05 (1.00 to 4.18) 0.04 Osteoarthritisa contralateral (n, %) 61/349 (18%) 8/110 (7%) 2.40 (1.19 to 4.87) 0.01 MJS contralateral (mean, SD) 3.55 (0.95) 3.74 (0.87) −0.20 (−0.39 to 0.00) 0.06 aOsteoarthritis is defined as either an MJS ≤2.5 mm or a K&L grade II EPZ015666 clinical trial or higher or previous surgery for osteoarthritis (total hip replacement) Table 2 Osteoarthritis measured by MJS and/or K&L in the case group comparing femoral neck fractures and trochanteric fractures   Cases, femoral neck fractures Cases, trochanteric fractures

Mean difference or RR with 95% confidence interval p MJS ≤2.5 mm ipsilateral (n, %) 8/96 (8%) 23/154 (15%) 0.56 (0.26 to 1.19) 0.12 K&L grade II or higher ipsilateral (n, %) 10/96 (10%) 30/154 (20%) 0.54 (0.27 to 1.04) 0.06 Osteoarthritisa ipsilateral (n, %) 14/96 (15%) 34/154 (22%) 0.66 (0.37 to 1.17) 0.14 MJS ipsilateral (mean, SD) 3.72 (0.90) 3.42 (1.03) 0.30 (0.05 to 0.55) 0.02 MJS ≤2.5 contralateral, mm (n,%) 15/177 (9%) 27/172 (16%) 0.54 (0.30 to 0.98) 0.04 K&L grade II or higher contralateral (n, %) 25/177 (14%) 27/172 (16%) 0.90 (0.55 to 1.49) 0.68 Osteoarthritisa

contralateral (n, %) 26/177 (15%) 35/172 (20%) 0.72 (0.46 to 1.15) 0.16 MJS contralateral (mean, SD) 3.62 (0.97) 3.47 (0.91) 0.14 (−0.06 to 0.34) 0.16 aOsteoarthritis is defined as either an MJS ≤2.5 mm or a K&L grade II or higher or previous surgery for osteoarthritis (total hip replacement) When comparing OA as defined by MJS and K&L, the Pearson correlation coefficient was r = 0.67 (p < 0.01) on the injured selleckchem side and r = 0.72 (p < 0.001) on Vildagliptin the non-injured side. The Pearson correlation coefficient of the overall OA between the injured and non-injured side was 0.24 (p < 0.001). Six patients in the fracture group, all with trochanteric fractures, and five patients in the contusion group,

had bilateral osteoarthritis. Three patients in the contusion group had osteoarthritis only on the non-injured side. Discussion In this study, we did not find a difference in the prevalence of OA on the injured side in patients with hip fractures compared to patients with hip contusion. Hence, we found no support for the theory that OA may protect against a hip fracture. The relative risk was close to 1 with narrow confidence intervals for all comparisons, and the difference in mean MJS was very close to 0 (Table 1). The relationship between OA and osteoporotic proximal femoral fractures is of special relevance to the ageing population because both conditions are common and both increase with age. It is of particular interest to investigate OA in the hip because it is often the only affected joint, suggesting that local biomechanical risk factors are important [21]. In this model, the fracture group represent patients with osteoporotic fractures and the contusion group represents patients with less osteoporosis, as their hip did tolerate a fall without fracturing.

One of the genes up-regulated at late-log growth phase was the locus BMEI0402. Veliparib cell line The product of this gene has not yet been characterized in B. melitensis;

however, it has high homology (63% sequence identity) to an immunogenic outer membrane protein, Omp31 (BMEII0844) [37]. Omp31 is a haemin-binding protein [38], which binds to, and extracts iron from, the host. Iron has been identified as a required element for epithelial invasion in microbial pathogens [39–41], and the expression of this locus, along with other iron-related genes in late-log phase cultures (BMEI0176–0177, BMEII0536, BMEII0567, BMEII0583, BMEII0704, BMEII0883, BMEII1120, BMEII1122), may influence the internalization ability of brucellae. SP41 is another surface-exposed outer membrane protein with a critical role in Brucella suis adherence to, and invasion of, non-phagocytic cells [13]. The role of this protein, which is encoded by the ugpB gene (BMEII0625) present in the chromosome

