10.1016/S0040-4020(01)97712-9
A study on the oxidation of organic sulfur compounds such as disulfides, thiolsulfinate, thiolsulfonate, thiol, sodium thiolate, and sodium sulfinate using superoxide anion generated from potassium superoxide and 18-crown-6-ether under mild conditions. The research, conducted by Shigeo Oae and colleagues at the University of Tsukuba, demonstrates that these compounds are readily oxidized to both sulfinic and sulfonic acids. The study also notes that sulfide and sulfoxide did not react with the superoxide anion. The oxidation reactions were found to be more effective in polar solvents like pyridine and acetonitrile compared to less polar solvents like benzene. The relative reactivities of the compounds were observed in the order: thiolsulfinate > thiolsulfonate > disulfide = sodium thiolate > sodium sulfinate. The study provides insights into the fundamental nature of the reactions of superoxide anion with organic sulfur compounds and discusses the potential involvement of nucleophilic attack and electron transfer processes in these oxidations.
10.1016/j.ejmech.2011.08.005
The research focuses on the discovery and kinetic evaluation of 6-substituted 4-benzylthio-1,3,5-triazin-2(1H)-ones as inhibitors of cathepsin B, a lysosomal cysteine protease with significant roles in both physiological and pathophysiological processes. The study involves the screening of a library of 2,4,6-trisubstituted 1,3,5-triazines and 1,3,5-triazin-2(1H)-ones against three human cathepsins (B, H, and L) and the synthesis of a focused library of new 1,3,5-triazin-2(1H)-ones. The experiments utilized various reactants, including amidine S-(benzyl)isothiourea hydrochloride, ethoxycarbonyl isothiocyanate, and different alkyl or aryl halides, to synthesize the compounds, which were then subjected to enzymatic evaluation. The analyses included detailed kinetics studies to determine the mode of inhibition and the calculation of inhibition constants (Ki and K0) for the compounds. The study revealed that these compounds act as reversible, partial mixed-type inhibitors of cathepsin B with low micromolar inhibitory constants, showing selectivity for cathepsin B over cathepsin H.
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