Abstract
Anti-adhesive activity of wheat germ-derived peptides, which is considered as one of the promising strategies for preventing Helicobacter pylori infection, was investigated. The underlying mechanism of anti-adhesive action was due to peptides acting as receptor analogues and binding to H. pylori adhesin proteins. However, there is lack of information on the nature and strength of this molecular interaction as well as the participating species and drug-likeness of the food-derived bioactive peptides. In this study, the biostability and ADME/Tox (absorption, distribution, metabolism, excretion and toxicity) profile of the anti-adhesive peptides were analyzed using bioinformatic tools, and their binding potential to H. pylori’s adhesins estimated by molecular docking. Binding is facilitated by mostly hydrogen bonding and hydrophobic interaction occurring in the active site of the adhesin proteins with affinities ranging from -6.0 to -7.4 and -6.0 to -7.8 kcal/mol for BabA and SabA, respectively. The results indicate highly possible binding capabilities of the peptides to adhesin proteins. Out of 16 peptides studied, 14 bound in the vicinity of the active site of BabA and SabA whereas two different peptides demonstrated allosteric binding. The most hydrophobic peptide, P210 showed strong binding affinity for both BabA and SabA and, therefore, predicted to be the most promising peptide for further development in the prevention, management and treatment of H. pylori infection. The selected peptides were shown to be non-toxic, and to have high potential of localized effect of interfering with bacterial adherence. This work provides insights into the anti-adhesive mechanism of peptides and new evidence demonstrating bioactive peptides as promising nutraceutical candidates for preventing H. pylori infection.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.