II of B. melitensis 16 M genome, was not previously described for B. melitensis adhesion to and/or penetration of epithelial cells. The transcript from the ugpB gene was not identified as differentially expressed in our cDNA microarray analysis between the most and the least invasive cultures. Therefore, under our experimental Ro 61-8048 cost conditions, this OMP seems not to be involved in the higher invasiveness of the late-log phase cultures. It is possible that the composition of the cell culture medium does not induce the expression of ugpB, or it is also possible that ugpB is constitutively expressed and/or act in concert with other factors. Although genetic analysis reveals that ugpB may belong to an operon (BMEII0621 to II0625) that encodes for a sn-glycerol-3-phosphate ABC transporter [42], the experimental evidence does not support this hypothesis. A previous study showed that

the product of ugpB in B. suis is indeed a surface-exposed protein with adhesion and invasion activity [13]. In fact, in this study, three of the transcripts predicted to encode the transport system [ugpC (BMEII00621) (ATP-binding thiprotein), ugpE (BMEII0622) and ugpA (BMEII0624) (permease proteins)] were highly up-regulated (> 50 fold) in late-log phase cultures, when compared to stationary Bay 11-7085 phase cultures. In concordance with previous experimental evidence, our microarray data would support the finding of others that ugpB does not belong to an operon that encodes for a sn-glycerol-3-phosphate ABC transporter. In addition, our results support growth-phase regulation of the sn-glycerol-3-phosphate ABC transport system, which has been implicated in Brucella pathogenesis [24, 43]. The ability of Brucella to invade host cells is linked to its OM properties. B. melitensis OMP profile changes during culture growth [44], as gene expression is transcriptional regulated by environmental conditions [12, 45].

“
“Introduction The glutamatergic system is an attractive molecular target for pharmacological intervention (Kaczor and Matosiuk, 2010). Ligands acting on ionotropic glutamate receptors (iGluRs: NMDA, AMPA, and kainate receptors) or

metabotropic glutamate receptors (mGluRs) are potential drug candidates for the treatment of neurodegenerative diseases (Alzheimer’s disease, Parkinson’s disease, Huntington’s disease), epilepsy, as well as schizophrenia, anxiety, and memory disorders (Kew and Kemp, 2005). Although only a few glutamate receptor ligands have turned out to be clinically useful (firstly, because of the crucial role of the glutamatergic system in many physiological processes, and secondly, due to the unfavorable psychotropic side effects, traditionally linked with high-affinity NMDA receptor antagonists), ligands of kainate receptors seem to be especially promising. Kainate receptors are involved www.selleckchem.com/products/Trichostatin-A.html in epileptogenesis and inducing synaptic plasticity, mainly via the mossy fiber long-term potentiation mechanism. Thus, antagonists of kainate receptors are potential anti-seizure and neuroprotective agents. Moreover, non-competitive antagonists of AMPA receptors are well tolerated in preclinical and clinical studies (Szénási et al., 2008),

thus it may be expected that this will also be the case for such ligands of kainate Selonsertib concentration receptors. Research on non-competitive antagonists Interleukin-2 receptor of kainate receptors is hindered by the fact that only three series of such compounds have been obtained up to now (Kaczor et al., 2012; Valgeirsson et al., 2003, 2004). Recently, we have reported 1,2,3,5-tetrasubstituted

indole derivatives which are among the most active non-competitive antagonists of the GluK1 receptor and are the first known such ligands of the GluK2 receptor, Fig. 1 (Kaczor et al., 2012). We have also suggested a binding site for them in the receptor transduction domain (Kaczor et al., 2014) which was enabled by the construction of whole receptor models (Kaczor et al., 2008, 2009, 2014). Here we present further modifications, 2–7, of the lead compound E099-25011, (1-ethyl-5-methoxy-2-(4-methoxyphenyl)-3-methylindole), 1. The lead compound was identified by searching the internal databases of compounds at the Elbion Institute, Radebul, Germany. 1 is an analog of Zindoxifene, an anti-estrogen, tumor-inhibiting compound (Schneider et al., 1991). We have previously optimized compound 1 by changing substituents in positions 1, 2, 3, and 5 of the indole system (Fig. 1) (Kaczor et al., 2012, 2014). Compounds 3 and 5–7 were tested for their affinity to the GluK2 receptor, and compounds 3 and 5 were found to be non-competitive antagonists at this receptor. Furthermore, we show how novel non-competitive antagonists 3 and 5 of the GluK2 receptor interact with the transduction domain of the previously constructed homology model of this receptor (Kaczor et al., 2014). Fig.

