This study investigates the differences in physicochemical properties, structural characteristics, and fibril morphology among three wheat gluten with distinct secondary structure contents (A protein: high α-helices, low β-sheets, low random coils; C protein: low α-helices, high β-sheets, high random coils; B protein: intermediate structure) when amyloid-like fibrils (AFs) are formed under boiling and steaming conditions. Congo red absorption, polarized light microscopy, and X-ray diffraction confirmed the formation of AFs in proteins A, B, and C under boiling and steaming conditions. Thioflavin T fluorescence revealed that C-protein-derived fibrils (CPF) exhibited the highest intensity, indicating the strongest fibril-forming ability. SE-HPLC analysis showed a gradual increase in molecular weight and AFs contents with prolonged heating. Increased heating time led to larger particle sizes, higher β-sheet content, and involvement of aromatic amino acids in β-sheet formation via π-π stacking, promoting fibril growth. These changes were more pronounced under steaming conditions. AFM revealed that under steaming, the C protein formed longer and taller fibril structures than under boiling. This work establishes a theoretical foundation for understanding the growth mechanism of AFs formed by gluten proteins with different structures during food processing.