Wheat Germ-Derived Peptides Exert Antiadhesive Activity against <i>Helicobacter pylori</i>: Insights into Structural Characteristics of Identified Peptides

Abstract

Approximately 50-80% of the world population are infected with <i>H. pylori</i>, which is categorized as a class I carcinogen. Antiadhesive therapy is emerging as a promising alternative to antibiotics against bacterial infection. This study demonstrated that defatted wheat germ protein hydrolysates (DWGPH) effectively inhibited <i>H. pylori</i> 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 antiadhesive concentration was 0.31 mg/mL. The antiadhesive activity is attributable to peptides acting as receptor analogs in binding to <i>H. pylori</i>. Peptides with potential <i>H. pylori</i>-binding ability (<i>n</i> = 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 <i>H. pylori</i> adhesins and for elucidating molecular mechanisms.