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Biodegradation of environmentally hazardous synthetic dyes by enzymes has been achieved the highest interest in recent years. In this work, we optimized Remazol Brilliant Blue R (RBBR) dye biodegradation by Arthrographis kalrae derived laccase via the Box-Behnken design (BBD) approach of the surface response methodology (RSM). Optimization of dye decolourisation by one variable at a time (OVAT) approach resulted in optimal dye decolourisation at laccase dose (2 IU mL-1), pH (7.0), temperature (35 °C), incubation time (240 min), and initial dye concentration (100 mg L-1). The optimized process through BBD enhanced dye decolourisation (97.18%). Fourier Transform Infrared Spectroscopy and UV-Visible Spectrophotometry have proven biodegradation. In addition, in comparison to untreated samples, the laccase-treated dye sample showed relatively less phyto- and cytotoxic effect on Allium cepa L. Extra Precision Glide docking exhibited the binding affinity score of -5.355 kcal mol-1, between laccase-RBBR complex.

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Systems-biology inspired identification of drug targets and machine learning-based screening of small molecules which modulate their activity have the potential to revolutionize modern drug discovery by complementing conventional methods. To utilize the effectiveness of such pipelines, we first analyzed the dysregulated gene pairs between control and tumor samples and then implemented an ensemble-based feature selection approach to prioritize targets in oral squamous cell carcinoma (OSCC) for therapeutic exploration. Based on the structural information of known inhibitors of CXCR4-one of the best targets identified in this study-a feature selection was implemented for the identification of optimal structural features (molecular descriptor) based on which a classification model was generated. Furthermore, the CXCR4-centered descriptor-based classification model was finally utilized to screen a repository of plant derived small-molecules to obtain potential inhibitors. The application of our methodology may assist effective selection of the best targets which may have previously been overlooked, that in turn will lead to the development of new oral cancer medications. The small molecules identified in this study can be ideal candidates for trials as potential novel anti-oral cancer agents. Importantly, distinct steps of this whole study may provide reference for the analysis of other complex human diseases.

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AIM: The aim of this study was to investigate the antioxidant and hepatoprotective effects of the polyherbal formulation (PHF)containing Cajanus cajan (L.)Millsp., Lawsonia inermis L. Linn, Mimosa pudica L., Uraria picta (Jacq.)DC. and Operculina turpethum (L.)Silva Manso on carbon tetrachloride (CCl4)induced acute liver damage in albino rats. MATERIALS AND METHODS: The groups of animals were administered with PHF at the doses 100, 200 and 400 mg/kg b.w. (per oral [p.o.])once in a day for 7 days and at day 6th and 7th the animals were administrated with Carbon tetrachloride (1.0 mL/kg b.w. 50% v/v with olive oil,; p.o.). The effect of PHF on serum glutamine pyruvate transaminase (SGPT), serum glutamine oxaloacetate transaminase, alkaline phosphatase (ALP)and total bilirubin were determined in CCl4 - induced hepatotoxicity in rats. Further, the effects of PHF on glutathione (GSH), superoxide dismutase (SOD)level and lipid peroxidation (LPO)activity were also investigated. RESULTS: The results demonstrated that PHF (400 mg/kg b.w.)significantly reduces the CCl4 induced increase in level of serum SGPT, serum ALP and total bilirubin. PHF (400 mg/kg b.w.)prevents the depletion level of GSH and decrease in the activity of SOD in CCl4 -induced liver injury in rats. In addition, PHF also showed a significant decrease in the LPO levels signifying the potent antioxidant activity. CONCLUSION: All our findings suggest that PHF could protect the liver cells from CCl4 - induced liver damages and the mechanism may be through the anti-oxidative effect of PHF.

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Shiga toxins are one of the very potent agents for causing dysentery, diarrhoea and haemolytic uremic syndrome with very low LD50. For better understanding of their biology, detection and neutralization, the components of toxins are needed to be expressed and purified in bulk amounts. However, following traditional expression procedures, this task is very tedious as the yield of the toxin is very low. In this manuscript, we have described the optimization of media for enhanced production of recombinant Shiga toxin B (rStx-B) chain protein in Escherichia coli. This protein is known to have neutralization ability against shiga toxins. Furthermore, fed-batch cultivation process in E. coli was also developed in the optimized medium. Expression was induced with 1 mM isopropyl-beta-thiogalactoside (IPTG). The purification of protein involved Ni-NTA affinity chromatography under native conditions followed by gel filtration chromatography. After fed-batch cultivation, the recombinant E. coli resulted in cell weight and purified protein of about 19.41 g/l (dry cell weight, 11.38 g/l) and 30 mg/l of culture, respectively. The purity of the recombinant StxB protein was checked by sodium dodecyl sulfate polyacrylamide gel electrophoresis analysis. Reactivity of this protein was determined by Western blotting as well as indirect ELISA using specific antibodies. These results establish the application of this protein for diagnosis of shiga toxin infection or for neutralizing the toxicity.

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