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Dawei Xu Li Zheng Xinhong Cheng Gang Wang Qian Wang Wenbo Xin Peiyi Ye Lingyan Shen Yuehui Yu 《Physics letters. A》2019,383(25):3134-3137
The efficient passivation of in situ NH3-plasma pre-treatment and its regulation of the band alignment between HfO2 and 4H-SiC have been investigated by XPS. With in situ NH3-plasma passivation by PEALD, a VBO of 0.72 eV and a CBO of 1.54 eV can be obtained across the HfO2/4H-SiC interface. The Si-O bonds components reduction in the passivated interface layers will lead to band bending or band shift at the interface and regulate the band alignments between HfO2 and 4H-SiC. The physical mechanism investigation of band alignments can be a cornerstone for the application of HfO2/4H-SiC heterojunctions in the high-power devices. 相似文献
945.
Hang Yin Qian Cheng Roselyne Rosas Prof. Stéphane Viel Dr. Valérie Monnier Prof. Laurence Charles Prof. Didier Siri Dr. Didier Gigmes Dr. Olivier Ouari Prof. Ruibing Wang Dr. Anthony Kermagoret Dr. David Bardelang 《Chemistry (Weinheim an der Bergstrasse, Germany)》2019,25(54):12552-12559
A viologen derivative carrying a benzimidazole group ( V-P-I 2+; viologen–phenylene–imidazole V-P-I ) can be dimerized in water using cucurbit[8]uril (CB[8]) in the form of a 2:2 complex resulting in a negative shift of the guest pKa, by more than 1 pH unit, contrasting with the positive pKa shift usually observed for CB-based complexes. Whereas 2:2 complex protonation is unclear by NMR, silver cations have been used for probing the accessibility of the imidazole groups of the 2:2 complexes. The protonation capacity of the buried imidazole groups is reduced, suggesting that CB[8] could trigger proton release upon 2:2 complex formation. The addition of CB[8] to a solution containing V-P- I 3+ indeed released protons as monitored by pH-metry and visualized by a coloured indicator. This property was used to induce a host/guest swapping, accompanied by a proton transfer, between V-P-I 3+ ⋅ CB[7] and a CB[8] complex of 1-methyl-4-(4-pyridyl)pyridinium. The origin of this negative pKa shift is proposed to stand in an ideal charge state, and in the position of the two pH-responsive fragments inside the two CB[8] which, alike residues engulfed in proteins, favour the deprotonated form of the guest molecules. Such proton release triggered by a recognition event is reminiscent of several biological processes and may open new avenues toward bioinspired enzyme mimics catalyzing proton transfer or chemical reactions. 相似文献
946.
The aim of this work was to further investigate the anticancer potential of Juglans mandshurica Maxim, including the separation of active constituents and their anti-proliferative effects with underlying mechanism of action. Five alkaloids (1–5) were isolated from the bark of J. mandshurica. Among them, 1 showed the highest cytotoxic activities against Hep3B and HepG2 cells with an IC50 values of 61.80 and 56.24 μM, respectively. Therefore, the cellular mechanism involved 1 was subsequently studied. Our results showed that 1 markedly caused apoptosis and autophagy, but without cell cycle arrest in HepG2 cells. Interestingly, only autophagic cell death was induced in 1-treated Hep3B cells. It is concluded that the isolated alkaloids exerted a certain anti-hepatoma potential, and our results may provide a basis for the further investigation of the alkaloids extracted from J. mandshurica. 相似文献
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The extent to which drugs combine with trypsin is influenced by the interaction of tartrazine and trypsin, which may cause overdose or underdose of drugs. Therefore, the interaction of tartrazine and trypsin is investigated by methods of spectrometry in this paper. The binding rate of tartrazine to trypsin is 80.95–95.71% at 310?K, and Hill’s coefficients are almost 1. The effect of tartrazine on trypsin structure was studied by synchronous and circular dichroism. The results showed that the binding of tartrazine and trypsin induced the conformational change of trypsin, and quenched the endogenous fluorescence in trypsin. The results of molecular docking revealed that tartrazine is located in the catalytic active site of trypsin, and is consistent with that of experimental calculation. 相似文献
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