The increasing resistance of pathogens to common antibiotics, as well as the need to control urease activity to improve the yield of soil nitrogen fertilization in agricultural applications, has stimulated the development of novel classes of molecules that target urease as an enzyme. In this context, the newly developed compounds on the basis of 1-heptanoyl-3-arylthiourea family were evaluated for Jack bean urease enzyme inhibition activity to validate their role as potent inhibitors of this enzyme. 1-Heptanoyl-3-arylthioureas were obtained in excellent yield and characterized through spectral and elemental analysis. All the compounds displayed remarkable potency against urease inhibition as compared to thiourea standard. It was found that novel compounds fulfill the criteria of drug-likeness by obeying Lipinski's rule of five. Particularly compound 4a and 4c can serve as lead molecules in 4D (drug designing discovery and development). Kinetic mechanism and molecular docking studies also carried out to delineate the mode of inhibition and binding affinity of the molecules.

• Klíčová slova
• Acyl thioureas, Antioxidant, Jack bean urease, Kinetic mechanism, Lipinski’s rules, Molecular modeling, Urease,
• MeSH
• Canavalia enzymologie   MeSH
• inhibitory enzymů chemie   farmakologie   MeSH
• kinetika MeSH
• molekulární struktura MeSH
• simulace molekulového dockingu * MeSH
• thiomočovina chemie   farmakologie   MeSH
• ureasa antagonisté a inhibitory   metabolismus   MeSH
• vztah mezi dávkou a účinkem léčiva MeSH
• vztahy mezi strukturou a aktivitou MeSH
• Publikační typ
• časopisecké články MeSH
• práce podpořená grantem MeSH
• Názvy látek
• inhibitory enzymů MeSH
• thiomočovina MeSH
• ureasa MeSH

In an attempt to develop a label- and reagent-free electrochemical method for the detection of lectin-glycoprotein interactions, we tested lectin-concanavalin A (ConA), glycoprotein-ovalbumin (Ova) and their complex using chronopotentiometric stripping (CPS) analysis and a hanging mercury drop electrode. Incubation of ConA with Ova resulted in an increase of the CPS peak H of the complex as compared to the CPS peaks of individual Ova and ConA proteins. Qualitatively similar results were obtained with other glycoprotein-lectin couples (ConA-RNase B and lectin from Sambucus nigra-fetuin). Using the CPS method, we were able to follow the course of complex formation in solution. Comparable responses of Ova, ConA and ConA-Ova complex were obtained not only at the mercury electrode but also with solid amalgam electrodes, which are more suitable for parallel analysis. It can be anticipated that electrochemical methods, namely CPS, will find application in glycomics and proteomics.

• Klíčová slova
• Concanavalin A, Constant current chronopotentiometric stripping, Lectin-glycoprotein interactions, Mercury electrodes, Ovalbumin, Protein-protein interactions,
• MeSH
• Canavalia chemie   MeSH
• elektrochemické techniky * MeSH
• konkanavalin A analýza   MeSH
• kur domácí MeSH
• molekulární modely MeSH
• ovalbumin analýza   MeSH
• roztoky MeSH
• zvířata MeSH
• Check Tag
• zvířata MeSH
• Publikační typ
• časopisecké články MeSH
• Názvy látek
• konkanavalin A MeSH
• ovalbumin MeSH
• roztoky MeSH

Hydrophobins are small proteins that play a role in a number of processes during the filamentous fungi growth and development. These proteins are characterized by the self-assembly of their molecules into an amphipathic membrane at hydrophilic-hydrophobic interfaces. Isolation and purification of hydrophobins generally present a challenge in their analysis. Hydrophobin SC3 from Schizophyllum commune was selected as a representative of class I hydrophobins in this work. A novel procedure for selective and effective isolation of hydrophobin SC3 based on solid-phase extraction with polytetrafluoroethylene microparticles loaded in a small self-made microcolumn is reported. The tailored binding of hydrophobins to polytetrafluoroethylene followed by harsh elution conditions resulted in a highly specific isolation of hydrophobin SC3 from the model mixture of ten proteins. The presented isolation protocol can have a positive impact on the analysis and utilization of these proteins including all class I hydrophobins. Hydrophobin SC3 was further subjected to reduction of its highly stable disulfide bonds and to chymotryptic digestion followed by mass spectrometric analysis. The isolation and digestion protocols presented in this work make the analysis of these highly hydrophobic and compact proteins possible.

