Insights from the molecular docking of curcumin to the virulent factors of Helicobacter pylori |
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Authors: | Akhileshwar Kumar Srivastava Vikas Kumar Bijoy Krishna Roy |
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Institution: | Department of Botany, Banaras Hindu University, Varanasi, 221005, India |
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Abstract: | The domains of virulent (Ureα/β, VacA-p55, and CagA) factors of Helicobacter pylori play a pivotal role in developmental
processes of numerous diseases including gastric cancer. The pharmacological role of curcumin indicates that it could regulate the
signaling of virulent factors by interacting with active domains. However, the controlling mechanism of the curcumin interactions
and the binding diversity on structural basis of virulent (Ureα/β, VacA-p55, and CagA) factors are unknown. Curcumin as
therapeutic agent was filtered by using Lipinski rule׳s five and the druglikeness property for assessment of pharmacological
properties. Here outcome of molecular docking presented the 3-D structure of curcumin complex, that interacted with especially
conserved residues of target domains. The structure revealed that the curcumin complexation with domains of these proteins
provided structural insight into the diverse nature of proteins (Ureα/β, VacA-p55, and CagA) recognition. In silico study
elucidated that the broad specificity of curcumin was achieved by multiple binding mode mechanisms such as distinct hydrogen
and hydrophobic interactions with involvement of binding energy. The higher score of curcumin in complexation with both
subunits Ureα/β showed the stable binding, and less stability with VacA-p55 complexation with lower score. Curcumin exhibited
good interaction with these targeted virulent factors, although extensive interactions of curcumin with Ureα/β subunits could have
an important implication to prevent survival and colonisation of H. pylori in stomach. |
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Keywords: | Curcumin Docking Helicobacter pylori Residues |
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