Nanofilm Formed via Amyloid-Like Protein Aggregation for Interfacial Modification: Prospects in Food, Agricultural, and Beyond

Amyloid formation, once primarily associated with neurodegenerative diseases, has recently emerged as a versatile platform in materials science and biotechnology. In particular, amyloid-like aggregation triggered by reductive cleavage of disulfide bonds enables the formation of phase-transitioned protein (PTP) nanofilm at interfaces. The resulting nanofilm combines facile fabrication, robust adhesion, flexibility, and tunable functionalities, making it attractive as a sustainable, biobased material, with unique potential in food and agricultural applications where reviews remain lacking. This review outlines current knowledge of PTP nanofilms, focusing on molecular and physicochemical mechanisms underlying their aggregation, as well as key characterization and modulation strategies. Emphasis is placed on interfacial phenomena such as adsorption and tension regulation that govern nanofilm retention and stability. Emerging applications in food preservation and agriculture are highlighted, demonstrating the potential of PTP nanofilm to enhance sustainability and productivity. Future challenges and opportunities are briefly discussed to guide further development of PTP-based systems.