Hydrophobicity‐modulating self‐assembled morphologies of α‐zein in aqueous ethanol

Summary Protein fibrillation serves a broad range of biological functions from surface colonising to mechanically reinforcing structures; it is also associated with the development of neurodegenerative disorders. Although fibrillation is considered to be an inherent ability of polypeptides to form backbones, relevant studies have long concentrated on aqueous‐soluble proteins rather than on insoluble structures. In this study, the self‐assembly of hydrophobic proteins into amyloid nanofibrils was studied using α‐zein as a model protein. The self‐assembled morphologies of α‐zein were determined by hydrophobic–hydrophilic characters of both the protein and the solvent. Upon thermally incubating in aqueous ethanol, α‐zein formed amyloid nanofibrils with lower ethanol compositions and near‐neutral pHs, while acidic conditions and high ethanol compositions result in the formation of spherical aggregations. The fibrillation of α‐zein shows a great potential in serving as bio‐based gels or reinforced fillers in food, cosmetic and pharmaceutical applications.