The development of luminescent materials for anticounterfeiting and encryption is of great importance. Herein, we develop a multistimuli-responsive luminescent material, NaCaGeO:Pb/Er, and use it to print luminescent images. The photoluminescence and upconversion luminescence of these images show different patterns and colors under different stimuli. The photostimulated luminescence (PSL) of the printed images causes dynamic changes in appearance and is accordingly applied for dynamic multimodal anticounterfeiting on banknotes. The PSL of these luminescent images is also applied in a virtual war scenario to demonstrate that the dynamic PSL-encrypted information in the fabricated image is sufficiently safe even in extreme cases and that spies will be detected. These results can inspire us with more creative security designs based on this luminescent material.

Background: Neonatal exposure to anaesthetics such as sevoflurane has been reported to result in behavioural deficits in rodents. However, while oxidative injury is thought to play an underlying pathological role, the mechanisms of neurotoxicity remain unclear. In the present study, we investigated whether the NADPH oxidase inhibitor apocynin protects against longterm memory impairment produced by neonatal sevoflurane exposure in mice. Methods: Postnatal day six mice were divided into four groups; (1) non-anaesthesia, (2) intraperitoneal apocynin (50 mg kg

Abstract. Nitrate is often found to be associated with atmospheric particles. Surface nitrate can change the hygroscopicity of these particles, and thus impact their chemical reactivity. However, the influence of nitrate on heterogeneous reactions of atmospheric trace gases is poorly understood. In this work, the effects of nitrate on heterogeneous conversion of SO2 with hematite at 298 K are investigated using an in situ diffuse reflectance infrared Fourier transform spectroscopy (DRIFTS) and a White cell coupled with Fourier transform infrared spectroscopy (White cell-FTIR). It is found that nitrate participates in heterogeneous reactions of SO2, accelerates the formation rate of sulfate, and leads to the formation of surface-adsorbed HNO3 and gas-phase N2O and HONO. The results indicate that low to moderate amounts of nitrate significantly enhance the reactivity of hematite–nitrate mixtures, the uptake of SO2, and the formation of sulfate on hematite. For mixtures, the sample containing 24% nitrate exhibits the highest sulfate formation rate, and its corresponding uptake coefficient calculated by geometric surface area is about 5.5 times higher than that of hematite alone. The sample containing 48% nitrate presents the highest Brunauer–Emmett–Teller (BET) uptake coefficient, and the value is about 8 times higher than that of pure hematite. No uptake of SO2 and formation of sulfate are observed on pure nitrate. Evidence presented herein implies a significant contribution of the unreleased HNO3 and HONO in the particles for the conversion of SO2 and the enhanced formation of sulfate in the atmosphere. A possible mechanism for the influence of nitrate on the heterogeneous conversion of SO2 on hematite is proposed, and atmospheric implications based on these results are discussed.

We report on the design of ultraviolet (UV) emitting persistent (PersL) materials.

Partially folded protein intermediates have been observed by 19F-NMR spectroscopy during the equilibrium unfolding of the membrane-associated D-lactate dehydrogenase (D-LDH) of Escherichia coli by a denaturant, guanidine hydrochloride (Gdn.HCl). The results from 19F-NMR and circular dichroism spectroscopic studies suggest that the intermediates observed at low Gdn.HCl concentrations (< 3.5 M) exhibit features similar to "molten globules" that contain considerable amounts of secondary and tertiary structure. The results of 19F-NMR studies on 5F-Trp-labeled D-LDH, such as the chemical shift changes, nuclear Overhauser effect, and solvent-induced isotopic shift effect, show that different regions of D-LDH unfold nonuniformly in Gdn.HCl in the presence of lysophosphatidylcholine. The polypeptide appears to unfold in a general order from the carboxyl end to the amino end, in agreement with previous findings from our laboratory that the carboxyl-terminal region of D-LDH is largely exposed to the solvent while the amino-terminal region is buried in the protein core. The structure of the partially unfolded intermediate forms of D-LDH is stabilized in the presence of lipid-like detergents, such as lysophosphatidylcholine.