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.

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 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.