title: Fungal transformation of cedryl acetate and α-glucosidase inhibition assay, quantum mechanical calculations and molecular docking studies of its metabolites.
abstract: 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.
authors: H.E.J. Research Institute of Chemistry, International Center for Chemical and Biological Sciences, University of Karachi, Karachi, Pakistan. sadiasultan301@yahoo.com
authors: Sadia
authors: S
authors: Sultan
authors: M Iqbal
authors: MI
authors: Choudhary
authors: Shamsun Nahar
authors: SN
authors: Khan
authors: Urooj
authors: U
authors: Fatima
authors: Muhammad
authors: M
authors: Atif
authors: Rahat Azhar
authors: RA
authors: Ali
authors: Atta-Ur-
authors: AU
authors: Rahman
authors: M Qaiser
authors: MQ
authors: Fatmi
mesh_terms: D000085:Acetates / Q000737:chemistry / Q000378:metabolism* / Q000494:pharmacology*; D020093:Cunninghamella / Q000737:chemistry* / Q000378:metabolism; D004305:Dose-Response Relationship, Drug; D004791:Enzyme Inhibitors / Q000737:chemistry / Q000378:metabolism* / Q000494:pharmacology*; D065089:Glycoside Hydrolase Inhibitors; D006801:Humans; D007413:Intestinal Mucosa / Q000378:metabolism; D007422:Intestines / Q000201:enzymology; D008958:Models, Molecular; D008968:Molecular Conformation; D011789:Quantum Theory; D012441:Saccharomyces cerevisiae / Q000201:enzymology / Q000378:metabolism; D012717:Sesquiterpenes / Q000737:chemistry / Q000378:metabolism* / Q000494:pharmacology*; D013237:Stereoisomerism; D013329:Structure-Activity Relationship; D000520:alpha-Glucosidases / Q000378:metabolism
chemical_list: D000085:Acetates; D004791:Enzyme Inhibitors; D065089:Glycoside Hydrolase Inhibitors; D012717:Sesquiterpenes; D000520:alpha-Glucosidases