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

An, B
Wu, X
Li, M
Chen, Yijun
Li, F
Yan, X
Wang, Jialin
Li, C
Brennan, CS
Journal Article
Fields of Research
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.
© 2016 Institute of Food Science and Technology
Creative Commons Rights
Access Rights