We report a facile method for the synthesis of cuprous oxide nanocrystals with systematic morphological evolution. Cubic, truncated cubic, cuboctahedral, truncated octahedral, octahedral, and short hexapod structures have been synthesized in an aqueous solution of CuCl2, NaOH, sodium dodecyl sulfate (SDS) surfactant, and hydroxylamine (NH2OH·HCl) reductant by simply varying the volume of hydroxylamine added to the reaction mixture. A slight modification in the volume of some reagents produced the extended hexapods. The order of the introduction of the reagents is important to the formation of these crystals with distinct morphologies and sharp faces. The sizes of these particles fall mostly in the range of 400−700 nm. Clear transition in the relative intensities of the (111) and the (200) reflection peaks in their XRD patterns was observed. Scattering bands dominate the UV−vis absorption spectra of these crystals. Crystal model analysis revealed that the {111} face contains surface copper atoms with dangling bonds, and is expected to interact more strongly with negatively charged molecules. Tests of photodegradation of negatively charged methyl orange showed that octahedra and the extended hexapods were catalytically active. The cubes with only the {100} faces were not active. On the contrary, both cubes and octahedra were not effective at photodecomposing positively charged methylene blue molecules. Surprisingly, octahedra and hexapods cannot be well suspended in the methylene blue solution; a significant amount of the crystals gradually moved to the surface of the solution with increasing stirring time. The results clearly demonstrate the dramatic differences in the catalytic activities of the {111} and {100} faces of Cu2O crystals for the first time.

The capsid of infectious bursal disease virus (IBDV), with a size of 60-65 nm, is formed by an initial processing of polyprotein (pVP2-VP4-VP3) by VP4, subsequent assemblage of pVP2 and VP3, and the maturation of VP2. In Sf9 cells, the processing of polyprotein expressed was restrained in the stage of VP2 maturation, leading to a limited production of capsid, i.e., IBDV-like particles (VLPs). In the present study, another insect cell line, High-Five (Hi-5) cells, was demonstrated to efficiently produce VLPs. Meanwhile, in this system, polyprotein was processed to pVP2 and VP3 protein and pVP2 was further processed to the matured form of VP2. Consequently, Hi-5 cells are better in terms of polyprotein processing and formation of VLPs than Sf9. In addition to the processing of pVP2, VP3 was also degraded. With insufficient intact VP3 protein present for the formation of VLPs, the excessive VP2 form subviral particles (SVPs) with a size of about 25 nm. The ratio of VLPs to SVPs is dependent on the multiplicity of infections (MOIs) used, and an optimal MOI is found for the production of both particles. VLPs were separated from SVPs with a combination of ultracentrifugation and gel-filtration chromatography, and a large number of purified particles of both were obtained. In conclusion, the insect cell lines and MOIs were optimized for the production of VLPs, and pure VLPs with morphology similar to that of the wild-type viruses can be effectively prepared. The efficient production and purification of VLPs benefits not only the development of an antiviral vaccine against IBDV but also the understanding of the structure of this avian virus that is economically important.

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