In this paper we report the docking evaluation and performance of catechin and its derivatives in inhibiting the FTO (Fat mass and obesity-associated) protein for controlling the obesity problem. The results show that Arg-52 and Tyr-39 residues play role in hydrogen binding, while Trp-42, Pro-47 and Ile-50 play role in hydrophobic interactions between ligands and the FTO enzyme. All catechin and its derivatives ,except epicatechin, shows a promising potential as FTO inhibitor as shown by their binding affinity (ΔG) values which are lower than the binding affinity of the patented drug, orlistat (-6.2 kcal/mol). The gallocatechin compound was found to be the best FTO inhibitor with the binding affinity of ΔG=-7.70 kcal/mol and the binding site similarity to orlistats of 63.6%.
Key words: catechin derivatives, green tea, FTO protein, obesity, molecular docking.
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