Preparation of a novel corn gluten meal hydrolysate against Helicobacter pylori: Structural characterization, screening and anti-adhesive mechanism analysis

In recent years, the number of people infected with Helicobacter pylori has increased rapidly, which has become a serious public health problem. Although the effect of antibiotic treatment is remarkable, the emergence of strain resistance and side effects associated with antibiotic use highlight the need to develop safe and novel adjunctive methods for the prevention and treatment of H. pylori . In this study, a novel corn gluten meal hydrolysate with high anti-adhesive activity against H. pylori and peptide recovery was prepared. First, the corn gluten meal was hydrolyzed with Neutrase, and the resulting Neutrase hydrolysate (CGMH 1 ) and precipitate were collected via centrifugation. Then, the precipitate was used as raw material and further hydrolyzed with Alcalase to yield the hydrolysate (CGMH 2 ). The combination of CGMH 1 and CGMH 2 yielded the hydrolysate (CGMH 4 ), which exhibits potent anti-adhesive activity against H. pylori and high peptide recovery. The anti-adhesive activity and peptide recovery rate of CGMH 4 were 45.86±0.35% and 72.01%, respectively, which lays a solid technical foundation for the subsequent development of CGMH 4 -based products. Superdex peptide gel chromatographic separation of CGMH 4 revealed that fractions less than 1 kDa had the best anti-adhesive activity. Based on the affinity specificity between peptides and H. pylori adhesins, 207 peptide sequences with potential anti-adhesive effects against H. pylori were isolated and identified from the less than 1 kDa fraction. Through the physicochemical properties of the identified peptides combined with molecular docking analysis, nine peptide sequences were further screened. Visual analysis results demonstrated that the binding energy between the screened peptides and adhesins was stronger, with hydrogen bonds and hydrophobic interactions serving as the primary driving forces for their binding. In addition, the screened peptides mainly bind to the active center of H. pylori adhesins and inhibit the interaction between these adhesins and gastric mucosal epithelial cell receptors via occupying the active site, which constitutes the primary mechanism underlying the anti-adhesive activity of CGMH 4 . This study provides a new strategy for the prevention and treatment of H. pylori infection. • A novel corn gluten meal hydrolysate (CGMH 4 ) against H. pylori was prepared. • The CGMH 4 has high anti-adhesive activity and peptide recovery. • Nine novel potential anti-adhesive peptides were identified and screened. • The screened peptide inhibited H. pylori infection by binding to the adhesins.