Multiscale hierarchical perspectives on food protein amyloid fibrils: A review

Amyloid fibrils (AFs) represent a promising form of hierarchical self-assembly and are considered fundamental supramolecular units for the development of various macroscopic protein materials. Following safety validation, food protein amyloid fibrils (FPAFs) have been assembled into multifunctional materials, with potential applications spanning a wide range of fields, including food science, biomedicine, and smart manufacturing. There has been research regarding the hierarchical architecture of AFs-based materials, from protein molecules to the macroscopic structures. However, the documentation on FPAFs has predominantly focused on their formation and functional applications, resulting in a lack of comprehensive reviews addressing the hierarchical assembly of food proteins across different length scales. This review aims to provide an overview of recent advancements in the self-assembly of FPAFs at both molecular and mesoscale levels. Furthermore, it emphasizes the construction of multi-scale hierarchical structures at the macroscopic level, exploiting the ordered framework and exceptional properties of FPAFs. Additionally, the review summarizes future opportunities and challenges associated with FPAFs, to identify promising avenues for significant breakthroughs in cutting-edge fields.