Eco-friendly one-pot synthesis of Prussian blue-embedded magnetic hydrogel beads for the removal of cesium from water

A simple one-step approach to fabricating Prussian blue-embedded magnetic hydrogel beads (PBMHBs) was fabricated for the effective magnetic removal of radioactive cesium (Cs-137) from water. Through the simple dropwise addition of a mixed aqueous solution of iron salts, commercial PB and polyvinyl alcohol (PVA) to an ammonium hydroxide (NH4OH) solution, the formation of hydrogel beads and the encapsulation of PB in beads were achieved in one pot through the gelation of PVA with in situ-formed iron oxide nanoparticles as the cross-linker. The obtained PB-MHBs, with 43.77 weight %of PB, were stable without releasing PB for up to 2 weeks and could be effectively separated from aqueous solutions by an external magnetic field, which is convenient for the large-scale treatment of Cs-contaminated water. Detailed Cs adsorption studies revealed that the adsorption isotherms and kinetics could be effectively described by the Langmuir isotherm model and the pseudo-second-order model, respectively. Most importantly, the PB-MHBs exhibited excellent selectivity for Cs-137 in (137)Cscontaminated simulated groundwater (55 Bq/g) with a high removal efficiency (>99.5%), and the effective removal of Cs-137 from real seawater by these PB-MHBs demonstrated the excellent potential of this material for practical application in the decontamination of Cs-137-contaminated seawate

Interactions between Amyloidophilic Dyes and Their Relevance to Studies of Amyloid Inhibitors

Amyloid fibrils are filamentous aggregates of peptides and proteins implicated in a range of neurodegenerative disorders such as Alzheimer's and Parkinson's diseases. It has been known almost since their discovery that these β-sheet-rich proteinacious assemblies bind a range of specific dyes that, combined with other biophysical techniques, are convenient probes of the process of amyloid fibril formation. Two prominent examples of such dyes are Congo red (CR) and Thioflavin T (ThT). It has been reported that in addition to having a diagnostic role, CR is an inhibitor of the formation of amyloid structures, and these two properties have both been explained in terms of the same specific noncovalent interactions between the fibrils and the dye molecules. In this article, we show by means of quartz-crystal microbalance measurements that the binding of both ThT and CR to amyloid fibrils formed by the peptide whose aggregation is associated with Alzheimer's disease, Aβ(1–42), can be directly observed, and that the presence of CR interferes with the binding of ThT. Light scattering and fluorescence measurements confirm that an interaction exists between these dyes that can interfere with their ability to reflect accurately the quantity of amyloid material present in a given sample. Furthermore, we show that CR does not inhibit the process of amyloid fibril elongation, and therefore demonstrate the ability of the quartz-crystal microbalance method not only to detect and study the binding of small molecules to amyloid fibrils, but also to elucidate the mode of action of potential inhibitors