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Kinetics of homogeneous degradation of Eosin Y (EY), also known as Acid red 87 (CI 45380), are studied, mostly using Fenton's process, at 30˚C by monitoring its absorbance at 517 nm (λ max of EY). This process is one of the advanced oxidation processes (AOPs). Mixture of H 2 O 2 and Fe(II) ion in acetate buffer medium (pH 2.74 -4.56) generates hydroxyl free radicals (• OH) which attack the dye molecules, resulting in degradation of the dye molecules. Results show that the initial rate of EY degradation decreases with the increasing of solution pH because of removal of kinetically important Fe (iron) species through formation of ferric hydroxide. On the other hand, the rate increases with increasing the concentrations of H 2 O 2 , Fe(II) and EY at low solution pH. The initial rate increases with increasing of concentration of H 2 O 2 and, subsequently remains unaffected with further increase of its concentration at a constant Fe(II) concentration because of the enhanced scavenging environment created by H 2 O 2 at its higher concentration. The initial rate also increases with increasing of concentration of Fe(II) at a constant H 2 O 2 concentration and remains unaffected with its further increase. EY concentration also enhances the initial rate at low pH. However, the initial rate is significantly enhanced by UV light. This is because of formation of additional hydroxyl radicals through excitation of the dye molecules by UV light. During the period of experiment, EY in aqueous solution alone hardly suffered any degradation. Degradation mechanism of EY by the Fenton and photo-Fenton's processes is also discussed. Statistical analysis was used to validate the experimental results. Low values of the standard deviation for both the initial rate and % degradation indicated the consistency of the experimental data.How to cite this paper: Hossain, A., Rayhan, A.B.M.S., Raihan, M

In this study, we have investigated the binding mechanism of two FDA approved drugs (ivermectin and levosalbutamol) with the spike protein of SARs-CoV-2 using three different computational modeling techniques. Molecular docking results predict that ivermectin shows a large binding affinity for spike protein (-9.0 kcal/mol) compared to levosalbutamol (-4.1 kcal/mol). Ivermectin binds with GLN492, GLN493, GLY496 and TRY505 residues in the spike protein through hydrogen bonds and levosalbutamol binds with TYR453 and TYR505 residues. Using density functional theory (DFT) studies, we have calculated the binding energies between ivermectin and levosalbutamol with residues in spike protein which favor their binding are − 17.8 kcal/mol and − 20.08 kcal/mol, respectively. The natural bond orbital (NBO) charge analysis has been performed to estimate the amount of charge transfer that occurred by two drugs during interaction with residues. Molecular dynamics (MD) study confirms the stability of spike protein bound with ivermectin through RMSD and RMSF analyses. Three different computer modeling techniques reveal that ivermectin is more stable than levosalbutamol in the active site of spike protein where hACE2 binds. Therefore, ivermectin can be a suitable inhibitor for SARS-CoV-2 to enter into the human cell through hACE2.

Detection of virulence gene is a key component in determining the pathogenicity of any isolates because these genes act multi-functionally and multi-factorially. Gyrase specific gene primer in combination of PCR technology allows precise detection of DNA gyrase subunit B2 gene (gyrB2) from different virulent microorganisms. In the present study, forward and reverse primers with a length of 20bp for both were used for detection of gyrB2 genes in clinical isolates of Pseudomonas sp. collected from patients suffering from urinary tract infection (UTI). A total of 12 isolates of Pseudomonas sp. viz., Ps1, Ps2, Ps3, Ps4, Ps5, Ps6, Ps7, Ps8, Ps9, Ps10, Ps11 and Ps12 were used in present study in which gyrB2 gene amplified in all 12 isolates and gave the expected 1130bp PCR product after visualization under gel documentation system in 1.2% agarose gel. This PCR was outstanding in the detection of gyrB2 gene in urinary tract infected patients caused by Pseudomonas sp. species.DOI: http://dx.doi.org/10.3329/icpj.v1i9.11612 International Current Pharmaceutical Journal 2012, 1(9): 235-238

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