Update of the interaction between polyphenols and amyloid fibrils

Amyloid fibrils were initially known for the implications in neurodegenerative diseases, such as Alzheimer’s and Parkinson’s diseases. In this context, the interaction between polyphenols and amyloid fibrils has attracted intensive interest in the journey of pursuing therapies to slow down the progress of amyloidosis-related diseases. It is generally concluded that polyphenols inhibit the formation of amyloid fibrils and remodel or cut the mature ones, which are observed in low protein concentrations. Unfolding and self-assembly of food-grade proteins result in amyloid fibrils. Our very recent studies demonstrated that polyphenols absorb and deposit on the surface of amyloid fibrils forming the supramolecular nanofilaments which self-assemble in multi-length scales to form hierarchical structures. This finding has created the food hybrid hydrogels with unique properties of incomparable high loading content and stability of polyphenols, target delivery to colon and re-construction of gut microbiota for health promotion. It paves ways for food molecular processing.