Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1394346 | European Journal of Medicinal Chemistry | 2013 | 7 Pages |
The fungal transformation of cedryl acetate (1) was investigated for the first time by using Cunninghamella elegans. The metabolites obtained include, 10β-hydroxycedryl acetate (3), 2α, 10β-dihydroxycedryl acetate (4), 2α-hydroxy-10-oxocedryl acetate (5), 3α,10β-dihydroxycedryl acetate (6), 3α,10α-dihydroxycedryl acetate (7), 10β,14α-dihydroxy cedryl acetate (8), 3β,10β-cedr-8(15)-ene-3,10-diol (9), and 3α,8β,10β -dihydroxycedrol (10). Compounds 1, 2, and 4 showed α-glucosidase inhibitory activity, whereby 1 was more potent than the standard inhibitor, acarbose, against yeast α-glucosidase. Detailed docking studies were performed on all experimentally active compounds to study the molecular interaction and binding mode in the active site of the modeled yeast α-glucosidase and human intestinal maltase glucoamylase. All active ligands were found to have greater binding affinity with the yeast α-glucosidase as compared to that of human homolog, the intestinal maltase, by an average value of approximately −1.4 kcal/mol, however, no significant difference was observed in the case of pancreatic amylase.
Graphical abstractThis paper describes fungal transformation of cedryl acetate (1) and α-glucosidase inhibitory activity of the transformed products. Detailed docking studies of all metabolites were performed using Autodock.Figure optionsDownload full-size imageDownload as PowerPoint slideHighlights► Reporting seven new bio-transformed products by Cunninghamella elegans. ► Introducing new class of organic compounds as potent yeast a-glucosidase inhibitors. ► Rationalizing inhibitors’ activity at molecular level. ► Inhibitors optimization at QM level to eliminate possible error in docking study.