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At least 19 recordsLinked to original sources
PubMed1975

Sulfonamide resistance mechanism in Escherichia coli: R plasmids can determine sulfonamide-resistant dihydropteroate synthases.

Several natural isolate E. coli strains highly resistant to sulfonamides and antibiotics are shown to contain a sulfonamide-resistant dihydropteroate synthase (2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine-diphosphate:4-aminobenzoate 2-amino-4-hydroxydihydropteridine-6-methenyltransferase, EC 2.5.1.15) in addition to the normal sensitive enzyme. The resistant dihydropteroate synthases examined are determined by an R plasmid and are smaller and less heat stable than the normal sulfonamide-sensitive enzyme. One synthase resistant to any sulfonamide tested, and to sulfanilic and arsanilic acids, was still inhibited by several non-sulfonamide analogs of p-aminobenzoate. Citrobacter and Klebsiella pneumoniae strains also show similar mechanisms of sulfonamide resistance.

Aminobenzoates↗
PubMed1976

Distribution of sulfonamides and sulfonamide potentiators between red blood cells, proteins and aqueous phases of the blood of different species.

The uptake of sulfonamides and sulfonamide potentiators by plasma albumin, red blood cells and hemoglobin of man, ox, rabbit and mouse has been determined. From the figures obtained the distribution of these compounds between cells, macromolecules and aqueous phases of blood has been calculated. In most cases more than 50% of a total sulfonamide in blood is bound to plasma albumin. The time necessary for establishment of concentration equilibrium of the drugs investigated between erythrocytes and surrounding medium varies between a few seconds and several minutes, differences between the species being encountered. Hemoglobin binding of the drugs is much smaller than albumin binding. Nevertheless, drug concentration within the erythrocytes is generally higher than in the surrounding medium.

Animals↗
PubMed1977

Studies on the in vitro development of drug resistance of Proteeae to sulfonamides, trimethoprim and combinations of a sulfonamide and trimethoprim.

A strain of Proteus mirabilis repeatedly subcultured in the presence of a combination of sulfisoxazole and 0.4 microgram/ml of trimethoprim and a strain of P. vulgaris subcultured in the presence of sulfamethoxazole and trimethoprim combined in a 5:1 ratio gradually developed resistance to the combinations. However, the level of resistance developed by the organisms exposed to the combination was always appreciably lower than the level of resistance developed by the same strains exposed to either the sulfonamide or trimethoprim alone.

Drug Combinations↗
PubMed1977

Determination of ionization state by resonance Raman spectroscopy Sulfonamide binding to carbonic anhydrase.

Resonance Raman (RR) spectroscopy has been used to study the ionization state of the sulfonamide, 4'-sulfamylphenyl-2-azo-7-acetamido-1-hydroxynaphthalene-3,-6-disulfonate (Neoprontosil), bound to carbonic anhydrase. The correlation of effects of pH and deuteration on the spectra of model compounds with these effects on the Neoprotosil spectrum allows us to assign spectral bands in the 900-1000 and 100-1200 cm-1 regions to the SO2NH2 group. Large shifts in these bands occur upon ionization of the sulfonamide. On the basis of the positions of bands in the enzyme complex, it was determined that the sulfonamide was bound to the enzyme as SO2NH2, rather than as SO2NH-. Rates of association and dissociation and the dissociation equilibrium constant were measured as a function of pH. The rate behavior for Neoprontosil is consistent with that observed for other sulfonamides and kdissoc/kassoc = kdissoc, suggesting a one-step binding mechanism. Since RR spectroscopy establishes that the final ionization state of the sulfonamide in the enzyme complex is SO2NH2, protonated sulfonamide must bind directly to basic form of the enzyme. These conclusions suggest that sulfonamides form "outer-space" complexes with metal at the enzyme active site.

Animals↗
PubMed1976

Resonance Raman studies in some carboni anhydrase-aromatic sulfonamide complexes.

Resonance Raman spectra of 4-sulfonamido -4'-dimethylaminoazobenzene, 4-sulfonamido-4'-hydroxyazobenzene, and 4-sulfonamideo-4' aminoazobenzene bound to various isoenzymes of carbonic anhydrase were obtained by exciting into the sulfonamide absorption bands in the 400-500-nm region. In this way it was possible to obtain vibrational spectra of the sulfonamides in the active site unmasked by contributions from the vibrational modes of the protein and H2O solvent. Direct evidence was obtained for the presence of -SO2NH- in the complex, and it was possible to eliminate hydrophobic bonding and twisting in the Ph--N==N--Ph bonds as sources of the observed spectral changes. No detectable differences were found in the spectra of 4-sulfonamido-4'-dimethylaminoazobenzene bound to human carbonic anhydrase B and C or between these and the spectra of the sulfonamide bound to bovine carbonic anhydrase or Co(II) human carbonic anhydrase B. A new band appears in the spectra of the bound sulfonamides, and this is interpreted in terms of a change in geometry about the sulfonamido sulfur atom. A possible explanation for this change in geometry is that the bound sulfonamide group closely mimics the transition state of the reactants in the reversible hydration of CO2. Sulfonamide binding at pH 12.0 was not detected in the resonance Raman spectrum. Sulfonamide replacement of CN- in the binding site occurred over a period of minutes and could be monitored in the resonance Raman spectra.

