Cerebral Ischemia is a neural disease which causes dying of a number of people every year. The disease usually exposures since stopping the blood pressure and also arresting of heart muscle. HMGB1 is a member of High Mobility Group superfamily proteins which all have a common DNA binding. HMGB1 is released as an extracellular signaling molecule and it binds to Toll like receptors at the cell membrane in the brain cells inflammations. Totally it leads to increase the cytokines and it also intensifies the inflammation. More inflammation can cause the brain cells apoptosis such as neurons and neuroglia cells. Rosamirinic acid, Tanshinone A and Tricin-7 Glucoside which were used for inhibition of HMGB1, they were studied using the Molegro Virtual Docker ans LiganScout softwares in this study. According to the scores, results showed that Tricin- 7 Glucoside had better physical and spatial interactions with HMGB1 and TLR2 than others and also Tanshinone A had the best interaction with TLR4.

Background and the purpose of the study: Boswellia carterii have been used in traditional medicine for many years for management different gastrointestinal disorders. In this study, we wish to report urease inhibitory activity of four isolated compound of boswellic acid derivative.Methods: 4 pentacyclic triterpenoid acids were isolated from Boswellia carterii and identified by NMR and Mass spectroscopic analysis (compounds 1, 3-O-acetyl-9, 11-dehydro-b-boswellic acid; 2, 3-O-acetyl-11-hydroxy-b-boswellic acid; 3.3-O-acetyl-11-keto-b-boswellic acid and 4, 11-keto-b-boswellic acid. Their inhibitory activity on Jack bean urease were evaluated. Docking and pharmacophore analysis using AutoDock 4.2 and Ligandscout 3.03 programs were also performed to explain possible mechanism of interaction between isolated compounds and urease enzyme.Results: It was found that compound 1 has the strongest inhibitory activity against Jack bean urease (IC50=6.27±0.03 mM), compared with thiourea as a standard inhibitor (IC50=21.1±0.3 mM).Conclusion: The inhibition potency is probably due to the formation of appropriate hydrogen bonds and hydrophobic interactions between the investigated compounds and urease enzyme active site and confirms its traditional usage.

Shewanella baltica is an important bacterium with capability of nitrate, sulfur, and Fe (III) bioreduction, and is very important in biodegradation/bioremediation. Existence of potential inhibitors in the environment can affect the effectiveness of bioremediation. Bisphenol-A (BPA) is an important pollutant in environment. Hence this ligand was selected as control ligand first to understand its inhibitory mechanism on diheme cytochrome C of S. baltica; and seconed as a control ligand to compare any other inhibitor with BPA. This study aimed to understand the detailed inhibitory mechanism of BPA, and to investigate whether Aminotriazole have any potential inhibitory effect on recombinant diheme cytochrome C of S. baltica. The 3D structure was obtained from protein data bank. Molegro Virtual Docker used for performing docking process with both MolDock and PLANTS scoring function. Discovery Studio, Ligandscout and MVD were used for visualizing the interaction between ligand and protein. Fifty docking poses were obtained for each method. The results revealed that both BPA and Aminotriazole interact with cytochrome C in active site and non-active site residues at heme groups. BPA as a control inhibitor interacts via hydrogen bonding, hydrophobic and electrostatic interactions, while Aminotriazole interact mostly via hydrogen bond. Moreover, MolDock and PLANTS score of Aminotriazol is much lower than the scores of BPA. Therefore, Aminotriazol may not be an inhibitor regarding the in-silico results and BPA can inhibit cytochrome C of S. baltica.