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  • Author or Editor: N. Li x
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Abstract

Gingipains, a group of arginine or lysine specific cysteine proteinases (also known as RgpA, RgpB and Kgp), have been recognized as major virulence factors in Porphyromonas gingivalis. This bacterium is one of a handful of pathogens that cause chronic periodontitis. Gingipains are involved in adherence to and colonization of epithelial cells, hemagglutination and hemolysis of erythrocytes, disruption and manipulation of the inflammatory response, and the degradation of host proteins and tissues. RgpA and Kgp are multi-domain proteins composed of catalytic domains and hemagglutinin/adhesin (HA) regions. The structure of the HA regions have previously been defined by a gingipain domain structure hypothesis which is a set of putative domain boundaries derived from the sequences of fragments of these proteins extracted from the cell surface. However, multiple sequence alignments and hidden Markov models predict an alternative domain architecture for the HA regions of gingipains. In this alternate model, two or three repeats of the socalled “cleaved adhesion” domains (and one other undefined domain in some strains) are the modules which constitute the substructure of the HA regions. Recombinant forms of these putative cleaved adhesin domains are indeed stable folded protein modules and recently determined crystal structures support the hypothesis of a modular organisation of the HA region. Based on the observed K2 and K3 structures as well as multiple sequence alignments, it is proposed that all the cleaved adhesin domains in gingipains will share the same β-sandwich jelly roll fold. The new domain model of the structure for gingipains and the Hag proteins of P. gingivalis will guide future functional studies of these virulence factors.

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Abstract  

A new complex, diaquadi(1,2,4-triazol-5-one)zinc(II) ion nitrate formulated as {[Zn(TO)2(H2O)2](NO3)2}n (1) (1,2,4-triazole-5-one, abbreviated as: TO) was synthesized and characterized by elemental analysis, X-ray single crystal diffraction, infrared spectrum (IR), differential scanning calorimetry (DSC), thermogravimetric analysis and differential thermogravimetric analysis (TG-DTG). The X-ray structure analysis reveals that the complex is orthorhombic with space group Pbca and unit-cell parameters a=6.9504(2) �; b=10.6473(3) �; c=17.8555(5) �. Based on the result of thermal analysis, the thermal decomposition process of the compound was derived. From measurement of the enthalpy of solution in water in 298.15 K, the standard molar enthalpy of solution of lignand TO and the complex were determined as 15.43�0.18 and 52.64�0.42 kJ mol−1, respectively. In addition, the standard molar enthalpy of formation of TO(aq) was calculated as −126.97�0.72 kJ mol−1.

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A micellar high-performance liquid chromatography (HPLC) method has been described for simultaneous determination of ephedrine, pseudoephedrine, and methylephedrine in Ephedra Herb and two traditional Chinese preparations. The separation and determination of ephedrine, pseudoephedrine, and methylephedrine were performed using a mobile phase containing 1.75 × 10−1 mol·L−1 sodium dodecyl sulphate and 0.02 mol·L−1 potassium hydrogen phosphate with 10% (v/v) methanol at pH 3.0, running at 1.5 mL·min−1 by a Venusil XBP C18 (250 × 4.6 mm, 5 μm) column at 40 °C. The detected wavelength was set at 210 nm. The method was validated according to the International Conference on Harmonization of Technical Requirements for Registration of Pharmaceuticals for Human Use (ICH) guidelines. The main analytical parameters were linearity (r > 0.9990), intra- and inter-day precisions (relative standard deviation [RSD %], 0.33–1.63, and RSD %, 1.26–2.20, respectively), limit of quantifications [LOQs], and limit of detections [LODs] (2.6 × 10−4 and 7.8 × 10−5 mg·mL−1 for ephedrine, 6.8 × 10−4 and 2.0 × 10−4 mg·mL−1 for pseudoephedrine, and 5.0 × 10−4 and 1.5 × 10−4 mg·mL−1 for methylephedrine). RSDs of recoveries were <5.5% in the three samples. Based on the optimized chromatographic conditions and the eluted orders, a model of separation mechanism for the analytes was established. The results indicated that the proposed method was an accurate, “green” and cheap method.

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Abstract  

Thermal analysis of phenylethynyl end-capped imide oligomer AFR-PEPA-4 was performed to characterize cure reaction, thermal stabilities and semicrystalline behavior of AFR-PEPA-4 oligomer and its cured polyimide. Cured AFR-PEPA-4 polyimide showed high T gs up to 418C. Both AFR-PEPA-4 oligomer and polyimide exhibit excellent thermal stabilities comparable to PETI-5 polyimides. AFR-PEPA-4 imide oligomer has a T m of 330C and exhibits spherulite crystalline morphology in the film. The crystallinity in AFR-PEPA-4 films could not be regenerated under any annealing conditions after the initial melt.

