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Online Journal of Bioinformatics

Established 1995

ISSN 1443-2250

 

Volume 20(1):32-42, 2019.


Molecular docking of curcumin analogs with phospholipase A2.

 

Dileep KV, Tintu G, Sadasivan, C*

 

Department of Biotechnology and Microbiology, Kannur University, Thalassery Campus, Palayad P O, Kerala 670661, India.

 

ABSTRACT

 

Dileep KV, Tintu G, Sadasivan C., Molecular docking of curcumin analogs with phospholipase A2, Onl J Bioinform., 20(1):32-42, 2019. The enzyme phospholipase A2 is responsible for the hydrolysis of membrane phospholipids that release arachidonic acid, which serves as substrate for pro-inflammatory mediators, such as prostaglandins and leukotrienes. Binding of the substrate to PLA2 occurs through a well-formed hydrophobic channel and blocking the hydrophobic channel is an effective way to inhibit PLA2. Compounds inhibiting PLA2 have been implicated as potential therapeutic agents in treatment of inflammation related diseases. Curcumin is a well studied compound isolated from the plant Curcuma longa. We describe binding of 28 curcumin analogs to PLA2 by molecular modeling and docking and mode of interactions of compounds with strong binding. We determined that natural and synthetic analogs rosmarinic acid, tetrahydrocurcumin, dihydrocurucmin and hexahydrocurcumin had higher binding energy than curcumin. These findings may lead to better understanding of PLA2 inhibition by curcumin analogs and improved anti-inflammatory drugs.

 

Keywords : PLA2: curcumin analogs : Molecular docking, PLA2


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