A novel series of novobiocin analogues has been synthesised by removing the lipophilic aryl chain in novobiocin and introducing an amino substituent. The structural modifications have been dictated by the control of lipophilicity and the dissociation constant of the resulting compounds. Antibacterial activity of the new coumarin derivatives could be correlated with the amount of uncharged form in physiological conditions.
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http://dx.doi.org/10.1016/s0960-894x(01)00257-8 | DOI Listing |
Front Chem
November 2024
Medicinal Chemistry Department, Faculty of Pharmacy, Minia University, Minia, Egypt.
RSC Adv
October 2024
Medicinal Chemistry Research Laboratory, School of Pharmaceutical Sciences, Siksha 'O' Anusandhan Deemed to be University Bhubaneswar 751003 Odisha India
The briskened urge to develop potential antibacterial candidates against multidrug-resistant pathogens has motivated the present research study. Herein, newly synthesized coumarin derivatives with azomethine and amino-methylated as the functional groups have been focused on their antibacterial efficacy. The study proposed two distinct series: 3-acetyl substituted coumarin derivatives, followed by the Schiff base approach (5a-5i), and formaldehyde-secondary cyclic amine-based derivatives (7a-7g), using the Mannich base approach, further the compounds have been confirmed through various spectral studies.
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September 2024
University of Ljubljana, Faculty of Pharmacy Aškerčeva cesta 7 1000 Ljubljana Slovenia
This study presents the discovery of a new series of -phenylpyrrolamide inhibitors of bacterial DNA gyrase with improved antibacterial activity. The most potent inhibitors had low nanomolar IC values against DNA gyrase (IC; 2-20 nM) and topoisomerase IV (22i, IC = 143 nM). Importantly, none of the compounds showed activity against human DNA topoisomerase IIα, indicating selectivity for bacterial targets.
View Article and Find Full Text PDFChemMedChem
December 2024
Department of Chemistry and Biochemistry, Warren Family Research Center for Drug Discovery and Development, University of Notre Dame, Notre Dame, Indiana, 46556, USA.
Heat Shock Protein 90 (Hsp90) is responsible for the proper folding and maturation of ~400 client protein substrates, many of which are directly associated with the ten hallmarks of cancer. Hsp90 is a great target for cancer therapy including melanoma, since Hsp90 inhibition can disrupt multiple oncogenic pathways simultaneously. In this study, we report the synthesis and anti-proliferative activity manifested by a series of Hsp90 C-terminal inhibitors against mutant BRAF and wild-type BRAF melanoma cells.
View Article and Find Full Text PDFEur J Med Chem
October 2024
Department of Medicine, Surgery and Pharmacy, University of Sassari, 07100, Sassari, Italy. Electronic address:
Multi-drug resistance (MDR) is a serious challenge in contemporary clinical practice and is mostly responsible for the failure of cancer medication therapies. Several experimental evidence links MDR to the overexpression of the drug efflux transporter P-gp, therefore, the discovery of novel P-glycoprotein inhibitors is required to treat or prevent MDR and to improve the absorption of chemotherapy drugs via the gastrointestinal system. In this work, we explored a series of novel pyridoquinoxaline-based derivatives designed from parental compounds, previously proved active in enhancing anticancer drugs in MDR nasopharyngeal carcinoma (KB).
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