Biological activity evaluation and molecular docking study of chromone derivatives as cyclooxygenase-2 inhibitors
| Autor: | Narumol Phosrithong, Chirattikan Maicheen, Jiraporn Ungwitayatorn |
|---|---|
| Rok vydání: | 2017 |
| Předmět: |
biology
010405 organic chemistry Stereochemistry Organic Chemistry Binding energy Biological activity 01 natural sciences 0104 chemical sciences 010404 medicinal & biomolecular chemistry chemistry.chemical_compound chemistry Docking (molecular) Chromone Mole Celecoxib medicine biology.protein Cyclooxygenase General Pharmacology Toxicology and Pharmaceutics Selectivity medicine.drug |
| Zdroj: | Medicinal Chemistry Research. 26:662-671 |
| ISSN: | 1554-8120 1054-2523 |
| DOI: | 10.1007/s00044-017-1786-0 |
| Popis: | A series of chromone derivatives have been evaluated as potential cyclooxygenase-2 (COX-2) inhibitors. The four most potent compounds, 48, 41, 39, and 35 displayed IC50 values of 3.30, 6.86, 7.36 and 7.46 µM, respectively. Compounds 35 and 38 showed higher selectivity for COX-2 (selectivity index, SI = 7.48 and 5.46, respectively) than celecoxib (SI = 4.17 in the same test) whereas compound 39 showed comparable selectivity (SI = 4.19) to celecoxib. The molecular volumes of compounds 35 (312.84 A3) and 38 (314.18 A3) were similar to celecoxib (299.28 A3) but larger than ibuprofen (211.83 A3). Docking results were in good agreement with the experimental biological data in terms of evaluation of binding energy and binding mode. Compounds 35, 38, and 39 had higher binding affinity against COX-2 (binding energy between −9.77 and −11.42 kcal/mole) than COX-1 (binding energy between −6.28 and −7.88 kcal/mole). These three chromone compounds also displayed active conformation in the same orientation as that of celecoxib. Thus, compounds in this series has the potential to be a new class of selective COX-2 inhibitor. |
| Databáze: | OpenAIRE |
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