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Authors
Affiliations
1 KMCH College of Pharmacy, Coimbatore, Tamilnadu, IN
Source
Asian Journal of Research in Chemistry, Vol 4, No 2 (2011), Pagination: 308-312
Abstract
Evaluating acetyl-CoA carboxylase (ACC) as the target enzyme for the treatment of hyperlipidemia can lead to the detection of new inhibitors that can potentially be optimized as lipid lowering agents and could also form a novel method of screening a large number of plant constituents. Inhibition of ACC2 may prevent lipid-induced insulin resistance and type 2 diabetes, making the enzyme an attractive pharmaceutical target. The crystal structures of the biotin carboxylase (BC) domain of human ACC2 (PDB ID: 3GLK) and carboxyl transferase (CT) domain of human ACC2 (PDB ID: 3FF6) have been selected for molecular targets for Insilico studies of some potent phytochemicals like hydroxycitric acid, terrestrosin, forskolin and EGC. The interactions between the compounds and crystal structures of the enzymes have been performed using Accelrys Discovery Studio 2.1 Ligandfit protocol. Findings from the docking procedure indicate different binding modes of the compounds , further more the studies reveal that EGC was found to be a ideal inhibitor for both ACC2 Domains, thus can be suggested as a better inhibitor for lipid lowering .
Keywords
Phytochemicals, Inhibitory Profiles, ACC Domains.