The antibiotics were serially diluted in 1 mL of M79 medium at concentrations from 256 μg/mL to 0.5 μg/mL. An overnight culture of A. amazonense was diluted to 4 × 104 cells/mL. One milliliter of this dilution was added to one milliliter of M79 medium containing the appropriate antibiotic concentration. The cells were cultivated in a rotary shaker at 150 rpm for 40 h at 35°C. Conjugation Conjugation was basically carried out as described by Clerico et al. (2007) [42]. However, some modifications were made as follows: overnight cultures of A. amazonense Y2 (receptor), E. coli XL1-Blue containing the plasmid pRK2013 (helper), and E. coli XL1-Blue containing the appropriate plasmid (donor) were used.

Approximately 1 mL of the A. amazonense culture with an OD600 = 2 (1.3 × 109 cfu/ml) was mixed with 1 mL of each helper and donor cultures with an OD600 = 0.2 (2 × 108 cfu/mL) LCZ696 in vivo (ratio 10:1:1), unless stated otherwise. This mixture was harvested by centrifugation at 6000 g for 2 min and then resuspended in 100 μL of MLB medium (LB and M79 mixture at a proportion of 8:2), and this volume was then spotted onto MLB agar and incubated for 20 h at 35°C. Following this, the cell mass

was resuspended in 200 μL of M79 medium and plated on M79 medium containing the appropriate antibiotic. Electroporation The preparation of cells was based on the protocol described by Schultheiss and Schüler (2003) [27]. A 3 mL GDC-0941 in vitro overnight culture of A. amazonense was inoculated in 250 mL of M79 and the cells were cultivated to an OD600 of ~0.12 (early-log growth phase), unless stated otherwise. From this point, all manipulations were conducted on ice. The cells were incubated in ice for 30 min and then harvested by Branched chain aminotransferase centrifugation at 5000 g for 20 min at 10°C. The cells were resuspended in 100 mL of electroporation buffer (pH 6.5 HEPES 1 mM, MgCl2 1 mM, and sucrose 200 mM) and again harvested by centrifugation (20 min at 5000 g). Subsequently, the cells were resuspended in 40 mL of electroporation buffer and again harvested by centrifugation. At the end, the cells were resuspended

in 250 μL of electroporation buffer (final concentration of ~1010 cfu/mL), distributed in aliquots of 40 μL, and frozen in liquid nitrogen. Cell electroporation was carried out as follows: the 40 μL aliquot was mixed with 50 ng of the pHRGFPGUS vector and electroporated through a Gene Pulser apparatus (Bio-Rad Laboratories Inc.) with 12.5 kV/cm, 25 μF and 200 Ω, unless stated otherwise. After electrical discharge, the cells were resuspended in 500 μL of M79 medium and incubated at 35°C for 3 h in a rotary shaker at 150 rpm. Subsequently, the cells were plated on solid M79 medium containing 20 μg/mL of kanamycin and incubated for 2 days at 35°C. Gene mutagenesis Site-directed mutagenesis was based on a protocol described by Eggeling and Reyes (2005) [43].

However, nothing is known about metabolites of the tryptophan catabolism on DC function. CD14+ cells were isolated from periperal blood and activated to fully mature DC in vitro. In parallel cultures, DCs were generated in the presence of different concentrations of kynurenine and quinolinic acid. These mature DC were used to analyse expression of differentiation markers by FACS, to stimmulate naïve T-cells to proliferation, and to induce Th-1 T-cell LY3039478 price response. Kynurenine, but not quinolinic acid, had a dramatic effect on the expression of the DC maturation marker CD83, suggesting that kynurenine has an impact on DC maturation.

