proteins. There was no significant difference based on the protein type. Our research indicated that the HIV recombinant protein gp41-p24, after refolding, has immunogenic activity and we suggest its application as an immunogen in immunization and stimulation of immune system