salicylates and diphenyl

A novel biphenyl-derived salicylhydrazone Schiff base (BSS) fluorescent probes for highly sensitive and selective identification of Cu

Topics: Biphenyl Compounds; Copper; Fluorescent Dyes; HeLa Cells; Humans; Hydrazones; Limit of Detection; Salicylates; Schiff Bases; Spectrometry, Fluorescence

Two new series of biphenyls, analogs of aglycone of natural product fortuneanoside E, were prepared using Suzuki-Miyaura cross-coupling and selective magnesium iodide demethylation/debenzylation, and their mushroom tyrosinase inhibitory activity was evaluated. Most of the 4-hydroxy-3,5-dimethoxyphenyl biphenyl compounds (series II, 20-36) were in general more active than 3,4,5-trimethoxyphenyl biphenyl compounds (series I, 1-19). Structure-activity relationships study showed that monosaccharide substituents, such as glucose, were not necessary and the presence of 4-hydroxy-3,5-dimethoxyphenyl moiety was crucial for inhibitory activity. Among the compounds synthesised, compound 21 (IC50=0.02 mM) was found to be the most active one, which exhibited an activity that was 7 times higher than that of fortuneanoside E (IC50=0.14 mM) and 10 times higher than that of arbutin (IC50=0.21 mM), known as potent tyrosinase inhibitors. The inhibition kinetics analyzed by Lineweaver-Burk plots revealed that compound 21 was a competitive inhibitor (Ki=0.015 mM).

Topics: Agaricales; Biphenyl Compounds; Drug Design; Enzyme Inhibitors; Kinetics; Monophenol Monooxygenase; Salicylates; Structure-Activity Relationship

Pseudomonas pseudoalcaligenes KF707 grows on biphenyl and salicylate as sole sources of carbon. The biphenyl-catabolic (bph) genes are organized as bphR1A1A2(orf3)A3A4BCX0X1X2X3D, encoding the enzymes for conversion of biphenyl to acetyl coenzyme A. In this study, the salicylate-catabolic (sal) gene cluster encoding the enzymes for conversion of salicylate to acetyl coenzyme A were identified 6.6-kb downstream of the bph gene cluster along with a second regulatory gene, bphR2. Both the bph and sal genes were cross-regulated positively and/or negatively by the two regulatory proteins, BphR1 and BphR2, in the presence or absence of the effectors. The BphR2 binding sequence exhibits homology with the NahR binding sequences in various naphthalene-degrading bacteria. Based on previous studies and the present study we propose a new regulatory model for biphenyl and salicylate catabolism in strain KF707.

Topics: Acetyl Coenzyme A; Bacterial Proteins; Biphenyl Compounds; Culture Media; Gene Expression Regulation, Bacterial; Genes, Bacterial; Molecular Sequence Data; Multigene Family; Protein Binding; Pseudomonas pseudoalcaligenes; Salicylates; Transcription Initiation Site

The aromatic compounds phenyl benzoate (PB), phenyl salicylate (PS), and biphenyl (BP), which have previously been found to leach from poly(methyl methacrylate) denture base materials, were tested for cytotoxicity and biologic effects by L929 cells in culture. The octanol-water partition coefficient (log P(ow), a descriptor for the lipophilicity, was determined for the compounds. Cytotoxicity was evaluated by total cell growth and the plating efficiency test, and biologic effects by the total fatty acid composition of L929 cells. The commonly used tests, total cell growth and plating efficiency, did not show any significant changes of the cells due to the compounds. On the other hand, BP and PS, in particular, induced changes in the total fatty acid composition of L929 cells. The problem of bioavailability of aromatic compounds in cell culture assays and the relation to lipophilicity was addressed.

Topics: Animals; Biocompatible Materials; Biological Availability; Biphenyl Compounds; Cell Division; Cells, Cultured; Denture Bases; Fatty Acids; Fibroblasts; Lipids; Materials Testing; Methylmethacrylates; Mice; Salicylates