The expression of MHC-class I molecules, the co-stimulatory receptors CD80/CD86 and CCR7 on DC was not affected by kynurenine or quinolinic acid. In further analysis we found that kynurenine treated DC dramatically decrease the ability of T-cells to produce INF-gamma a key cytokine indicating a Th-1 immune response. Subsequently T-cell subpopulations were analysed and found that the portion of CD4+CD25+ T-cells was significantly increased in the T-cell population generated by kynurenine treated DC, which indicate an increase in a suppressor Thiazovivin cell line T-cell population. In summary, these data suggest that kynurenine “primed” mDC induce generation of suppressor T-cells. Based on the data

presented above we hypothesize that metabolites of the kynurenine pathway are important determinants in turning the immune system especially DC to a tolerogenic phenotype. Poster No. 54 Impact of Hypoxia on Furin Trafficking and the Formation of Invadopodia Dominique Arsenault 1 , Sébastien GrandMont1, Martine Charbonneau1, Kelly Harper1, Claire M. Dubois1 1 Department of Pediatric, Immunology Division, Université de Sherbrooke, Sherbrooke,

QC, Canada Recent studies indicate that tumoral invasion and metastasis, triggered by the hypoxic microenvironment, involves strategic relocalization of convertases, adhesion molecules, and metalloproteases. We used the highly invasive human Reverse transcriptase fibrosarcoma cells HT-1080, stably transfected with eGFP-tagged-furin in order to study the impact of hypoxia on the cellular localization of the convertase furin. Our results indicate that in hypoxic cells, furin is relocalized at the plasma membrane and is internalized via both clathrin- and caveolin/raft dependent endocytosis. Using furin trafficking mutants, we demonstrate that filamin-A, a cytoskeletal tethering protein, is essential for the membrane localization of furin under hypoxia. We further demonstrate that in hypoxic cells, furin and its substrate MT1-MMP relocalize to specific pericellular compartments and this relocalisation is associated with an increased cell ability to convert pro-MT1-MMP into its active form.

A crosslinked SAM of 5,5′-bis (mercaptomethyl)-2,2′-bipyridine-Ni2+ (BPD-Ni2+) has been prepared on top of the pre-patterned Au bottom contacts. Then the top Au contacts were evaporated. A two-electrode probe station

was used to assess the fidelity of the molecular junctions. Additionally, to elucidate the molecular transport in the device junctions, temperature-dependent I-V examinations were performed. Methods Fabrication of the crossbar molecular devices Fabrication of the bottom electrode Lithography of bottom electrodes was accomplished by starting with a clean single-side polished SiO2 substrate. Photoresist TPCA-1 mw PMMA 950 was spin-coated on SiO2 at 2,000 rpm for 90 s and baked at 180°C for 3 min (Figure 1a). Then, to avoid the charge-up of PMMA, 15 nm of conductive polymer (ESPACER 300Z; Showa Denko K.K., Minato, Tokyo, Japan) was spin-coating on the top of the PMMA at 2,000 rpm for 60 s. RO4929097 The

100-nm bar patterns were fabricated using an electron beam lithography system (50 kV, 100 mC/cm2; Elionix Co. Ltd., Hachioji, Tokyo, Japan). The resist was developed in MIBK methyl isobutyl ketone + IPA isopropanol 1:3 solution (MIBK-IPA) for 30 to 40 s to remove the irradiated zones and to form a pattern for the bottom electrode bars (Figure 1b). Finally, using electron-beam deposition, 10 nm of titanium and 150 nm of gold were deposited on the photoresist-patterned wafer. The wafer was immersed in acetone to remove the photoresist and the excess metal which adhered on the resist (Figure 1c). Figure 1 Scheme process flow for fabrication of crossbar molecular devices. (a) Photoresist patterning for bottom contacts on SiO2. (b) The 100-nm bar patterns were created

using electron beam lithography. (c) Deposition of 10 nm of Ti and 150-nm Au over patterned substrate and lift-off excess Au with photoresist removal. (d) Deposition of SAM over the entire substrate. (e) Preparation and deposition of top electrodes. Preparation of the crosslinked BPD-Ni2+ SAM The SAM of BPD films was fabricated in the following manner: 5,5′-bis(mercaptomethyl)-2,2′-bipyridine was purchased from Aldrich and used as received. The SAM of 5,5′-bismercaptomethyl-2,2′-bipyridine (BPD) was prepared by Carnitine palmitoyltransferase II immersing the bottom electrodes in freshly prepared 1-mM solution of n-hexane for 1 h at 60°C. Solutions were well-degassed using Ar. All preparation steps were performed in the absence of ambient light, which is the same as the process in our previous studies [4, 6]. Subsequently, the bottom gold bar was modified with a layer of BPD and immersed for 3 h in a 50-mM aqueous solution of NiCl2 (see Figure 2a,b). Figure 2 Preparation of the cross-linked BPD-Ni 2+ SAM. (a) Preparation of the BPD SAM. (b) Encapsulation of Ni on the BPD SAM. (c) A BPD-Ni system was employed as a negative resist for e-beam lithography. Microscope image of etched BPD-Ni/Au template, preliminary patterned by electrons in proximity printing geometry using a metal mesh as mask.

