Wheat germ-derived peptides exert anti-adhesive activity against Helicobacter pylori: Insights into structural characteristics of identified peptides.

Approximately 50-80% of the world population are infected with H. pylori, which is categorized as a class I carcinogen. Anti-adhesive therapy is emerging as a promising alternative to antibiotics against bacterial infection. This study demonstrated that defatted wheat germ protein hydrolysates (DWGPH) effectively inhibited H. pylori adhesion to gastric epithelial cells. DWGPH prepared by Pronase possessed the best activity where its inhibitory percentage at 10 mg/mL was 51.7±6.8% and the minimum anti-adhesive concentration was 0.31 mg/mL. The anti-adhesive activity is attributable to peptides acting as receptor analogs in binding to H. pylori. Peptides with potential H. pylori-binding ability (n=267) were identified and their structural characteristics were comprehensively analyzed, including net charge, Boman index, instability index, aliphatic index, molecular weight, isoelectric point, hydrophobicity, and Hmoment (α-helix and β-sheet). This work provided an array of peptide sequences for further exploration as putative ligands of H. pylori adhesins and for elucidating molecular mechanisms.