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

• DOI: 10.1111/ijfs.13248
• Publication Date: 2016-10-25T09:23:13Z
• Authors: Baozhen An; Xiaochen Wu; Mingjie Li; Yijun Chen; Fei Li; Xiaofei Yan; Jialin Wang; Chaoxu Li; Charles Brennan
• Keywords: 0301 basic medicine; 03 medical and health sciences; ANZSRC::3210 Nutrition and dietetics; hydrophobic interaction; ANZSRC::3006 Food sciences; amyloid nanofibrils; ANZSRC::4004 Chemical engineering; α-zein; 540; self-assemble

SummaryProtein 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.