• Klíčová slova
• Hydrophobin SC3, Isolation, Mass spectrometry, Polytetrafluoroethylene microparticles, Protein analysis,
• MeSH
• albuminy chemie   MeSH
• ananasovník chemie   MeSH
• bromelainy chemie   MeSH
• Canavalia chemie   MeSH
• chymotrypsin chemie   MeSH
• cytochromy c chemie   MeSH
• disulfidy chemie   MeSH
• erytrocyty enzymologie   MeSH
• extrakce na pevné fázi metody   MeSH
• hmotnostní spektrometrie metody   MeSH
• karboanhydrasy chemie   MeSH
• kaseiny chemie   MeSH
• koně MeSH
• konkanavalin A chemie   MeSH
• kur domácí MeSH
• lidé MeSH
• mikrosféry * MeSH
• mléko enzymologie   MeSH
• myokard metabolismus   MeSH
• polytetrafluoroethylen chemie   MeSH
• proteomika metody   MeSH
• Schizophyllum chemie   MeSH
• skot MeSH
• spektrometrie hmotnostní - ionizace laserem za účasti matrice MeSH
• tandemová hmotnostní spektrometrie MeSH
• thermolysin chemie   MeSH
• zvířata MeSH
• Check Tag
• lidé MeSH
• skot MeSH
• zvířata MeSH
• Publikační typ
• časopisecké články MeSH
• práce podpořená grantem MeSH
• Názvy látek
• albuminy MeSH
• bromelainy MeSH
• chymotrypsin MeSH
• cytochromy c MeSH
• disulfidy MeSH
• karboanhydrasy MeSH
• kaseiny MeSH
• konkanavalin A MeSH
• polytetrafluoroethylen MeSH
• thermolysin MeSH

The antiurease activity of the aqueous extracts of 42 plants growing in the Czech Republic was investigated. A phenol-hypochlorite reaction was used for the determination of ammonia produced by urease. The inhibitory activity of the extracts at a concentration of 0.2 mg/mL varied from 17.8% to 80.0%. Extracts from six Potentilla species expressed inhibitory activity against jack bean urease. They were further investigated for their phenolic constituents and the major compounds were subjected to molecular docking. The results revealed that both jack bean urease and Helicobacter pylori urease were inhibited by quercetin-3-O-β-D-galactopyranoside-6″-gallate (1), myricetin-3-O-β-D-glucuronide (2), tiliroside (3) and B-type procyanidin (4). The antiurease activity of the investigated Potentilla species is probably due to the presence of complex phenolic constituents such as flavonoid glycosides and catechin dimers.

• Klíčová slova
• Potentilla species, docking, phenolic constituents, phenol–hypochlorite, urease,
• MeSH
• algoritmy MeSH
• Canavalia enzymologie   MeSH
• fenoly chemie   izolace a purifikace   farmakologie   MeSH
• flavonoidy chemie   izolace a purifikace   farmakologie   MeSH
• galaktosidy chemie   izolace a purifikace   farmakologie   MeSH
• Helicobacter pylori účinky léků   MeSH
• infekce vyvolané Helicobacter pylori farmakoterapie   MeSH
• léčivé rostliny chemie   MeSH
• Potentilla chemie   MeSH
• quercetin analogy a deriváty   MeSH
• ureasa antagonisté a inhibitory   MeSH
• Publikační typ
• časopisecké články MeSH
• práce podpořená grantem MeSH
• Geografické názvy
• Česká republika MeSH
• Názvy látek
• fenoly MeSH
• flavonoidy MeSH
• galaktosidy MeSH
• myricetin 3-O-glucuronide MeSH Prohlížeč
• quercetin-3-O-beta-D-galactopyranoside MeSH Prohlížeč
• quercetin MeSH
• tiliroside MeSH Prohlížeč
• ureasa MeSH