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Resorcinol-based Bolaamphiphilic Quaternary Ammonium Compounds.
ChemMedChem
January 2025
Villanova University, Chemistry, 800 E Lancaster Ave, 19085, Villanova, UNITED STATES OF AMERICA.
Quaternary ammonium compounds (QACs) play crucial disinfectant roles in healthcare, industry, and domestic settings. Most commercially utilized QACs like benzalkonium chloride have a common architectural theme, leading to a rise in bacterial resistance and urgent need for novel structural classes. Some potent QACs such as chlorhexidine (CHX) and octenidine (OCT) feature a bolaamphiphilic architecture, comprised of two cationic centers at the molecular periphery and a non-polar region connecting them; these compounds show promise to elude bacterial resistance mechanisms.
View Article and Find Full Text PDFExperimental and DFT studies on the green synthesis of 2-amino-4H-chromenes using a recyclable GOQDs-NS-doped catalyst.
Sci Rep
December 2024
Department of Chemistry, Faculty of Science, K. N. Toosi University of Technology, P.O. Box 15875-4416, Tehran, Iran.
This research presents an innovative approach for synthesizing 2-amino-4H-chromene derivatives, utilizing 30 mg of NS-doped graphene oxide quantum dots (GOQDs) as a catalyst in a one-pot, three-component reaction conducted in ethanol. The NS-doped GOQDs were synthesized using a cost-effective bottom-up method through the condensation of citric acid (CA) with thiourea and the reaction was carried out at 185 C, resulting in the elimination of water. The catalytic performance of the synthesized NS-doped GOQDs resulted in high product yields, achieving up to 98% for the 2-amino-4H-chromene derivatives from aromatic aldehydes, malononitrile, resorcinol, -naphthol, and dimedone.
View Article and Find Full Text PDFSupramolecular Host:Guest Arrays Site-Selectively Recognize Peptide Phosphorylation and Kinase Activity.
J Am Chem Soc
January 2025
Department of Chemistry, University of California─Riverside, Riverside, California 92521, United States.
A synergistic combination of cationic styrylpyridinium dyes and water-soluble deep cavitand hosts can recognize phosphorylated peptides with both site- and state-selectivity. Two mechanisms of interaction are dominant: either the cationic dye interacts with Trp residues in the peptide or the host:dye pair forms a heteroternary complex with the peptide, driven by both strong dye-peptide and cavitand-peptide binding ( values up to 4 μM). The presence of multiple recognition mechanisms results in varying fluorescence responses dependent on the phosphorylation state and position, eliminating the need for covalent modification of the peptide target.
View Article and Find Full Text PDFVitamin E Mitigates Apoptosis in Ovarian Granulosa Cells by Inhibiting Zearalenone-Induced Activation of the PERK/eIF-2α/ATF4/Chop Signaling Pathway.
J Agric Food Chem
December 2024
State Key Laboratory of Animal Nutrition and Feeding, College of Animal Science and Technology, China Agricultural University, Beijing 100193, China.
A study aimed to investigate the signaling pathway of zearalenone (ZEA) leading to the apoptosis of ovarian granulosa cells (GCs) and explore the potential of vitamin E (VE) in alleviating ZEA-induced apoptosis of GCs. We constructed an apoptosis model for GCs based on exposure to the environmental toxin ZEA. Transcriptome analysis revealed that ZEA induced endoplasmic reticulum stress by activating the ATF4-Chop pathway.
View Article and Find Full Text PDFPreparation and characterization of aptamer-based sorbent for the selective extraction of zearalenone and its derivatives from human urine.
Anal Bioanal Chem
January 2025
Department of Analytical, Bioanalytical Sciences, and Miniaturization (LSABM), UMR 8231 Chemistry, Biology and Innovation (CBI), ESPCI Paris, PSL University, Paris, France.
The aim of this work is the development of a biomimetic strategy involving a molecular recognition mechanism using aptamers immobilized on a solid support for the analysis of the mycotoxin zearalenone (ZEA) and two of its derivatives in human urine: alpha-zearelenol (α-ZEL) and beta-zearelenol (β-ZEL). Three oligonucleotide sequences reported in the literature as being specific to ZEA were thus covalently grafted onto activated sepharose, and a thorough study of the percolation and washing conditions was performed to promote the selective retention of the three targeted compounds. With the optimized extraction procedure, a strong and selective retention was obtained for ZEA and to a lesser extent α-ZEL and β-ZEL, with extraction recoveries of 88±9%, 77±15%, and 45±12% respectively, in standard solutions.
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