Abstract
The fungal transformation of cedryl acetate (1) was investigated for the first time by using Cunninghamella elegans. The metabolites obtained include, 10 beta-hydroxycedryl acetate (3), 2 alpha, 10 beta-dihydroxycedryl acetate (4), 2 alpha-hydroxy-10-oxocedryl acetate (5), 3 alpha,10 beta-dihydroxycedryl acetate (6), 3 alpha,10 alpha-dihydroxycedryl acetate (7), 10 beta,14 alpha-dihydroxy cedryl acetate (8), 3 beta,10 beta-cedr-8(15)-ene-3,10-diol (9), and 3 alpha,8 beta,10 beta -dihydroxycedrol (10). Compounds 1, 2, and 4 showed alpha-glucosidase inhibitory activity, whereby 1 was more potent than the standard inhibitor, acarbose, against yeast alpha-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 alpha-glucosidase and human intestinal maltase glucoamylase. All active ligands were found to have greater binding affinity with the yeast alpha-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. (C) 2013 Elsevier Masson SAS. All rights reserved.