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Title: Modeling studies on phospholipase A₂-inhibitor complexes
Authors: Nirmal, Nithya
Praba, G Om
Velmurugan, D
Keywords: Phospholipase A₂
Aplysulphurin 1
Chlorogenic acid
Gracilin A
Issue Date: Aug-2008
Publisher: CSIR
Abstract: Phospholipase A₂ (PLA₂) is a ubiquitous enzyme that specifically catalyzes hydrolysis of membrane phospholipids to produce lysophospholipids and free fatty acid, namely arachidonic acid, which provides substrate for eicosanoids biosynthesis. Thus, the compounds inhibiting PLA₂ have been implicated as potential therapeutic agents in treatment of inflammation related diseases. Plant and marine organisms serve as sources of compounds that act as potential therapeutic agents for treatment of various diseases. The present study reveals the relationship between the structure and function of the medicinally important herbal compounds (acalyphin, chlorogenic acid, stigmasterol, curcumin and tectoridin) and marine compounds (gracilin A and aplysulphurin A). To understand the binding mechanisms of these compounds, molecular modeling studies has been performed with Russell’s viper and bovine pancreatic PLA₂ as target molecules using molecular operating environment (MOE) software. These compounds show favorable interactions with the amino acid residues at the active site of Russell’s viper and bovine pancreatic PLA₂, thereby substantiating their proven efficacy as anti-inflammatory compounds and antidotes.
Description: 256-262
ISSN: 0301-1208
Appears in Collections: IJBB Vol.45(4) [August 2008]

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