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Active compound from the leaves of vitex negundo L. shows anti-inflammatory activity with evidence of inhibition for secretory phospholipase A2 through molecular docking

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Author(s): Thangaraj Vinuchakkaravarthy * | Kaliya Perumal Kumaravel | Samuthirapandian Ravichandran | Devadasan Velmurugan *

Journal: Bioinformation
ISSN 0973-2063

Volume: 7;
Issue: 4;
Start page: 199;
Date: 2011;
Original page

Keywords: Vitex negundo | Tris(2 | 4-di-tert-butylphenyl) phosphate | Anti-inflammatory | Carrageenan | Antidote | PLA2 | Induced Fit Docking

ABSTRACT
Novel compounds with significant medicinal properties have gained much interest in therapeutic approaches for treating various inflammatory disorders like arthritis, odema and snake bites and the post-envenom (impregnating with venom) consequences. Inflammation is caused by the increased concentration of secretory Phospholipases A2 (sPLA2s) at the site of envenom. A novel compound Tris(2,4-di-tert-butylphenyl) phosphate (TDTBPP) was isolated from the leaves of Vitex negundo and the crystal structure was reported recently. The acute anti-inflammatory activity of TDTBPP was assessed by Carrageenan-induced rat paw odema method. TDTBPP reduced the raw paw odema volume significantly at the tested doses of 50 mg/kg and 70 mg/kg body weight. Molecular docking studies were carried out with the X-ray crystal structures of Daboia russelli pulchella’s (Vipera russelli, Indian Russell’s viper) venom sPLA2 and Human non-pancreatic secretory PLA2 (Hnps PLA2) as targets to illustrate the anti-inflammatory and antidote activities of TDTBPP. Docking results showed hydrogen bond (H-bond) interaction with Lys69 residue lying in the anti-coagulant loop of D. russellis venom PLA2, which is essential in the catalytic activity of the enzyme and hydrophobic interactions with the residues at the binding site (His48, Asp49). Docking of TDTBPP with Hnps PLA2 structure showed coordination with calcium ion directly as well as through the catalytically important water molecule (HOH1260) located at the binding site.
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