Comparison of the Improvement Effect of Deep Ocean Water with Different Mineral Composition on the High Fat Diet-Induced Blood Lipid and Nonalcoholic Fatty Liver Disease in a Mouse Model.

Accumulated lipid droplets in liver cause nonalcoholic fatty liver disease (NAFLD). Deep ocean water (DOW) containing high levels of magnesium, calcium, and potassium, etc. was proven to suppress hepatic lipid in obese rats fed high fat diet in the previous study.

Real-Time Observation of Anion Reaction in High Performance Al Ion Batteries.

Recently, aluminum ion batteries (AIBs) have attracted great attention across the globe by virtue of their massive gravimetric and volumetric capacities in addition to their high abundance. Though carbon derivatives are excellent cathodes for AIBs, there is much room for further development. In this study, flexuous graphite (FG) was synthesized by a simple thermal shock treatment, and for the first time, an Al/FG battery was applied as a cathode for AIBs to reveal the real-time intercalation of AlCl into FG with high flexibility by using in-situ scanning electron microscope (SEM) measurements exclusively.

Revealing structural changes of prion protein during conversion from α-helical monomer to β-oligomers by means of ESR and nanochannel encapsulation.

Under nondenaturing neutral pH conditions, full-length mouse recombinant prion protein lacking the only disulfide bridge can spontaneously convert from an α-helical-dominant conformer (α-state) to a β-sheet-rich conformer (β-state), which then associates into β-oligomers, and the kinetics of this spontaneous conversion depends on the properties of the buffer used. The molecular details of this structural conversion have not been reported due to the difficulty of exploring big protein aggregates. We introduced spin probes into different structural segments (three helices and the loop between strand 1 and helix 1), and employed a combined approach of ESR spectroscopy and protein encapsulation in nanochannels to reveal local structural changes during the α-to-β transition.

Amyloid core formed of full-length recombinant mouse prion protein involves sequence 127-143 but not sequence 107-126.

The principal event underlying the development of prion disease is the conversion of soluble cellular prion protein (PrP(C)) into its disease-causing isoform, PrP(Sc). This conversion is associated with a marked change in secondary structure from predominantly α-helical to a high β-sheet content, ultimately leading to the formation of aggregates consisting of ordered fibrillar assemblies referred to as amyloid. In vitro, recombinant prion proteins and short prion peptides from various species have been shown to form amyloid under various conditions and it has been proposed that, theoretically, any protein and peptide could form amyloid under appropriate conditions.

Slow spontaneous α-to-β structural conversion in a non-denaturing neutral condition reveals the intrinsically disordered property of the disulfide-reduced recombinant mouse prion protein.

In prion diseases, the normal prion protein is transformed by an unknown mechanism from a mainly α-helical structure to a β-sheet-rich, disease-related isomer. In this study, we surprisingly found that a slow, spontaneous α-to-coil-to-β transition could be monitored by circular dichroism spectroscopy in one full-length mouse recombinant prion mutant protein, denoted S132C/N181C, in which the endogenous cysteines C179 and C214 were replaced by Ala and S132 and N181 were replaced by Cys, during incubation in a non-denaturing neutral buffer. No denaturant was required to destabilize the native state for the conversion.