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Abstract

The crystal structure of the K1 domain, an adhesin module of the lysine gingipain (Kgp) expressed on the cell surface by the periodontopathic anaerobic bacterium, Porphyromonas gingivalis W83, is compared to the previously determined structures of homologues K2 and K3, all three being representative members of the cleaved adhesin domain family. In the structure of K1, the conformation of the most extensive surface loop is unexpectedly perturbed, perhaps by crystal packing, and is displaced from a previously reported arginine-anchored position observed in K2 and K3. This displacement allows the loop to become free to interact with other proteins; the alternate flipped-out loop conformation is a novel mechanism for interacting with target host proteins, other bacteria, or other gingipain protein domains. Further, the K1 adhesin module, like others, is found to be haemolytic in vitro, and so, functions in erythrocyte recognition thereby contributing to the haemolytic function of Kgp. K1 was also observed to selectively bind to haem-albumin with high affinity, suggesting this domain may be involved in gingipain-mediated haem acquisition from haem-albumin. Therefore, it is most likely that all cleaved adhesin domains of Kgp contribute to the pathogenicity of P. gingivalis in more complex ways than simply mediating bacterial adherence.

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The aim of this study was to investigate the effects of maternal lead exposure on the learning and memory ability and expression of tau protein phosphorylation (P-tau) and beta amyloid protein (Aβ) in hippocampus of mice offspring. Pb exposure initiated from beginning of gestation to weaning. Pb acetate administered in drinking solutions was dissolved in distilled deionized water at the concentrations of 0.1%, 0.5% and 1% groups. On the 21 th of postnatal day, the learning and memory ability of the mouse pups was tested by Water Maze test and the Pb levels in blood and hippocampus of the offspring were also determined. The expression of P-tau and Aβ in hippocampus was measured by immunohistochemistry and Western blotting. The Pb levels in blood and hippocampus of all exposure groups were significantly higher than that of the control group ( P < 0.05). In Water Maze test, the performances of 0.5% and 1% groups were worse than that of the control group ( P < 0.05). The expression of P-tau and Aβ was increased in Pb exposed groups than that of the control group ( P < 0.05). Tau hyper-phosphorylation and Aβ increase in the hippocampus of pups may contribute to the impairment of learning and memory associated with maternal Pb exposure.

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Abstract  

A ternary binuclear complex of dysprosium chloride hexahydrate with m-nitrobenzoic acid and 1,10-phenanthroline, [Dy(m-NBA)3phen]2·4H2O (m-NBA: m-nitrobenzoate; phen: 1,10-phenanthroline) was synthesized. The dissolution enthalpies of [2phen·H2O(s)], [6m-HNBA(s)], [2DyCl3·6H2O(s)], and [Dy(m-NBA)3phen]2·4H2O(s) in the calorimetric solvent (VDMSO:VMeOH = 3:2) were determined by the solution–reaction isoperibol calorimeter at 298.15 K to be
\documentclass{aastex} \usepackage{amsbsy} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{bm} \usepackage{mathrsfs} \usepackage{pifont} \usepackage{stmaryrd} \usepackage{textcomp} \usepackage{upgreek} \usepackage{portland,xspace} \usepackage{amsmath,amsxtra} \pagestyle{empty} \DeclareMathSizes{10}{9}{7}{6} \begin{document} $$\Updelta_{\text{s}} H_{\text{m}}^{\theta }$$ \end{document}
[2phen·H2O(s), 298.15 K] = 21.7367 ± 0.3150 kJ·mol−1,
\documentclass{aastex} \usepackage{amsbsy} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{bm} \usepackage{mathrsfs} \usepackage{pifont} \usepackage{stmaryrd} \usepackage{textcomp} \usepackage{upgreek} \usepackage{portland,xspace} \usepackage{amsmath,amsxtra} \pagestyle{empty} \DeclareMathSizes{10}{9}{7}{6} \begin{document} $$\Updelta_{\text{s}} H_{\text{m}}^{\theta }$$ \end{document}
[6m-HNBA(s), 298.15 K] = 15.3635 ± 0.2235 kJ·mol−1,
\documentclass{aastex} \usepackage{amsbsy} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{bm} \usepackage{mathrsfs} \usepackage{pifont} \usepackage{stmaryrd} \usepackage{textcomp} \usepackage{upgreek} \usepackage{portland,xspace} \usepackage{amsmath,amsxtra} \pagestyle{empty} \DeclareMathSizes{10}{9}{7}{6} \begin{document} $$\Updelta_{\text{s}} H_{\text{m}}^{\theta }$$ \end{document}
[2DyCl3·6H2O(s), 298.15 K] = −203.5331 ± 0.2200 kJ·mol−1, and
\documentclass{aastex} \usepackage{amsbsy} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{bm} \usepackage{mathrsfs} \usepackage{pifont} \usepackage{stmaryrd} \usepackage{textcomp} \usepackage{upgreek} \usepackage{portland,xspace} \usepackage{amsmath,amsxtra} \pagestyle{empty} \DeclareMathSizes{10}{9}{7}{6} \begin{document} $$\Updelta_{\text{s}} H_{\text{m}}^{\theta }$$ \end{document}
[[Dy(m-NBA)3phen]2·4H2O(s), 298.15 K] = 53.5965 ± 0.2367 kJ·mol−1, respectively. The enthalpy change of the reaction was determined to be
\documentclass{aastex} \usepackage{amsbsy} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{bm} \usepackage{mathrsfs} \usepackage{pifont} \usepackage{stmaryrd} \usepackage{textcomp} \usepackage{upgreek} \usepackage{portland,xspace} \usepackage{amsmath,amsxtra} \pagestyle{empty} \DeclareMathSizes{10}{9}{7}{6} \begin{document} $$\Updelta_{\text{r}} H_{\text{m}}^{\theta } = 3 6 9. 4 9 \pm 0. 5 6 \;{\text{kJ}}\cdot {\text{mol}}^{ - 1} .$$ \end{document}
According to the above results and the relevant data in the literature, through Hess’ law, the standard molar enthalpy of formation of [Dy(m-NBA)3phen]2·4H2O(s) was estimated to be
\documentclass{aastex} \usepackage{amsbsy} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{bm} \usepackage{mathrsfs} \usepackage{pifont} \usepackage{stmaryrd} \usepackage{textcomp} \usepackage{upgreek} \usepackage{portland,xspace} \usepackage{amsmath,amsxtra} \pagestyle{empty} \DeclareMathSizes{10}{9}{7}{6} \begin{document} $$\Updelta_{\text{f}} H_{\text{m}}^{\theta }$$ \end{document}
[[Dy(m-NBA)3phen]2·4H2O(s), 298.15 K] = −5525 ± 6 kJ·mol−1.
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Abstract

