Sustainable Aerobic Bromination with Controllable Chemoselectivity.

The formation of C-Br(s) is one of the most fundamental reactions in organic synthesis. Oxidative bromination is a "green" way to achieve it. Aerobic bromination has drawn great interest in the past decades, while the poor substrate scope and selectivity, low efficiency, and the use of metal catalyst still confine its application. In this article, we establish a transition-metal-free aerobic bromination promoted by ionic liquid in a catalytic amount with controllable chemoselectivity toward numbers of C-Br(s) formed, and both NaBr/AcOH and HBr(aq) could be used as the bromine source. This methodology shows high efficiency and has a broad substrate scope for various kinds of C-H(s). We also validate this system by the gram-scale (one-pot) synthesis of functional molecules and direct recycle of the catalyst. The possible radical pathway of this catalysis is also presented with evidence.

Residue characteristics of sludge from a chemical industrial plant by microwave heating pyrolysis.

Sludge from biological wastewater treatment procedures was treated using microwave heating pyrolysis to reduce the environmental impact of a chemical plant. In this study, major elements, trace elements, PAHs and nitro-PAHs in raw sludge, and pyrolysis residues were investigated. The contents of major element from raw sludge were carbon 46.7 ± 5.9%, hydrogen 5.80 ± 0.58%, nitrogen 6.81 ± 0.59%, and sulfur 1.34 ± 0.27%. Trace elemental concentrations including Zn, Mn, Cr, Cd, As, and Sn were 0.410 ± 0.050, 0.338 ± 0.008, 0.063 ± 0.006, 0.019 ± 0.001, 0.004 ± 0.001, and 0.003 ± 0.002 mg/g, respectively. For various pyrolysis temperatures, Ca, Fe, Sr, Cr, and Sn contents remained at almost the same level as those in raw sludge. Results indicated that these elements did not easily volatilize. The content of 16 PAH species was about 4.78 µg/g in the raw sludge and 23-65 µg/g for pyrolysis residues associated with various temperatures. The content of ten nitro-PAHs was about 58 ng/g for the raw sludge and 141-744 ng/g for pyrolysis residues. The total nitro-PAH content was highest at 600 °C and then decreased when the temperature was over 600 °C. Total nitro-PAH content was about 247 ng/g at 800 °C.

Temperature influence on product distribution and characteristics of derived residue and oil in wet sludge pyrolysis using microwave heating.

Sludge taken from a wastewater treatment plant of the petrochemical industry was dewatered and pyrolyzed to produce liquid oil as an alternative fuel via microwave heating. Element contents of dried sludge were 45.9±3.85wt.% carbon, 7.70±1.43wt.% hydrogen, 4.30±0.77wt.% nitrogen and 3.89±0.52wt.% sulfur. Two major thermal degradation peaks of sludge were determined during the microwave pyrolysis process, one at 325-498K (most of the water was vaporized, and the weight loss was over 85wt.%) and the other at 548-898K for sludge constituent decomposition. Zn content was high in the dried raw material and residues. Other toxic elements such as Ni, Cr, Pb, As and Cd contents were 0.61-0.99, 0.18-0.46, 0.15-0.25, 0.018-0.034, and 0.006-0.017mg/g, respectively. About 14-20wt.% of oil was produced based on the dried sludge cake, and the oil major elements were C (69-72wt.%), H (5.7-6.7wt.%), N (1.9-2.2wt.%), and S (0.58-0.82wt.%). The heat values of liquid oils were 8700-9200kcal/kg at 400-800°C.

Recombinant VLP-Z of JC Polyomavirus: A Novel Vector for Targeting Gene Delivery.

Virus-like particle (VLP) of JC polyomavirus (JCPyV) is capable of packaging and delivering exogenous DNA into human cells and can be used for mediating therapeutic gene expression. However, many human cells express the JCPyV receptor. Thus, wild-type VLP can transduce a wide range of human cells nonspecifically. This study tested the feasibility of using a modified VLP with a IgG binding domain (Z domain) of protein A in its capsid for targeted gene delivery. The Z domain of protein A isolated from the membrane of Staphylococcus aureus was inserted into the NH3-terminus of VP1, the major JCPyV capsular protein. The recombinant VLP-Z was produced using Escherichia coli. Electron-microscopic analysis showed that VLP-Z has a viral-like structure. A hemagglutination test showed that VLP-Z has hemagglutination activity. VP(1) was detected in the nuclei of HeLa cells by immunostaining after VLP-Z inoculation, suggesting that VLP-Z is viable and can enter the cell nucleus. Inoculating HeLa cells with pEGFP-N(1) plasmid packaged in VLP-Z has resulted in enhanced green fluorescent protein expression in the cells. In addition, a binding assay showed that VLP-Z was able to bind IgG through the interaction of the Z domain in VLP-Z and IgG. These data suggest that VLP-Z could be armed with cell-specific antibody and be used to deliver therapeutic genes to target cells.