In silico docking analysis of piperine with cyclooxygenases


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Prashantha Karunakar, . and Krishnamurthy, V. and Girija, C.R. and Krishna, V. and Vasundhara, D.E. and Noor Shahina Begum, . and Akheel Ahmed Syed, . (2012) In silico docking analysis of piperine with cyclooxygenases. Journal of Biochemical Technology, 3 (5). pp. 122-127. ISSN 0974-2328

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The structure of 1-[5-(1,3-benzodioxol- 5-yl)-1-oxo-2,4- pentadienyl]piperidine (Piperine), C17H19O3N, a versatile bioactive molecule has been redetermined at 100(2) K by X-ray crystallography to explore their potential utilization in inhibition of prostaglandin release. The crystal structure is stabilized by weak nonclassical intermolecular C-H…O hydrogen bonds and also intermolecular C-H…π interactions. The crystallographic coordinates of the compound were extrapolated to docking studies to elucidate the action of piperine against the enzymes, cyclooxygenases (COX-1 and COX-2) involved in biosynthesis of prostaglandin release. Using AutoDock suite, piperine was docked at the binding site of COX-1 and COX-2 enzyme and a strong affinity (-9.06kcal/mol, Ki =227.73nM and -8.77kcal/mol, Ki = 375.62nM, respectively) was formed by Hydrogen bonds and hydrophobic interactions. These results suggest that piperine can be a promising lead for the development of COX family inhibitors.

Item Type: Article
Uncontrolled Keywords: Prostaglandin, Molecular Docking, X-ray crystallography, COX-1, COX-2.
Subjects: Faculty of Science > Pure Sciences > Chemistry
Divisions: Jnana Bharathi / Central College Campus > Department of Chemistry
Depositing User: Ms. Sathyavathi N
Date Deposited: 05 Nov 2016 07:12
Last Modified: 05 Nov 2016 07:12

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