16 Insilico Prediction of Curcumin Binding Site in Human Serum Albumin Using Autodock Vina

Wednesday, November 4, 2009
Ballroom A+B (Camino Real Hotel)
Suman Sirimulla , Department of Chemistry, University of Texas at El Paso, El Paso, TX
William C. Herndon , Department of Chemistry, University of Texas at El Paso, El Paso, TX
Mahesh Narayan , Department of Chemistry, University of Texas at El Paso, El Paso, TX

Curcumin is known for its antitumor, antioxidant, antiarthritic, anti-amyloid, anti-ischemic, and anti-inflammatory properties. The low bioavailability of curcumin in both humans and animals has raised several concerns that this may limit its clinical impact. Curcumin associates with serum albumin by hydrophobic interactions and is transported to appropriate cells wherein it elicits its pharmacological actions. As the bioavailability of curcumin is low, there is a need to develop new analogs which have preferentially enhanced biological activity and bioavailability. In the present study we used Autodock Vina, a docking software to predict the binding site of curcumin in human serum albumin. Docking was performed placing grid box on entire protein molecule. The docking results propose four possible binding pockets for curcumin in human serum albumin, two in each chain. Depending upon the binding affinity best 9 docking poses were taken in to further consideration. The best docking pose was near amino acids, ALA194, PRO 113. The binding affinities of these poses range from -6.9 to -6.0 kcal/mol. These results indicate that human serum albumin may serve as a viable agent to improve the bioavailability of curcumin.

Predicted binding site of curcumin within Human Serum albumin with binding affinity-6.9Kcal/mol

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