| Zein as a kind of natural and amphiphilic polymer materials, has extensive research and application. Zein is a kind of mixed protein and contains most α-zein. In this study, the self-assemble 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, and the inhibitory effect of hydrophobic interactions and ethanol in fibrillation of hydrophobic proteins was proved. The fibrillation of α-zein shows great potential in serving as bio-based gels or reinforced fillers in food, cosmetic and pharmaceutical applications.By adding nanocrystalline cellulose crystal into zein ethanol solution observed diluting ethanol concentration of the ethanol solution can inhibit self-assembly process into a spheres, prevented α-zein generating spheres. On hot hatch self-assembled nano crystalline cellulose fiber had a promoting effect, promoted generating branched chain nanofibers. At the same time, crystal fiber could improve the modulus of α-zein film increase membrane brittleness and fracture tensile, reduce elongation at break.We prepared curcμmin-loaded α-zein spheres by dilution method and hot hatch method, the experiments verified α-zein and curcμmin combined by hydrogen bond force. We found that hot hatch α-zein spheres drugs slow-release effect is the best, release quantity is good by comparing the preparation of curcμmin-loaded α-zeins. |