Comparative analysis of peptide and protein self-assembly in food systems: Driving forces, influencing factors,...

Protein and peptide self-assembly is a crucial strategy for bioactive delivery, texture modulation, and food packaging. This review provides a systematic comparative analysis of protein and peptide self-assembly, focusing on intrinsic driving forces, the regulatory effects of external stimuli and coexisting components, the resulting forms of self-assembled products, and the main differences in their applications within food systems. Protein self-assembly is driven by multi-level conformational interactions and synergistic non-covalent forces combined with disulfide bonds, which confers outstanding performance in food texture improvement and preservation. Peptide self-assembly is dominated by amino acid sequences, with sequence-dependent π-π stacking and metal coordination as pivotal tunable driving forces, exhibiting superior advantages in targeted delivery and sensory modulation. Under external regulation, both can form typical assembled structures including nanoparticles, nanofibers, and hydrogels. By harnessing protein and peptide self-assembly, these bottom-up technologies enable food structuring and textural enhancement, opening new avenues for modern food systems.