Animals↗
PubMed2026

The Role of In Vivo, In Vitro and Pharmacogenomic Diagnostic Approaches to Sulfonamide Allergy.

Sulfonamide antibiotics are commonly reported as a medication allergy, presenting as both immediate IgE-mediated reactions and delayed hypersensitivity reactions ranging from benign cutaneous eruptions to severe cutaneous adverse reactions. Sulfonamide antibiotics have retained importance as treatment for multiple indications and are especially relevant in immunocompromised patients wherein use is indicated for prevention of opportunistic infections. Sulfonamide antibiotic allergy labels may lead to inappropriate avoidance of other "sulfur"-containing medications, because cross-reactivity is unlikely between antibiotic and nonantimicrobial sulfonamides. In this review, we discuss the typical presentation of sulfonamide antibiotic hypersensitivity reactions. We also review risk stratification tools and current in vivo procedures and experimental in vitro evaluation methods. Lastly, we will provide an update on emerging pharmacogenomics data associated with sulfonamide medication adverse reactions.

Humans↗
PubMed1978

Structures of silver sulfonamides.

The structures of silver sulfonamides were found to depend highly on the substituent at the amide nitrogen of the sulfonamide. Silver is coordinated to that nitrogen and the sulfonamide is in the amido form if no substituent is present or if the substituent is a phenyl, acetyl, or 2-pyrimidyl group. If the substituent is a 2-thiazolyl or 2-pyridinyl group, the sulfonamide is in the imido form and silver coordinates to the nitrogen of the substituent. Depending on the number of suitable donor atoms per sulfonamide, the silver compounds are charged or uncharged and the primary amino group may be involved in complexation.

Chemical Phenomena↗
PubMed2024

Sulfonamide-induced DNA hypomethylation disturbed sugar metabolism in rice (Oryza sativa L.).

DNA methylation is well-accepted as a bridge to unravel the complex interplay between genome and environmental exposures, and its alteration regulated the cellular metabolic responses towards pollutants. However, the mechanism underlying site-specific aberrant DNA methylation and metabolic disorders under pollutant stresses remained elusive. Herein, the multilevel omics interferences of sulfonamides (i.e., sulfadiazine and sulfamerazine), a group of antibiotics pervasive in farmland soils, towards rice in 14 days of 1 mg/L hydroponic exposure were systematically evaluated. Metabolome and transcriptome analyses showed that 57.1-71.4 % of mono- and disaccharides were accumulated, and the differentially expressed genes were involved in the promotion of sugar hydrolysis, as well as the detoxification of sulfonamides. Most differentially methylated regions (DMRs) were hypomethylated ones (accounting for 87-95 %), and 92 % of which were located in the CHH context (H = A, C, or T base). KEGG enrichment analysis revealed that CHH-DMRs in the promoter regions were enriched in sugar metabolism. To reveal the significant hypomethylation of CHH, multi-spectroscopic and thermodynamic approaches, combined with molecular simulation were conducted to investigate the molecular interaction between sulfonamides and DNA in different sequence contexts, and the result demonstrated that sulfonamides would insert into the minor grooves of DNA, and exhibited a stronger affinity with the CHH contexts of DNA compared to CG or CHG contexts. Computational modeling of DNA 3D structures further confirmed that the binding led to a pitch increase of 0.1 Å and a 3.8° decrease in the twist angle of DNA in the CHH context. This specific interaction and the downregulation of methyltransferase CMT2 (log2FC = -4.04) inhibited the DNA methylation. These results indicated that DNA methylation-based assessment was useful for metabolic toxicity prediction and health risk assessment.

DNA Methylation↗
PubMed1976

On the influence of concomitant food intake on sulfonamide bioavailability.

The influence of food intake on the bioavailability of a frequently used short-acting sulfonamide, sulfaisomidine (Elkosin), has been examined in eight healthy volunteers. The drug was administered as a single oral dose, both on an empty stomach and together with a standardized breakfast. Numerous venous blood samples were drawn for the first eight hours after ingestion of the drug, and the concentration of unmetabolized sulfonamide in serum was assessed by spectrophotometry. The observations indicate that concomitant food intake alters neither absorption rate, peak concentration, time to reach peak concentration, elimination rate, nor total amount of sulfonamide reaching the general circulation. Thus, the absorption of orally administered sulfaisodimidine is not at all affected by concomitant intake of food. This finding contrasts with previous observations on some other sulfonamides, and it may signify a therapeutic advantage of sulfaisodimidine. In addition, the amount absorbed showed only a little interindividual variation. This suggests that the use of standardized size and interval of sulfaisodimidine dosage can be recommended. The present findings emphasize that conclusions about the absorption of a certain drug should not be derived from studies with other, albeit chemically related, compounds.

Adolescent↗