Elucidating the Differences in the Biofilm Suppression Mechanism of 6-Gingerol and 6-Shogaol in Pseudomonas aeruginosa through Molecular Docking

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Research Paper 01/02/2021
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Elucidating the Differences in the Biofilm Suppression Mechanism of 6-Gingerol and 6-Shogaol in Pseudomonas aeruginosa through Molecular Docking

ohn Sylvester B. Nas, Francisco R. Gellecanao, Danica M. Malacad, Jose Alfonso G. Manugas, Gildred Christian L. Mutia, Mikaela D. Paguibitan, Mark Johndel M. Quilala, Trisha Joy Basille A. Rodriguez, Mary Janniezl S. Tee
Int. J. Biosci.18( 2), 1-10, February 2021.
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Abstract

The virulence of Pseudomonas aeruginosa (P. aeruginosa) is associated with its biofilm formation via quorum sensing. Compounds present in Zingiber officinale (Z. officinale) such as 6-gingerol and 6-shogaol show antibacterial property against different bacteria. However, the mechanism of action of these compounds is underexplored. Hence, we compared the biofilm reduction of these compounds and visualized their binding interactions to different pathways to hypothesize a possible mechanism of action associated with the biofilm reduction. In this study, the biofilm formation of P. aeruginosa treated with varying concentrations of either 6-shogaol or 6-gingerol was determined through biofilm accumulation assay. The binding affinity of 6-gingerol and 6-shogaol with various enzymes involved in the membrane integrity, lipopolysaccharide formation, motility, and fatty acid synthesis were ranked through molecular docking. The crystal structures of the compounds docked to the top 3 enzymes with the most negative docking score were evaluated. Results show that 6-gingerol suppressed the biofilm formation of P. aeruginosa significantly higher (p<0.05) than 6-shogaol. Besides, 6-gingerol has a strong binding affinity to an enzyme associated with membrane integrity while 6-shogaol to a motility-related enzyme. The top enzymes were associated with membrane integrity, lipopolysaccharide formation, and motility. The differences in the binding affinity of 6-gingerol and 6-shogaol may be attributed to the varying substructures involved during the non-covalent interactions. Moreover, we speculate that there are other factors involved that resulted in a higher binding affinity of 6-shogaol despite having fewer interactions. These factors may be independent or complementary with the non-covalent bonding, which may be essential to their biofilm suppression property.

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