Molecular docking of gliadin peptide towards bacterial toxins of Escherichia coli, Pseudomonas aeruginosa, and Staphylococcus aureus

Finding effective biocompatible antibacterial compounds is indispensable for reducing multidrug-resistant (MDR)-associated foodborne infections. Applying natural materials extracted from plant species with high availability against bacterial toxins may be one promising strategy. In this study, we surveyed the interaction of peptide related to alpha/beta-gliadin MM۱, a main component of Triticum aestivum (wheat) gluten, with three main bacterial toxins, involving Shiga toxin type ۲ (Stx-۲) B subunit, Pseudomonas elastase, and alpha-hemolysin (α-HL), related to E. coli, P. aeruginosa, and S. aureus, respectively. This molecular docking study, according to the protein-protein HDOCK server, suggests that gliadin can interact with these three receptors. Results displayed high and low affinities of gliadin for α-HL and Stx-۲ B subunit receptors, respectively. In future studies, in vitro and in vivo tests should be used to evaluate these results.  In this case, preparing different nanoformulations of gliadin with other antibacterial agents may be an effective approach.

کلیدواژه ها:

multidrug-resistant bacteria ، Gliadin peptide ، Molecule docking ، Bacterial Toxins ، Shiga toxin type ۲ ، Pseudomonas elastase ، Alpha-hemolysin