thiourea and formamide

This research article presents the preparation and characterization of monolithic capillary columns with incorporated bare fumed silica nanoparticles (FSNPs) and surface coated gluconamide FSNPs and their subsequent use in hydrophilic interaction capillary electrochromatography (HI-CEC) of small relatively polar solutes. The monolithic support was based on the in situ polymerization of glyceryl monomethacrylate (GMM) and ethylene glycol dimethacrylate (EDMA) yielding the poly(GMM-co-EDMA) monolith for the incorporation of bare and gluconamide-FNSPs. The poly(GMM-co-EDMA) monolith functioned as a true "support" for both types of polar FSNPs "stationary phases". In other words, monolithic capillary columns with "FSNPs stationary phases" were obtained in the sense that the contribution of the monolith proper to solute' retention was at its minimum. The gluconamide-FSNPs were obtained by reacting the FSNPs with the polar organosilane N-(3-triethoxysilylpropyl)gluconamide either by a pre- or on-column approach yielding p-gluconamide-FSNPs or o-gluconamide-FSNPs, respectively. While the p-gluconamide-FSNPs was coated by an oligosiloxane gluconamide layer as revealed by thermogravimetric analysis, the o-gluconamide-FSNPs are thought to be covered with a monomeric layer of gluconamide ligands as was manifested by the higher plate number obtained on the latter than on the former gluconamide-FSNPs incorporated monolithic columns. In the on-column modification process of FSNPs, the reaction was performed in a closed system whereby atmospheric water vapor are not available to cause the polymerization of the trifunctional organosilane N-(3-triethoxysilylpropyl)gluconamide. Also, the fact that the o-gluconamide-FSNPs incorporated monoliths were made from bare-FSNPs incorporated monoliths may indicate that the bare FSNPs were better dispersed into the monolithic matrix than the p-gluconamide-FSNPs, a condition that might have further contributed to the lower plate count obtained on p-gluconamide- than o-gluconamide-FSNPs incorporated monolithic columns. Overall, o-gluconamide-FSNPs stationary phases and to a lesser extent bare-FSNPs stationary phases proved useful in HI-CEC of small polar solutes, including DMF, formamide, thiourea, some phenols and nucleobases.

Topics: Capillary Electrochromatography; Dimethylformamide; Formamides; Gluconates; Glycerides; Hydrophobic and Hydrophilic Interactions; Methacrylates; Nanoparticles; Phenols; Polymerization; Purines; Pyrimidines; Silicon Dioxide; Thiourea

Expression of urea transporter UT-B confers high urea permeability to mammalian erythrocytes. Erythrocyte membranes also permeate various urea analogues, suggesting common transport pathways for urea and structurally similar solutes. In this study, we examined UT-B-facilitated passage of urea analogues and other neutral small solutes by comparing transport properties of wildtype to UT-B-deficient mouse erythrocytes. Stopped-flow light-scattering measurements indicated high UT-B permeability to urea and chemical analogues formamide, acetamide, methylurea, methylformamide, ammonium carbamate, and acrylamide, each with P(s)>5.0 x 10(-6) cm/s at 10 degrees C. UT-B genetic knockout and phloretin treatment of wildtype erythrocytes similarly reduced urea analogue permeabilities. Strong temperature dependencies of formamide, acetamide, acrylamide and butyramide transport across UT-B-null membranes (E(a)>10 kcal/mol) suggested efficient diffusion of these amides across lipid bilayers. Urea analogues dimethylurea, acryalmide, methylurea, thiourea and methylformamide inhibited UT-B-mediated urea transport by >60% in the absence of transmembrane analogue gradients, supporting a pore-blocking mechanism of UT-B inhibition. Differential transport efficiencies of urea and its analogues through UT-B provide insight into chemical interactions between neutral solutes and the UT-B pore.

Topics: Acrylamide; Animals; Cell Membrane Permeability; Diffusion; Erythrocytes; Formamides; Lipid Bilayers; Membrane Transport Proteins; Methylurea Compounds; Mice; Mice, Transgenic; Thiourea; Urea

The permeability of the Na channel of squid giant axon to organic cations and small nonelectrolytes was studied. The compounds tested were guanidinium, formamidinium, and 14C-labeled urea, formamide, thiourea, and acetone. Permeability was calculated from measurements of reversal potential and influx on internally perfused, voltage clamped squid axons. The project had two objectives: (1) to determine whether different methods of measuring the permeability of organic cations yield similar values and (2) to see whether neutral analogs of the organic cations can permeate the Na channel. Our results show that the permeability ratio of sodium to a test ion depends upon the ionic composition of the solution used. This finding is consistent with the view put forward previously that the Na channel can contain more than one ion at a time. In addition, we found that the uncharged analogs of permeant cations are not measurably permeant through the Na channel, but instead probably pass through the lipid bilayer.

Topics: Acetone; Animals; Axons; Cell Membrane Permeability; Decapodiformes; Electric Conductivity; Formamides; Guanidines; Ion Channels; Membrane Potentials; Sodium; Structure-Activity Relationship; Thermodynamics; Thiourea; Urea

Acetamide and N-methylurea have been shown for the first time to be substrates for jack bean urease. In the enzymatic hydrolysis of urea, formamide, acetamide, and N-methylurea at pH 7.0 and 38 degrees C, kcat has the values 5870, 85, 0.55, and 0.075 s-1, respectively. The urease-catalyzed hydrolysis of all these substrates involves the active-site nickel ion(s). Enzymatic hydrolysis of the following compounds could not be detected: phenyl formate, p-nitroformanilide, trifluoroacetamide, p-nitrophenyl carbamate, thiourea, and O-methylisouronium ion. In the enzymatic hydrolysis of urea, the pH dependence of kcat between pH 3.4 and 7.8 indicates that at least two prototropic forms are active. Enzymatic hydrolysis of urea in the presence of methanol gave no detectable methyl carbamate. A mechanism of action for urease is proposed which involves initially an O-bonded complex between urea and an active-site Ni2+ ion and subsequently an O-bonded carbamato-enzyme intermediate.

Topics: Acetamides; Benzoates; Benzoic Acid; Carbamates; Fluoroacetates; Formamides; Hydrogen-Ion Concentration; Kinetics; Methylurea Compounds; Models, Chemical; Nitrobenzenes; Phenylcarbamates; Structure-Activity Relationship; Substrate Specificity; Thiourea; Trifluoroacetic Acid; Urea; Urease

Topics: 1-Propanol; Alcohols; Amides; Anesthesia; Anura; Biological Transport; Cytoplasm; Ethanol; Formamides; Methanol; Muscles; Permeability; Research; Thiourea