Sodium salt promoted the generation of nano zero valent iron by carbothermal reduction: For activating peroxydisulfate to degrade antibiotic.

Carbothermal reduction is a promising method for the industrial preparation of nano-zero-valent iron. Preparing it also involves very high pyrolysis temperatures, which leads to a significant amount of energy consumption. The temperature required for the preparation of nano-zero-valent iron by carbothermal reduction was reduced by 200 °C by the addition of sodium salt. Carbon-loaded nano zero-valent iron (Fe0/CB-Na) was prepared by carbothermal reduction through the addition of sodium salt. The results showed that Fe0/CB-Na@700 had the same activation performance as Fe0/CB@900 and the newly prepared nano-zero-valent iron. The addition of sodium salt promoted the transfer of oxygen from the iron oxide to the carbon structure during the roasting process so that the iron oxide was reduced to as much Fe0 as possible. Thus, sodium salts were optimized for the preparation of nano-zero-valent iron by carbothermal reduction through interfacial amorphization and oxygen transfer, thus reducing the preparation cost.

Enzymatic Generation of Thioaldehyde Motifs by Flavin-Dependent Cysteine Decarboxylases for Peptide Bioconjugation and Macrocyclization.

Thioaldehyde is a highly electrophilic group under aqueous conditions and can be generated via oxidative enzymatic modifications of cysteine residues in peptides and proteins. Herein, we report the installation of thioaldehyde and aldehyde groups at the C-terminus of peptides by flavin-dependent cysteine decarboxylases from the biosynthesis of ribosomally synthesized and post-translationally modified peptides. The in situ generated (thio)aldehyde is utilized as a reactive handle for peptide bioconjugation and macrocyclization.

Selection of immunodominant fragments from envelope gene for vaccine against Japanese encephalitis virus in DNA priming-protein boosting protocols.

Fragmentation of E gene of JEV into smaller fragments, none of the fragments either in plasmids form or in recombinant protein form can induce optimal protection against the virus infection. It is only when DNA priming-protein boosting strategies are used then the N-terminal E(A) and the C-terminal E(B) showed full protection against JEV as those induced by commercial vaccine, provided both fragments are preceded in the N-terminal by a signal peptide M(15) derived from C-terminal of prM gene in JEV genome. When the subfragments of E(A): E(A1) and E(A2) and E(B): E(B1) and E(B2) are tested, only E(A1) subfragment can replace E(A) in protein boosting to induce optimal protection against JEV, E(A2), E(B1), E(B2) in plasmid or protein forms are not. Therefore, along the E gene (978-2330 bp) N-terminal, E(A1) (978-1580 bp) and C-terminal E(B) (1851-2330 bp) are the most effective in inducing immunity against JEV but not the middle fragment E(A2) (1518-1877 bp) (see for orientation of E(A1), E(A2) and E(B) in E gene). Under the notion that molecular complexity determines the outcome of immune response of the host, E(B) being shorter, simpler in molecular structure and can be easily expressed in soluble form in E. coli (as opposed to insoluble E(A1)), E(B) probably will be the choice as a candidate vaccine to protect the host against JEV infection.