Amyloid fibrils from food proteins as functional delivery systems for bioactive compounds

Abstract

The accelerating demand for bioactive compounds (bioactives) that preserve their biological activity at the molecular level has necessitated novel delivery systems capable of shielding these compounds from diverse physicochemical stresses during processing, storage, and passage through the gastrointestinal tract (GIT) and its associated physical/chemical barriers. Most bioactives remain intrinsically unstable, poorly soluble, and rapidly degraded, underscoring the necessity for carrier systems with structural resilience and programmable release behaviour. Recently, food protein amyloid fibrils (PAFs) have emerged as a distinctive class of soft-matter architectures whose anisotropic morphology, exceptional mechanical rigidity, and polyvalent surface chemistry collectively enable controlled stabilization and protection of cargos. This review distills cutting-edge advances in PAF-engineered micro/nano-delivery systems, including fibril-stabilized emulsions, Pickering interfaces, hierarchical fibrillar complexes, and supramolecular hydrogels, emphasizing how PAF architecture dictates interfacial performance, GIT stability, and bioactive accessibility. By correlating molecular assembly pathways with macroscopic functional outcomes, we highlight emerging design principles and prospective opportunities for constructing next-generation amyloid-based delivery systems capable of enhanced bioavailability.