Anti-adhesive activity peptides against Helicobacter pylori from corn protein: Properties, identification, structural characterization and molecular docking in vitro and in silico

Abstract

The population infected with Helicobacter pylori (H. pylori) is huge, and it is designated as a class I carcinogen by the World Health Organization (WHO). Inhibiting H. pylori adhesion to gastric mucosal epithelial cells (GES-1 cells) is an effective way to prevent H. pylori infection. In the present study, the properties, identification, structural characterization and mechanism of anti-adhesive activity peptides against H. pylori from corn protein were studied in vitro and in silico. It was found that corn protein-derived peptides prepared by Neutrase could effectively inhibit H. pylori adhesion to GES-1 cells as a receptor analog, and they possessed a low molecular weight distribution (less than 1000 Da accounting for 74.10%) and more hydrophobic amino acids. 241 peptide sequences with potential H. pylori-binding ability were identified and further analyzed for their structural characteristics. Anti-adhesive mechanism studies revealed that Neutrase-CPH inhibited H. pylori adhesion to GES-1 cells by interacting specifically with H. pylori adhesins SabA and BabA, and hydrogen bonds are the main driving forces. In addition, two novel anti-adhesive activity peptides, EFFAEY and VCENPIL, were evaluated in vitro, their anti-adhesive activity was 40.77 ± 1.57% and 34.86 ± 1.36% at 4 mg/mL, respectively. Overall, corn protein-derived anti-adhesive peptides might be applied as a potential functional food ingredient to prevent H. pylori infection, and this study provides theoretical support for the development of anti-adhesive functional food.