Objective: The pharmacokinetic parameters of isoniazid and ciprofloxacin administered orally to garlic (Allium sativum) pretreated rats of both sex divided into four groups of five rats per group was determined. Methods: Two groups received ciprofloxacin 20 mg/kg and Isoniazid 15 mg/kg respectively while the other groups received garlic extract for 10 days followed by the administration of ciprofloxacin or Isoniazid on the 11th day. Blood samples were collected from each group at different time interval and plasma concentrations of the drugs determined spectrophotometrically. The pharmacokinetic parameters were determined using the non-compartmental method as implemented in win Nonlin. Secondly, the effect of Allium sativum on the lung penetration of the drugs at same dose range was determined also in rats. Results: Garlic significantly increased the AUC of ciprofloxacin from 119.00±0.962 to 256.32±0.680 and decreased Vd from 1.13±0.172 to 0.90±0.009 and CL from 0.16±0.011 to 0.062±0.001. The AUC of INH was also increased from 491.84±56.765 to 574.04±50.600 and CL was significantly decreased from 0.02±0.007 to 0.01±0.003 where as Vd showed little or no change, (0.397±0.009/0.42±0.143). Garlic increased the maximum concentration of ciprofloxacin achieved in the lung fluid and the time to attain this concentration was delayed, while the maximum concentration of INH achieved in the presence and absence of the herb showed no difference though, the time to attain this concentration were delayed. Conclusion: Our findings therefore suggested that the co-administration of garlic with ciprofloxacin or Isoniazid may pose a negative clinical implication of increased drug toxicity and/or adverse effects.

Computational techniques such as homology modeling and molecular dynamics were used to identify novel intramolecular ioniclock interactions among key charged residues spanning the transmembrane helices and extracellular loops of human complement C3a receptor and the synthetically prepared human C3a receptor ligand SB290157. The results shed light on the active site of the human C3aR and the arginine specificity of the ligand. A strong ionic-lock region with interactions among the charged residues R161 (R4.64), E162 (ER4.65), R340 (R5.42), K96 (K3.36), D167 (D4.70), D417 (D7.35) and H418 (H7.36) is critical for the structural integrity of human C3aR. Results of docking both the stereoisomer of SB290157 with human C3aR indicate that the active site consist of the aromatic residues F107 (F3.37), Y160 (Y4.63), F345 (F5.47), W390 (W6.48), Y393 (Y6.51) and F396 (F6.54) together with the ionic-lock region and reveal the lack of stereospecific preference of human C3aR for SB290157. The active site features of human C3aR and the proposed ligand-binding region may permit the discovery of novel antagonists for C3aR as potential therapeutic agents for conditions such as asthma.

Anthrax is an infectious disease caused by spores of the bacterium, Bacillus anthracis. The B. anthracis spores are highly resistant to inactivation and may be present in the soil, for example, for decades, occasionally infecting grazing animals that ingest the spores. Goats, sheep and cattle are examples of animals that may become infected. Human infection may occur by three routes of exposure to anthrax spores: cutaneous (through the skin), gastrointestinal (by ingestion) and pulmonary (inhalation). A major factor in the virulence of Bacillus anthracis is its secretion of three binary toxins, protective antigen, lethal toxin and edema toxin. These toxins possess a common cell receptor-binding (B) component but have distinct biochemically active (A) components. In traditional vaccine approaches made researchers to produce vaccine very easy. The current approach was based upon the insilico identification of T-Cell Epitopes and its binding affinity with MHC Class II. The T-Cell Epitope was identified using the HLAPred which identifies the peptide class that binds with both MHC Class I and II. Further the Epitope was analyzed for peptide characteristics such as antigenic nature, lipophilicity and solvent assessable. Out of all peptides the peptide which shows all the character for further analyzed for protein peptide interaction to find the high affinity binding peptide with low energy.

Statins are the most prescribed drugs, highly effective in reducing the risk of cardiovascular and cerebrovascular events, primarily by lowering low density lipoprotein (LDL) cholesterol. Although large clinical trials found a 27% average relative risk reduction of major coronary events, there is large variability in benefits from statin therapy. Researchers have found three SNPs (C3435T, G2677T/A, C1236T) of MDR1gene, which codes for P-Glycoprotein (P-gp) (a drug efflux transporter), responsible for the reduced bioavailability of statins. We aimed to design a new drug molecule based on synonymous and nonsynonymous SNPs of MDR1 gene, which is not a substrate to P-gp and acts directly on ßhydroxy methylglutaryl coenzyme A reductase (HMG-CoA), a target site for statins, using Insilico tools. Structural changes in mRNA due to synonymous and nonsynonymous SNPs were evaluated by SNPfold. The 3D structures of normal and mutant proteins of P-gp and HMG-CoA reductase were modeled by Molecular Operating Environment (MOE). A new lead molecule was designed from native structure by VegaZZ and parameters of drug were validated with HyperChem and Pharmacophore mapping was done using LigandScout. We docked the lead molecule with normal and mutant P-gp and found no interactions with P-gp showing that it is not a substrate for P-gp. However, it forms clear hydrogen bond interactions with HMG-CoA reductase. This is a novel approach in the field of bioinformatics and pharmacogenomics (pharmacogenoinformatics) for the development of new drug molecules based on the SNPs of genes involved in drug metabolism in a particular population.