Cinnamaldehyde (CIN) is a promising natural preservative and generally recognized as safe for commodities as well as consumers. In this work, the antifungal effects of CIN on Aspergillus flavus were evaluated both in solid and in liquid culture conditions. Our results indicated that CIN effectively inhibited radial growth, spore production, mycelium formation, and aflatoxin B1 biosynthesis by A. flavus in a dose-dependent manner. At the concentration of 104 mg L(-1), CIN exposure was able to completely inhibit fungal growth as well as aflatoxin B1 production. Furthermore, the inhibitory activities of CIN were closely connected with the treatment period and the tested fungal species. Compared with the control strains, CIN dose dependently changed the morphology and ultrastructure of mycelium in different degree. Especially, the reduction of hydrogen peroxide was considered to follow the destruction of mitochondrial. Meanwhile, CIN significantly cut the levels of lipid peroxidation and reduced glutathione. The activity of total superoxide dismutase was significantly inhibited after CIN treatment at the end of incubation, whereas the activities of catalase and glutathione peroxidase were opposite. These results indicated that the inhibitory effect of CIN could attribute to oxidative stress alleviation possibly induced by modifications of cellular structure as well as redox status.

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Metallic phase molybdenum disulfide (1T-MoS 2 ), with its fast carrier mobility and highly abundant active sites, plays a vital role in the field of catalysis. However, the development of a simple and efficient strategy for the preparation of stabilized 1T-MoS 2 remains a great challenge. Herein, we report the spontaneous phase transformation of MoS 2 from the 2H to the 1T phase, caused by the strong metal−support interaction during iridium (Ir) adsorption. The resulting Ir/MoS 2 heterostructures show higher catalytic activity for overall water splitting than those of commercial Pt/C and IrO 2 in alkaline media. We believe that the spontaneous phase transformation of this material not only opens up a new perspective for developing advanced catalysts for alkaline water splitting but also presents an efficient and intriguing method for the phase engineering of two-dimensional materials.

Metallic 1T-phase transition metal dichalcogenides (TMDs) are of considerable interest in enhancing catalytic applications due to their abundant active sites and good conductivity. However, the unstable nature of 1T-phase TMDs greatly impedes their practical applications. Herein, we developed a new approach for the synthesis of highly stable 1T-phase Au/Pd-MoS2 nanosheets (NSs) through a metal assembly induced ultrastable phase transition for achieving a very high electrocatalytic activity in the hydrogen evolution reaction. The phase transition was evoked by a novel mechanism of lattice-mismatch-induced strain based on density functional theory (DFT) calculations. Raman spectroscopy and transmission electron microscopy (TEM) were used to confirm the phase transition on experimental grounds. A novel heterostructured 1T MoS2–Au/Pd catalyst was designed and synthesized using this mechanism, and the catalyst exhibited a 0 mV onset potential in the hydrogen evolution reaction under light illumination. Therefore, this method can potentially be used to fabricate 1T-phase TMDs with remarkably enhanced activities for different applications.

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Spike protein is one of the major structural proteins of severe acute respiratory syndrome-coronavirus. It is essential for the interaction of the virons with host cell receptors and subsequent fusion of the viral envelop with host cell membrane to allow infection. Some spike proteins of coronavirus, such as MHV, HCoV-OC43, AIBV and BcoV, are proteolytically cleaved into two subunits, S1 and S2. In contrast, TGV, FIPV and HCoV-229E are not. Many studies have shown that the cleavage of spike protein seriously affects its function. In order to investigate the maturation and proteolytic processing of the S protein of SARS CoV, we generated S1 and S2 subunit specific antibodies (Abs) as well as N, E and 3CL protein-specific Abs. Our results showed that the antibodies could efficiently and specifically bind to their corresponding proteins from E.coli expressed or lysate of SARS-CoV infected Vero-E6 cells by Western blot analysis. Furthermore, the anti-S1 and S2 Abs were proved to be capable of binding to SARS CoV under electron microscope observation. When S2 Ab was used to perform immune precipitation with lysate of SARS-CoV infected cells, a cleaved S2 fragment was detected with S2-specific mAb by Western blot analysis. The data demonstrated that the cleavage of S protein was observed in the lysate, indicating that proteolytic processing of S protein is present in host cells.

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The systems of open-ended carbon nanotubes (CNTs) immersed in methanol-water solution are studied by molecular dynamics simulations. For the (6,6) CNT, nearly pure methanol is found to preferentially occupy interior space of the CNT. Even when the mass fraction (MF) of methanol in bulk solution is as low as 1%, the methanol MF within the CNT is still more than 90%. For CNTs with larger diameters, the methanol concentrations within CNTs are also much higher than those outside CNTs. The methanol selectivity decreases with increasing CNT diameter, but not monotonically. From microscopic structural analyses, we find that the primary reason for the high selectivity of methanol by CNTs lies on high preference of methanol in the first solvation shell near the inner wall of CNT, which stems from a synergy effect of the van der Waals interaction between CNT and the methyl groups of methanol, together with the hydrogen bonding interaction among the liquid molecules. This synergy effect may be of general significance and extended to other systems, such as ethanol aqueous solution and methanol/ethanol mixture. The selective adsorption of methanol over water in CNTs may find applications in separation of water and methanol, detection of methanol, and preservation of methanol purity in fuel cells.