Background
Self-assembly behavior of bioactive peptides has emerged as a research hotspot, offering novel approaches to enhance digestive stability and develop functional foods.
Scope and approach
This study systematically elucidated the molecular mechanisms of peptide self-assembly and its crucial role in enhancing peptide structural stability and digestive resistance.
Key findings and conclusion
By adjusting environmental factors (such as temperature and pH), and by designing peptide sequences enriched with aromatic amino acids, bioactive peptides can undergo molecular self-assembly to form highly ordered nanostructures, including through molecular self-assembly, including nanofibers, micelles, and hydrogels. This self-assembling structure can markedly enhance the digestive stability of bioactive peptides in the gastrointestinal environment, thereby improving their bioavailability and delivery efficiency. Bioactive peptides rich in proline also exhibit excellent anti-digestive activity. These self-assembling peptides exhibit multifunctional biological activities, including antioxidant, antibacterial, and anti-inflammatory properties. Self-assembly enables improved encapsulation efficiency, controlled and targeted release, enhanced bioavailability, and optimized sensory properties, supporting the development of functional foods and nutritional supplements for precision nutrition. However, clinical translation remains constrained by challenges in structural stability, in vivo absorption, and safety. Notably, the self-assembly behavior of bioactive peptides under physiological conditions is still poorly understood. This study reviewed the molecular basis of peptide self-assembly in regulating digestive stability and provides a theoretical framework for designing efficient delivery systems and functional foods.


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