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: Amyloid (mycology); Hydrophobic effect

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