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At least 145 records · Page 8Linked to original sources
PubMed2005

The proton-transfer compounds of strychnine with achiral salicylic acids: strychninium 3,5-dinitrosalicylate and the strychninium 5-nitrosalicylate bis(5-nitrosalicylic acid) adduct.

In the crystal structures of the proton-transfer compounds of strychnine with 3,5-dinitrosalicylic acid, namely strychninium 3,5-dinitrosalicylate, C21H23N2O2+.C7H3N2O7-, (I), and 5-nitrosalicylic acid, namely strychninium-5-nitrosalicylate-5-nitrosalicylic acid (1/1/2), C21H23N2O2+.C7H4NO5-.2C7H5NO5, (II), protonation of one of the N atoms of the strychnine molecule occurs and this group is subsequently involved in intermolecular hydrogen-bonding interactions. In (I), this is four-centred, the primary being with an adjacent strychninium carbonyl O-atom acceptor in a side-to-side interaction giving linear chains. Other interactions are with the phenolate and nitro O-atom acceptors of the anionic species, resulting in a one-dimensional polymer structure. In (II), the N+-H interaction is three-centred, the hydrogen bonding involving carboxyl O-atom acceptors of the anion and both acid adduct species, giving unique discrete hetero-tetramer units. The structure of (II) also features pi-bonding interactions between the two acid adduct molecules.

Journal Article↗
PubMed2004

Synthesis, X-ray crystal structure, anti-fungal and anti-cancer activity of [Ag2(NH3)2(salH)2] (salH2=salicylic acid).

[Ag(2)(NH(3))(2)(salH)(2)] (salH(2)=salicylic acid) was synthesised from salicylic acid and Ag(2)O in concentrated aqueous NH(3) and the dimeric Ag(I) complex was characterised using X-ray crystallography. The complex is centrosymmetric with each metal coordinated to a salicylate carboxylate oxygen and to an ammonia nitrogen atom in an almost linear fashion. The two [Ag(NH(3))(salH)] units in the complex are linked by an Ag-Ag bond. Whilst metal-free salH(2) did not prevent the growth of the fungal pathogen Candida albicans [Ag(2)(NH(3))(2)(salH)(2)], [Ag(2)(salH)(2)] and some simple Ag(I) salts greatly inhibited cell reproduction. SalH(2), [Ag(2)(NH(3))(2)(salH)(2)] [Ag(2)(salH)(2)] and AgClO(4) produced a dose-dependent cytotoxic response against the three human derived cancer cell lines, Cal-27, Hep-G2 and A-498, with the Ag(I)-containing reagents being the most effective.

Animals↗
PubMedDate not supplied

Kidney and liver contributions to salicylate metabolism in rats.

The pharmacokinetics and metabolism of radiolabelled salicylate were studied in rats and compared with that of the isolated perfused rat liver and the perfused rat kidney. Both parent compound and salicylate metabolites (mainly conjugates with glycine and glucuronic acid) were eliminated mostly into urine. The comparison of a relative proportion of metabolites eliminated in whole rats with that of the isolated perfused rat liver and the perfused rat kidney showed that both kidney and liver contributed to the salicylate metabolism. The glycine conjugate of salicylate was formed predominantly in the kidney whereas both kidney and liver participated in the formation of glucuronic acid derivatives.

Animals↗
PubMed1990

The absorption of bismuth and salicylate from oral doses of Pepto-Bismol (bismuth salicylate).

Plasma bismuth and plasma salicylate concentrations were measured before and after three 30-ml oral doses of bismuth salicylate (Pepto-Bismol liquid) in 10 fasting healthy subjects. From 0 to 120 min following the first dose of bismuth salicylate, the plasma bismuth concentration was less than 1 ng/ml. The peak median plasma bismuth concentration was at +240 min (1.7 ng/ml; range 0.8-5.3 ng/ml). Salicylate appeared in the plasma of all subjects at +30 min, and it reached a peak at +120 min (median 61 mg/L; range 46-104 mg/L). The study demonstrates that, despite rapid and substantial absorption of salicylate, there is negligible absorption of bismuth into the bloodstream from standard oral doses of bismuth salicylate.

Adult↗
PubMed1994

Characterization of esterase and alcohol dehydrogenase activity in skin. Metabolism of retinyl palmitate to retinol (vitamin A) during percutaneous absorption.

