Fungal transformation of cedryl acetate and α-glucosidase inhibition assay, quantum mechanical calculations and molecular docking studies of its metabolites

• Published in: European Journal of Medicinal Chemistry
• Main Author: Sultan S.; Choudhary M.I.; Khan S.N.; Fatima U.; Atif M.; Ali R.A.; Rahman A.-U.-.; Fatmi M.Q.
• Format: Article
• Language: English
• Published: 2013
• Online Access: https://www.scopus.com/inward/record.uri?eid=2-s2.0-84875993094&doi=10.1016%2fj.ejmech.2013.01.036&partnerID=40&md5=479d80fd85ac73ec2c1b895441e35312

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. © 2012 Elsevier Masson SAS. All rights reserved.