Electrocatalytic glycol cleavage by periodate / iodate redox system under phase transfer conditions

Oxidative cleavage of glycols and related compounds by electrogenerated periodate in a 2-phase anolyte employing phase transfer catalysis is reported. A divided cell with lead dioxiode anode is used to generate periodate which is transferred to the organic phase where oxidation takes place. The iodate formed in this step is transferred back to the aqueous phase and reoxidises to periodate at the anode, completing the catalytic cycle. Iodate can be taken in substoichiometric quanitity. Conversion and selectivity for aldehyde are hiWi in the oxidation of hydrobenzoin, benzoin and erythro -9, IO-dihydroxyoctadecanoic acid

Influence of Sacrificial Cathodic Protection on the Chloride Profile in Concrete

The durability of reinforced concrete structures significantly depends on the condition of the steel embedded in them. Structures exposed to chloride containing environment have reduced durability due to corrosion of the reinforcement steel. Several diffusion models have been proposed for chloride penetration. They mainly aim at predicting the initiation of corrosion of the reinforcement. They are based on diffusion conditions influenced by parameters such as relative humidity, temperature, rains etc. This work presents the influence of sacrificial cathodic protection on the chloride profile in concrete. Cathodic protection to the embedded steel in concrete was established by plugging-in a sacrificial magnesium alloy anode at the center of the slab and providing an electrical link between them. The current flowing between the magnesium anode and the embedded steel was regularly measured. The water soluble chloride content at different distances from the anode and at different times was determined after implementation of cathodic protection. The chloride content decreased at different distances from the anode, with increase in time. The diffusion of chloride occurred at a more accelerated rate due to the flow of cathodic protection current

Synthesis, spectral characterisations, biological evaluation, DFT calculation and molecular docking analysis of 3,5-diethyl-2,6-di(2-bromophenyl)piperidin-4-one picrate with topological indices studies

The 3,5-diethyl-2,6-di(2-bromophenyl)piperidin-4-one picrates (3,5-DEBPP) compound was synthesised and characterised by spectral techniques. The title molecule adopt a normal chair conformation with all of its substituents, such as the bromophenyl group at positions C-2 and C-6 and the ethyl group at locations C-3 and C-5, orientated equatorially, according to the measured chemical shifts and coupling constants. The DFT/B3LYP/6-311++G(d,p) basis set was used to optimise the molecular structure. The non-linear optical behaviour of the material was assessed by computing the first order hyperpolarisability. Using NBO analysis, it was determined whether the molecule's stability as a result of hyper conjugative interactions and charge delocalisation was satisfactory. The HOMO and LUMO values were used to compute the physico-chemical parameters. The electrophilic and nucleophilic attack of the current molecule is visible on the MEP surface. The Escherichia coli, Staphylococcus aureus, Bacillus subtilis, Vibreo cholerae, Pseudomonas aeruginosa, Candida albicans, Aspergillus niger, Aspergillus flavus and Trichophyton rubrum were among the bacterial strains that the 3,5-DEBPP was tested against. Docking investigations were thoroughly conducted to establish knowledge regarding the interactions between protein and this new chemical theoretically. Structure-based topological indices enable prediction of chemical properties and the bioactivities of this compound through quantitative structure–activity and structure–property relationships methods.</p

Exploring the Binding Interaction Mechanism of Taxol in β-Tubulin and Bovine Serum Albumin: A Biophysical Approach

In this present study on understanding the taxol (PTX) binding interaction mechanism in both the β-tubulin and bovine serum albumin (BSA) molecule, various optical spectroscopy and computational techniques were used. The fluorescence steady-state emission spectroscopy result suggests that there is a static quenching mechanism of the PTX drug in both β-tubulin and BSA, and further time-resolved emission spectroscopy studies confirm that the quenching mechanism exists. The excitation-emission matrix (EEM), Fourier transform infrared, and resonance light scattering spectra (FT-IR) confirm that there are structural changes in both the BSA and β-tubulin molecule during the binding process of PTX. The molecular docking studies revealed the PTX binding information in BSA, β-tubulin, and modeled β-tubulin and the best binding pose to further subject the molecular dynamics simulation, and this study confirms the stability of PTX in the protein complex during the simulation. Density functional theory (DFT) calculations were performed between the free PTX drug and PTX drug (single point) in the protein molecule active site region to understand the internal stability. © 2019 American Chemical Society

Comparative Binding Analysis of N-Acetylneuraminic Acid in Bovine Serum Albumin and Human α-1 Acid Glycoprotein

The present study focuses on the determination of the biologically significant N-acetylneuraminic acid (NANA) drug binding interaction mechanism between bovine serum albumin (BSA) and human α-1 acid glycoprotein (HAG) using various optical spectroscopy and computational methods. The steady state fluorescence spectroscopy result suggests that the fluorescence intensity of BSA and HAG was quenched by NANA in a static mode of quenching. Further time-resolved emission spectroscopy measurements confirm that mode of quenching mechanism of NANA in the BSA and HAG system. The FT-IR, excitation-emission matrix and circular dichroism (CD) analysis confirms the presence of NANA in the HAG, BSA system, and fluorescence resonance energy transfer analysis shows that NANA transfers energy between the HAG and BSA system. The molecular docking result shows good binding affinity in both protein complexes, and further molecular dynamics simulations and charge distribution analysis were performed to gain more insight into the binding interaction mechanism of NANA in the HAG and BSA complex. © 2018 American Chemical Society