Recent advances in bimetallic nanoscale zero-valent iron composite for water decontamination: Synthesis, modification and mechanisms.

The environmental pollution of water is one of the problems that have plagued human society. The bimetallic nanoscale zero-valent iron (BnZVI) technology has increased wide attention owing to its high performance for water treatment and soil remediation. In recent years, the BnZVI technology based on the development of nZVI has been further developed. The material chemistry, synthesis methods, and immobilization or surface stabilization of bimetals are discussed. Further, the data of BnZVI (Fe/Ni, Fe/Cu, Fe/Pd) articles that have been studied more frequently in the last decade are summarized in terms of the types of contaminants and the number of research literatures on the same contaminants. Five contaminants including trichloroethylene (TCE), Decabromodi-phenyl Ether (BDE209), chromium (Cr(VI)), nitrate and 2,4-dichlorophenol (2,4-DCP) were selected for in-depth discussion on their influencing factors and removal or degradation mechanisms. Herein, comprehensive views towards mechanisms of BnZVI applications including adsorption, hydrodehalogenation and reduction are provided. Particularly, some ambiguous concepts about formation of micro progenitor cell, production of hydrogen radicals (H·) and H2 and the electron transfer are highlighted. Besides, in-depth discussion of selectivity for N2 from nitrates and co-precipitation of chromium are emphasized. The difference of BnZVI is also discussed.

Cell surface glycan engineering reveals that matriglycan alone can recapitulate dystroglycan binding and function.

α-Dystroglycan (α-DG) is uniquely modified on O-mannose sites by a repeating disaccharide (-Xylα1,3-GlcAß1,3-)n termed matriglycan, which is a receptor for laminin-G domain-containing proteins and employed by old-world arenaviruses for infection. Using chemoenzymatically synthesized matriglycans printed as a microarray, we demonstrate length-dependent binding to Laminin, Lassa virus GP1, and the clinically-important antibody IIH6. Utilizing an enzymatic engineering approach, an N-linked glycoprotein was converted into a IIH6-positive Laminin-binding glycoprotein. Engineering of the surface of cells deficient for either α-DG or O-mannosylation with matriglycans of sufficient length recovers infection with a Lassa-pseudovirus. Finally, free matriglycan in a dose and length dependent manner inhibits viral infection of wildtype cells. These results indicate that matriglycan alone is necessary and sufficient for IIH6 staining, Laminin and LASV GP1 binding, and Lassa-pseudovirus infection and support a model in which it is a tunable receptor for which increasing chain length enhances ligand-binding capacity.