Hierarchically Porous Organic Cages.

Imparting mesopores to organic cages of an intrinsic microporous nature to build up hierarchically porous cage soft materials is a grand challenge and will reshape the property and application scope of traditional organic cage molecules. Herein, we discovered how to engineer mesopores into microporous organic cages via their host-guest interactions with long chain ionic surfactants. Equally important, the ionic head of surfactants equips the supramolecularly assembled porous structures with charge-selective uptake and release function in solution. Interestingly, such hierarchically porous organic cage can serve as a nanoreactor once trapping enzymes within the cavity, which show 5-fold enhanced activity of enzymatic catalysis when compared with the free enzymes.

Self-assembled artificial enzyme from hybridized porous organic cages and iron oxide nanocrystals.

HYPOTHESIS: Although it is well-accepted that iron oxide nanoparticles are considered as artificial enzymes when their surface is hydrophilic, the enzyme-like properties of iron oxide nanoparticles with hydrophobic surface coating is unexplored. This work demonstrates that hydrophobic iron oxide nanocrystals coated with a layer of oleic acid could serve as artificial enzymes when their surface is covered by a layer of ionic surfactant. Furthermore, the co-assembly of iron oxide nanocrystals and porous organic cages could modulate their enzyme-like activities. EXPERIMENTS: Co-assembly of iron oxide (Fe3O4) nanocrystals with different size and porous organic cages (POCs) was performed by an emulsion-confined strategy to achieve hybridized Fe3O4/POCs co-assemblies. The peroxidase-mimic activity of these co-assemblies were assessed in the presence of 3, 3', 5, 5'-Tetramethylbenzidine (TMB) and hydrogen peroxide. Finally, these co-assemblies were applied as sensors to detect glucose and hydrogen peroxide. FINDINGS: Co-assembly of Fe3O4 nanocrystals and POCs resulted in the self-assembly of Fe3O4 nanoparticles into two-dimensional nanoparticle superlattices on the eight (111) facets of the octahedral POCs colloidal crystals. The unique oil-in-water (O/W) emulsion confined assembly method switches the Fe3O4 nanoparticles and POC crystals from hydrophobic to hydrophilic because of the strong hydrophobic interactions. Importantly, these co-assemblies dispersed in water showed strong peroxidase-mimic activity in water despite that their surface is covered by a bilayer of aliphatic chains. Furthermore, the intrinsic enzymatic activity of the co-assemblies is highly dependent on the size of the nanocrystals, and a higher catalytic activity is achieved from a larger sized Fe3O4 nanocrystal.

Discrete Supracrystalline Heterostructures from Integrative Assembly of Nanocrystals and Porous Organic Cages.

Although self-assembly across multiple length scales has been well recognized and intensively investigated in natural biological system, the design of artificial heterostructures enabled by integrative self-assembly is still in its infancy. Here we report a strategy toward the growth of discrete supracrystalline heterostructures from inorganic nanocrystals and porous organic cages (CC3-R), which in principle relies on the host-guest interactions between alkyl chains coated on nanocrystals and the cavity of cage molecules. Density functional theory calculation indicates that an attractive energy of ∼-2 kBT is present between an alkyl chain and the cavity of a CC3-R molecule, which is responsible for the assembly of nanocrystal superlattices on the CC3-R octahedral crystals. Of particular interest is that, determined by the shape of the nanocrystals, two distinct assembly modes can be controlled at the mesoscale level, which eventually produce either a core/shell or heterodimer supracrystalline structure. Our results highlight opportunities for the development of such a noncovalent integrative self-assembly not limited to a particular length scale and that could be generally applicable for flexible integration of supramolecular systems.

[Effects of high temperature on Bt protein content and nitrogen metabolic physiology in boll wall of Bt cotton].

Bt cotton cultivar Sikang 1 (a conventional cultivar) and Sikang 3 (a hybrid cultivar) from China, and 99B (a conventional cultivar) and Daiza 1 (a hybrid cultivar) from USA were selected as experimental materials, the ball wall Bt protein content and nitrogen metabolic physiology were investigated under different high temperature levels at peak boll stage. The results showed that the Bt protein content of boll wall decreased with the increasing temperature. Compared with the control (32 °C, the boll wall Bt protein content decreased significantly when the temperature was above 38 °C for the conventional cultivars and above 40 °C for the hybrid cultivars. The Bt protein contents of cultivar Sikang 1 and 99B decreased by 53.0% and 69.5% respectively with the temperature at 38 °C, and that of cultivar Sikang 3 and Daiza 1 decreased by 64.8% and 54.1% respectively with the temperature at 40 °C. Greater reductions in the boll wall soluble protein contents and GPT activities, larger increments for the boll wall free amino acid contents and proteinsase activities were also observed when the boll wall Bt protein content was significantly reduced. Therefore, high temperature resulted in the reduction of Bt protein synthesis and increase of the insecticidal protein degradation in the boll wall significantly, which caused the reductions in boll wall Bt protein content and insect resistance.

[Effects of high temperature on Bt proteins expression and nitrogen metabolic physiology in square of Bt cotton at the peak squaring stage].

Taking Bt cotton Sikang 1 (a conventional cultivar), Sikang 3 (a hybrid cultivar) from China and 99B (a conventional cultivar), Daiza 1 (a hybrid cultivar) from USA as test materials, the effects of different high temperatures on thesquare Bt proteins expression and nitrogen metabolic physiology were investigated. The results showed that the square Bt protein contents of the four cultivars decreased significantly above 38 °C compared with that at 32 °C. The higher the temperature was above 38 °C, the greater the reduction extent of the Bt protein content was. The square Bt protein contents of the hybrid cultivars were higher than that of the conventional cultivars, and were less reduced under the high temperature stress. The cultivars with bigger reductions in Bt protein content also showed greater reductions in the square soluble protein contents, pyruvic transaminase activities and glutamic oxaloacetic transaminase activities, while larger increments were detected for the square free amino acid contents, proteinsase activities and peptidase activities.