Comparison of Fibrillation Ability, Self-Assembly Behavior and Structural Characteristics of Wheat Gluten and Its Components Amyloid Fibrils

) for nucleation. The lowest hydrophobicity index (168.45) and Zeta potential (-19.6 mV) of glutenin hydrolyzed peptides conferred diminished fibrillation propensity, ultimately yielding short (2.77 μm) flexible fibrils. Fibrils derived from gluten hydrolysates exhibited the highest β-sheet content (50.05%), the largest particle size (434.85 nm), and the greatest fibril length (5.72 μm). Gluten amyloid fibrils displayed morphological polymorphism, potentially resulting from synergistic interactions between glutenin and gliadin, including template-induced assembly and disulfide cross-linking. This study reveals component-level formation mechanisms of wheat gluten amyloid fibrils, with potential implications for food applications.