Investigation of the effect of curcumin on helicobacter pylori 5'-methylthioadenosine/s-adenosylhomocysteine nucleosidase with molecular dynamics method

Helicobacter pylori (H. pylori) is a bacteria that causes gastric ulcers and stomach infections. H. pylori requires the protein 5′-methylthioadenosine/S-adenosylhomocysteine nucleosidase (MTAN) for many bacterial metabolic processes including the methionine and purine salvage pathways, the futalosine pathway, and polyamine biosynthesis. Since MTAN plays an important role in bacterial metabolism and communication, it can be an important inhibitor target to prevent H. pylori growth. A natural compound curcumin can be considered as potent inhibitor against H. pylori growth. In this study, we investigated the effect of curcumin on the conformational structure and dynamics of HpMTAN using Molecular Dynamics simulations. We compared the behavior of HpMTAN when curcumin is bound to single and both chain(s) of HpMTAN. Our results reveal that curcumin has a high binding energy of around -8 kcal/mol with HpMTAN and forms Hydrogen bonds with some active site residues. In addition, it was observed that curcumin binding to HpMTAN does not cause large conformational changes and large residue fluctuations, however, it arises both inter and intra chain correlations of HpMTAN.