Four groups of novel sulfonamide derivatives: (i) acetoxybenzamide, (ii) triacetoxybenzamide, (iii) hydroxybenzamide and (iv) trihydroxybenzamide, all having thiazole, pyrimidine, pyridine, isoxazole and thiadiazole moieties were prepared and their inhibitory effects were studied on two metalloenzymes, i.e. carbonic anhydrase isozymes (hCA I and II), purified from human erythrocyte cells by Sepharose-4B-l-tyrosine-sulfanilamide affinity chromatography. These enzymes are present in almost all living organisms to catalyse the synthesis of bicarbonate ion (HCO) from carbon dioxide and water. The sulfonamide derivatives were found to be active against hCA I and II in the range of 2.62-136.54 and 5.74-210.58 nM, respectively.
Carbonic anhydrase inhibitors are both in clinical use as antiglaucoma, diuretics, antiepileptics and management of altitude sickness, and under investigation as anticancer, anticonvulsant and antiobesity agents. Sulphonamides have been known for decades as carbonic anhydrase inhibitors and are in clinical use. Sulphonamide derivatives of p-hydroxybenzoic acid and 3,4,5-trihydroxybenzoic acid (gallic acid) were synthesized and their inhibition values over hCA I and hCA II isozymes, purified from human erythrocyte cells by Sepharose-4B-L-tyrosine-sulphanilamide, were determined. Compounds synthesized showed efficient carbonic anhydrase inhibition activity at low nM levels.
The European Water Framework Directive 2000/60/EC requires monitoring of organic priority pollutants in so-called whole water samples, i.e. in aqueous nonfiltered samples that contain natural colloidal and suspended particulate matter. Colloids and suspended particles in the liquid phase constitute a challenge for sample homogeneity and stability. Within the joint research project ENV08 ''Traceable measurements for monitoring critical pollutants under the European Water Framework Directive 2000/60/EC'', whole water test materials were developed by spiking defined amounts of aqueous slurries of ultrafinely milled contaminated soil or sediment and aqueous solutions of humic acid into a natural mineral water matrix. This paper presents the results of an European-wide interlaboratory comparison (ILC) using this type of test materials. Target analytes were tributyltin, polybrominated diphenyl ethers and polycyclic aromatic hydrocarbons in the ng/L concentration range. Results of the ILC indicate that the produced materials are sufficiently homogeneous and stable to serve as samples for, e.g. proficiency testing or method validation. To our knowledge, this is the first time that ready-to-use water materials with a defined amount of suspended particulate and colloidal matter have been applied as test samples in an interlaboratory exercise. These samples meet the requirements of the European Water Framework Directive. Previous proficiency testing schemes mainly employed filtered water samples fortified with a spike of the target analyte in a water-miscible organic solvent. KeywordsWater Framework Directive Á Interlaboratory comparison Á Whole water sample Á Suspended particulate matter Á Polycyclic aromatic hydrocarbons Á Polybrominated diphenyl ethers Á Tributlyltin Electronic supplementary material The online version of this article (
Secondary sulfonamides (4a–8h) incorporating acetoxybenzamide, triacetoxybenzamide, hydroxybenzamide, and trihydroxybenzamide and possessing thiazole, pyrimidine, pyridine, isoxazole and thiadiazole groups were synthesized. Lactoperoxidase (LPO, E.C.1.11.1.7), as a natural antibacterial agent, is a peroxidase enzyme secreted from salivary, mammary, and other mucosal glands. In the present study, the in vitro inhibitory effects of some secondary sulfonamide derivatives (4a–8h) were examined against LPO. The obtained results reveal that secondary sulfonamide derivatives (4a–8h) are effective LPO inhibitors. The Ki values of secondary sulfonamide derivatives (4a–8h) were found in the range of 1.096 × 10−3 to 1203.83 µM against LPO. However, the most effective inhibition was found for N-(sulfathiazole)-3,4,5-triacetoxybenzamide (6a), with Ki values of 1.096 × 10−3 ± 0.471 × 10−3 µM as non-competitive inhibition.
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