Amyloid‐Like Assembly to Form Film at Interfaces: Structural Transformation and Application

Abstract Protein‐based biomaterials are attracting broad interest for their remarkable structural and functional properties. Disturbing the native protein's three‐dimensional structural stability in vitro and controlling subsequent aggregation is an effective strategy to design and construct protein‐based biomaterials. One of the recent developments in regulating protein structural transformation to ordered aggregation is amyloid assembly, which generates fibril‐based 1D to 3D nanostructures as functional materials. Especially, the amyloid‐like assembly to form films at interfaces has been reported, which is induced by the effective reduction of the intramolecular disulfide bond. The main contribution of this amyloid‐like assembly is the large‐scale formation of protein films at interfaces and excellent adhesion to target substrates. This review presents the research progress of the amyloid‐like assembly to form films and related applications and thereby provides a guide to exploiting protein‐based biomaterials.