Renal injury is reported to have a high mortality rate. Additionally, there are several limitations to current conventional treatments that are used to manage it. This study evaluated the protective effect of hesperidin against ischemia/reperfusion (I/R)-induced kidney injury in rats. Renal injury was induced by generating I/R in kidney tissues. Rats were then treated with hesperidin at a dose of 10 or 20 mg/kg intravenously 1 day after surgery for a period of 14 days. The effect of hesperidin on renal function, serum mediators of inflammation, and levels of oxidative stress in renal tissues were observed in rat kidney tissues after I/R-induced kidney injury. Moreover, protein expression and mRNA expression in kidney tissues were determined using Western blotting and RT-PCR. Hematoxylin and eosin (H&E) staining was done for histopathological observation of kidney tissues. The data suggest that the levels of blood urea nitrogen (BUN) and creatinine in the serum of hesperidin-treated rats were lower than in the I/R group. Treatment with hesperidin also ameliorated the altered level of inflammatory mediators and oxidative stress in I/R-induced renal-injured rats. The expression of p-IκBα, caspase-3, NF-κB p65, Toll-like receptor 4 (TLR-4) protein, TLR-4 mRNA, and inducible nitric oxide synthase (iNOS) was significantly reduced in the renal tissues of hesperidin-treated rats. Histopathological findings also revealed that treatment with hesperidin attenuated the renal injury in I/R kidney-injured rats. In conclusion, our results suggest that hesperidin protects against renal injury induced by I/R by involving TLR-4/NF-κB/iNOS signaling.

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Abstract  

The acidity of mesoporous materials FeSiMCM-41, LaSiMCM-41, SiMCM-41, AlSiMCM-41 and HAlSiMCM-41 has been investigated by microcalorimetric studies of the adsorption of ammonia and temperature programmed ammonia desorption method. In the initial stage, the acid strength sequence is SiMCM-41>HAlSiMCM-41>AlSiMCM-41>FeSiMCM-41>LaSiMCM-41, in agreement with that found for microporous molecular sieves materials. A small number of strong acid sites of SiMCM-41 may result from the aluminum impurity contained in the silica source material. The acid density sequence is HAlSiMCM-41>AlSiMCM-41>FeSiMCM-41>LaSiMCM-41SiMCM-41 and can be explained by the studies of existing states of trivalent atoms in these samples reported in previous work. Since some NH3-TPD plots of these samples show the profiles that could not be back to baseline at elevated temperature, the technique of microcalorimetric adsorption is preferable in studying these samples.

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Abstract  

Adsorption of carrier-free radiotracers 181W and 93mMo produced in the 181Ta(p, n) and natNb(p, n) reactions, respectively, on anion-exchange resin was studied in mixed solution of HF and HNO3 in a concentration range of 10−4–10−1 M HF/0.1 M HNO3. Distribution coefficients (K d) of 181W and 93mMo at 70 °C showed the V-shaped variation with the minimum at around 10−1 M HF/0.1 M HNO3, although variation of the K d values for 93mMo was quite small compared with that for 181W. Formation of oxofluoro complexes for W and Mo is briefly discussed.

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