Structure–activity relationship of wedelolactone analogues: Structural requirements for inhibition of Na+,K+-ATPase and binding to the central benzodiazepine receptor
| Autor: | Paulo R. R. Costa, Elisa Suzana Carneiro Pôças, Chaquip D. Netto, Fernanda Leitão, Camilla D. Buarque, Paulo Henrique Cotrim Pimenta, Alcides J. M. da Silva, Flávia V. Brito, Daniele V.S. Lopes, François Noël |
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| Rok vydání: | 2006 |
| Předmět: |
Stereochemistry
Clinical Biochemistry Catechols Pharmaceutical Science Kidney Ligands Biochemistry Chemical synthesis Structure-Activity Relationship chemistry.chemical_compound Coumarins Coumestan Drug Discovery Humans Structure–activity relationship Enzyme Inhibitors Na+/K+-ATPase Receptor Molecular Biology biology Chemistry Ligand Organic Chemistry Receptors GABA-A Wedelolactone Enzyme inhibitor Drug Design biology.protein Molecular Medicine Sodium-Potassium-Exchanging ATPase Protein Binding |
| Zdroj: | Bioorganic & Medicinal Chemistry. 14:7962-7966 |
| ISSN: | 0968-0896 |
| DOI: | 10.1016/j.bmc.2006.07.053 |
| Popis: | Coumestans 2a–i, bearing different patterns of substitution in A- and D-rings, were synthesized and evaluated as inhibitors of kidney Na+,K+-ATPase and ligands for the central benzodiazepine (BZP) receptor. The presence of a hydroxyl group in position 2 favours the effect on Na+,K+-ATPase but decreases the affinity for the BZP receptor, allowing the design of more selective molecules than the natural wedelolactone. On the other hand, the presence of a catechol in ring D is important for the effect on both molecular targets. |
| Databáze: | OpenAIRE |
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