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EN
Developing catalyst is very significant for biologically important reactions which yield products, used as drugs. Mechanistic study on meso-tetraphenylporphyriniron(III) chloride (TPP) catalysed oxidation of indole by sodium perborate in aqueous acetic acid medium have been carried out. The reaction follows a fractional order with respect to substrate and catalyst. The order with respect to oxidant was found to be one. Increase in the percentage of acetic acid and increase in the concentration of [H+] decreased the rate. The reaction fails to initiate polymerization, and a radical mechanism is ruled out. Activation and thermodynamic parameters have been computed. A suitable kinetic scheme based on these observations has been proposed. Significant catalytic activity is observed for the reaction system in the presence of TPP.
EN
A simple, low cast and efficient solvent-free procedure for the preparation of bis(in -dolyl)methanes via condensation of indoles with aldehydes as well as ketones in the presence of catalytic amount of magnesium sulfate (MgSO4) is described. The reactions proceed rapidly in high yields at 50°C.
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Content available remote Alkylation of ambident indole anion in ionic liquids
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EN
Alkylation of indole salts in different ionic liquids is reported. Ionic liquids increase the alkylation reaction rate of ambident indole anion and reduce the effects of counter ions and/or additives, the alkylation reaction rates being independent of the presence of small amounts of protic solvents or water. [...]
EN
Based on overlapping structural requirements for both efficient aldose reductase inhibitors and PPAR ligands, [5-(benzyloxy)-1H-indol-1-yl]acetic acid (compound 1) was assessed for inhibition of aldose reductase and ability to interfere with PPARγ. Aldose reductase inhibition by 1 was characterized by IC50 in submicromolar and low micromolar range, for rat and human enzyme, respectively. Selectivity in relation to the closely related rat kidney aldehyde reductase was characterized by approx. factor 50. At organ level in isolated rat lenses, compound 1 significantly inhibited accumulation of sorbitol in a concentration-dependent manner. To identify crucial interactions within the enzyme binding site, molecular docking simulations were performed. Based on luciferase reporter assays, compound 1 was found to act as a ligand for PPARγ, yet with rather low activity. On balance, compound 1 is suggested as a promising lead-like scaffold for agents with the potential to interfere with multiple targets in diabetes.
EN
This work is devoted to study how immobilization in the PVA films affects the fluorescence and phosphorescence lifetime of indole and its derivatives. The obtained results indicated that immobilization of the studied indoles in the PVA matrix, which leads to the increased microrigidity of the environment around the indole moiety, results in the increase of singlet and triplet excited state lifetime of the studied compounds. Most probably, the enhancement of the rigidity of the environment near the chromophore reduces the rates of the non-radiative deactivation pathways, which leads to the increase of excited state lifetimes of the studied compounds.
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