Hydrophobicity-modulating self-assembled morphologies of α-zein in aqueous ethanol. An, B. , Wu, X. , Li, M. , Chen, Y. , Li, F. , & Yan, X. , et al. (2016).International Journal of Food Science & Technology, 51(12), 2621-2629.-成果-仿生智能材料研究组  
Hydrophobicity-modulating self-assembled morphologies of α-zein in aqueous ethanol. An, B. , Wu, X. , Li, M. , Chen, Y. , Li, F. , & Yan, X. , et al. (2016).International Journal of Food Science & Technology, 51(12), 2621-2629. 2016 生物质基 论文
lvll 2019-6-18 256

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 selfassembly 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.

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