PubMed · 2453323
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1988-03-07. Treating scabies.. https://pubmed.ncbi.nlm.nih.gov/2453323/
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The effects of several environmental factors on the dissipation, transformation, and mineralization of isoxaflutole were investigated in laboratory incubations. In the soil, isoxaflutole hydrolyzed to a diketonitrile derivative, which is the active form of the herbicide. The diketonitrile was then metabolized to an inactive benzoic acid derivative and later into two unknown products, which were found only in small quantities. Degradation of isoxaflutole was faster in soil maintained at -100 or -1500 kPa compared to that in air-dry soil. At 25 degrees C, the half-lives for isoxaflutole were 9.6, 2.4, and 1.5 days in air-dry, -1500 kPa, and -100 kPa moisture regimes, respectively. A simple Arrhenius expression described the response of isoxaflutole transformation (mineralization and transformation) to temperature in the range of 5 to 35 degrees C. An activation energy value (E(a)) of 67 kJ/mol for isoxaflutole suggested the transformation of the herbicide to the diketonitrile derivative was primarily a chemical reaction. Moreover, biological activity had little effect on the hydrolysis of isoxaflutole, with half-lives of 1.8 and 1.4 days in sterile and nonsterile soil, respectively. However, the transformation of diketonitrile to benzoic acid and the production of the unknown products were greatly reduced in the sterile soil, suggesting one or more biologically mediated processes.
The human immunodeficiency virus type 1 (HIV-1) is a major health problem worldwide. In this study, 17 analogues of L-chicoric acid, a potent inhibitor of HIV integrase, were studied. Of these analogues, five submicromolar inhibitors of integrase were discovered and 13 compounds with activity against integrase at less than 10 microM were identified. Six demonstrated greater than 10-fold selectivity for HIV replication over cellular toxicity. Ten analogues inhibited HIV replication at nontoxic concentrations. Alteration of the linkages between the two bis-catechol rings, including the use of amides, mixed amide esters, cholate, and alkyl bridges, was explored. Amides were as active as esters but were more toxic in tissue culture. Alkyl and cholate bridges were significantly less potent against HIV-1 integrase in vitro and were inactive against HIV-1 replication. Two amino acid derivates and one digalloylderivative of L-chicoric acid (L-CA) showed improved selectivity over L-CA against integration in cell culture. These data suggest that in addition to the bis-catechols and free carboxylic acid groups reported previously, polar linkages are important constituents for optimal activity against HIV-1 integrase and that new derivatives can be developed with increased specificity for integration over HIV entry in vivo.
Bacteria grow on multicomponent substrates in most natural and engineered environments. To advance our ability to model bacterial growth on such substrates, axenic cultures were grown in chemostats at a low specific growth rate and a constant total energy flux on binary and ternary substrate mixtures and were assayed for key catabolic enzymes for each substrate. The substrates were benzoate, salicylate, and glucose, and the enzymes were catechol 1,2-dioxygenase, gentisate 1,2-dioxygenase, and glucose-6-phosphate dehydrogenase, respectively. The binary mixtures were salicylate with benzoate and salicylate with glucose. Measurements were also made of oxygen uptake rate by whole cells in response to each substrate. The effects of the substrate mixture on the oxygen uptake rate paralleled the effects on the measured enzymes. Catechol 1,2-dioxygenase exhibited a threshold response before synthesis occurred. Below the threshold flux of benzoate through the chemostat, either basal enzyme levels or nonspecific enzymes kept reactor concentrations too low for enzyme synthesis. Above the threshold, enzyme levels were linearly related to the fraction of the total energy flux through the chemostat due to benzoate. Gentisate 1,2-dioxygenase exhibited a linear response to the salicylate flux when mixed with benzoate, but a threshold response when mixed with glucose. Glucose-6-phosphate dehydrogenase activity increased in direct proportion to the glucose flux through the chemostat over the entire range studied. The results from two ternary mixtures were consistent with those from the binary mixtures.