Retinyl palmitate, a widely used ingredient in cosmetic products, is promoted for its beneficial effects on the appearance of skin. Previous studies suggest that enzymes are available in skin to metabolize this ingredient during skin absorption. Esterase activity hydrolyzes retinyl palmitate to retinol (vitamin A), which is oxidized in many tissues to retinoic acid primarily by alcohol dehydrogenase. The activities of esterase and alcohol dehydrogenase were characterized in hairless guinea pig skin by using flow-through diffusion cells and radiolabeled model compounds (methyl salicylate and benzyl alcohol) previously shown to be metabolized by these enzymes. Methyl salicylate was hydrolyzed by esterase to a greater extent in viable skin than in nonviable skin. Glycine conjugation of salicylic acid and benzoic acid occurred only in viable skin. The metabolism of methyl salicylate and benzyl alcohol occurred to a greater extent in male guinea pig skin than in female guinea pig skin. The percutaneous absorption of both radiolabeled compounds was similar in viable and nonviable skin. About 30 and 18% of topically applied retinyl palmitate were absorbed from an acetone vehicle by hairless guinea pig skin and human skin, respectively. Less than 1% of the applied dose of this lipophilic compound diffused from skin into the receptor fluid. Retinol was the only detectable metabolite of retinyl palmitate in both hairless guinea pig and human skin. In human skin, 44% of the absorbed retinyl palmitate was hydrolyzed to retinol. The use of retinyl palmitate in cosmetic formulations may result in significant delivery of retinol into the skin.

Alcohol Dehydrogenase↗
PubMedDate not supplied

Charge-shift strategy for isolation of hemoglobin-carcinogen adducts formed at the beta 93 cysteine sulfhydryl groups.

Qualitative and quantitative analysis of human hemoglobin-carcinogen adducts has potential as a diagnostic tool for estimation of biologically effective levels of carcinogen exposure and for attaining a better understanding of individual susceptibility to chemical carcinogenesis. The purpose of this study was to devise a strategy for preanalytical enrichment of the class of covalent human hemoglobin-carcinogen adducts formed by reaction at the hemoglobin beta 93 cysteine sulfhydryl groups. The results define a charge-shift strategy in which a mixture composed of natural hemoglobin (Hb-SH) and low levels of hemoglobin-S-xenobiotic adducts (Hb-SX) is treated with an anionic sulfhydryl reagent (R-), followed by anion-exchange liquid chromatographic separation of Hb-SR- from the unreactive Hb-SX adducts. Using 4-(iodoacetamido)-salicylic acid as the charge-shift reagent, we applied the strategy to the isolation of chromatographically similar adducts with either 4-nitrosobiphenyl or [3H]-N-ethylmaleimide. The strategy was effective for adduct concentrations less than or equal to 10 mumol/mol of hemoglobin. Application of the strategy provides an adduct-enriched fraction useful for subsequent analysis using either currently available techniques or alternate chemical or biochemical techniques that may be designed to take advantage of the enrichment procedure.

Aminobiphenyl Compounds↗
PubMed2006

Synthesis and biological evaluation of benzamides and benzamidines as selective inhibitors of VEGFR tyrosine kinases.

A series of benzamidines and benzamides was synthesized as selective inhibitors of vascular endothelial growth factor receptor (VEGFR) tyrosine kinases, and tested for inhibitory activity toward autophosphorylation by the enzyme assay. Selective inhibition of VEGFR-2 tyrosine kinase was observed in the salicylic amide 4e and the anthranilic amidine 5a, and their percent inhibitions of VEGFR-2 tyrosine kinase were 44-60% at a 10 microM concentration of compounds. The salicylic amide 4a showed inhibition of both VEGFR-1 and VEGFR-2 tyrosine kinases at a 10 microM concentration.

Animals↗
PubMed2002

Spectroscopic evidence in support of horseradish peroxidase compound II-catalyzed oxidation of salicylic acid but not of phenylethylamine.

Salicylic acid and phenylethylamine are putative substrates for naturally occurring reactions for generation of reactive oxygen species, which are catalyzed by plant peroxidases. Here, we used commercially available highly purified horseradish peroxidase-C (HRP-C) as a model enzyme for spectroscopic analysis, and obtained data suggesting that the Compound II form of HRP-C does not utilize phenylethylamine as substrate. In contrast, addition of salicylic acid to Compound II resulted in rapid conversion of Compound II to the native form.

Catalysis↗