Investigating the molecular docking of aurantamide in the medicinal plant Moringa Olifera on the inhibition of prostaglandins
Subject Areas : Journal of Quality and Durability of Agricultural Products and Food Stuffs
Hamideh
Khageh
1
(M.Sc, Department of Biotechnology, University of Zabol, zabol, Iran)
zahra
Jomee Ghasemabadi
2
(Ph. D. student, Department of Biotechnology, School of Agriculture, University of Zabol, Zabol, Iran)
Keywords: moringa, Molecular docking, Bioinformatics, Prostaglandin, aurantamide,
Abstract :
Pain is defense mechanism and occurs when tissue is damaged. Pain receptors in the skin and tissues are free nerve endings. The pain in the tissues is due to the production of a substance called proaglandin, which is reduced by anti-inflammatory drugs. Eliphara plant is valuable in the food and herbal medicine industry and has a rare medicinal compound called aurantamide. Due to its anti-rheumatic anti-inflammatory effects in the treatment of diseases like arthritis, rheumatism and psoriasis, and by preventing the production of prostaglandins and increasing the production of glutathione, reducing the activity of aspartate aminotransferase, alanine aminotransferase enzyme and reducing the production of TNF-a factor, it reduces side effects. The aim of this study is to investigate the effect of Orantamide drug combination on prostaglandins with molecular docking. PubChem and PDB databases were used to investigate how the drug binds to the active site of the molecule, draw the chemical structure of the drug, energy optimization, binding studies and final analysis. The drug interaction with the receptor was done through different docks using Pyrex, Chimera and Viewer Lite software. The results showed that the desired compound was able to bind the active site of the enzyme and among the software, the best result was obtained from Pirex software. In fact, this compound had the highest level of negative binding energy (-7.5). Therefore, it was shown that the highest affinity for key amino acids is the active site of the enzyme and the site of interaction with the crystal molecule
_||_