Microbiology 2000,146(Pt 12):3217–3226.PubMed 10. Zhang S,

Adams LG, Nunes J, Khare S, Tsolis RM, Baumler AJ: Secreted effector proteins of Salmonella enterica serotype typhimurium elicit host-specific chemokine profiles in animal models of typhoid fever and enterocolitis. Infect Immun 2003, 71:4795–4803.PubMedCrossRef 11. Wigley P, Hulme S, Powers C, Beal R, Smith A, Barrow P: Oral infection with the Salmonella enterica serovar Gallinarum 9R attenuated live vaccine as a model to characterise immunity to fowl typhoid in the chicken. BMC Vet Res 2005, 1:2.PubMedCrossRef 12. Geddes K, Cruz F, Heffron F: Analysis of cells targeted by Salmonella type III secretion in vivo. PLoS Pathog 2007, 3:e196.PubMedCrossRef 13. Hersh D, Monack DM, Smith MR, Ghori N, Falkow S, LY2835219 cost Zychlinsky A: The Salmonella invasin SipB induces macrophage apoptosis by binding to caspase-1. Proc Natl Acad Sci USA 1999, 96:2396–2401.PubMedCrossRef

14. Lundberg U, Vinatzer U, Berdnik D, von Gabain A, Baccarini M: Growth phase-regulated induction of Salmonella -induced macrophage apoptosis correlates with transient expression of SPI-1 genes. J Bacteriol 1999, 181:3433–3437.PubMed 15. Halici S, Zenk SF, Jantsch J, Hensel M: Functional analysis of the Salmonella pathogenicity island 2-mediated inhibition of antigen presentation in dendritic cells. Infect Immun 2008, 76:4924–4933.PubMedCrossRef 16. Kirby AC, Yrlid U, Wick MJ: The innate immune response differs check details in primary and secondary Salmonella infection. J Immunol 2002, 169:4450–4459.PubMed PLEK2 17. Hensel M, Shea JE, Waterman SR, Mundy R, Nikolaus T, Banks G, Vazquez-Torres A, Gleeson C, Fang FC, Holden DW: Genes encoding putative effector proteins of the type III secretion system of Salmonella

pathogenicity island 2 are required for bacterial virulence and proliferation in macrophages. Mol Microbiol 1998, 30:163–174.PubMedCrossRef 18. Murray RA, Lee CA: Invasion genes are not required for Salmonella enterica serovar typhimurium to breach the intestinal epithelium: evidence that Salmonella pathogenicity island 1 has alternative functions during infection. Infect Immun 2000, 68:5050–5055.PubMedCrossRef 19. Jiang X, Rossanese OW, Brown NF, Kujat-Choy S, Galan JE, Finlay BB, Brumell JH: The related effector proteins SopD and SopD2 from Salmonella enterica serovar Typhimurium contribute to virulence during systemic infection of mice. Mol Microbiol 2004, 54:1186–1198.PubMedCrossRef 20. Pfeifer CG, Marcus SL, Steele-Mortimer O, Knodler LA, Finlay BB: Salmonella typhimurium virulence genes are induced upon bacterial invasion into phagocytic and nonphagocytic cells. Infect Immun 1999, 67:5690–5698.PubMed 21. Kaniga K, Trollinger D, Galan JE: Identification of two targets of the type III protein secretion system encoded by the inv and spa loci of Salmonella typhimurium that have homology to the Shigella IpaD and IpaA proteins. J Bacteriol 1995, 177:7078–7085.PubMed 22.

5 g/L YE broth at 1.9 ml/min (residence time 185 m). A diagram of

the CDC reactor system as it was used for this study is available from the manufacturer at http://​www.​biosurfacetechno​logies.​com. After 24 h of culture under these conditions, one coupon holders was again replaced HSP990 order aseptically, and examined by epifluorescence microscopy. After 48 h of continuous culture, all remaining biofilm coupons were removed and examined by epifluorescence microscopy. Viability Staining The biofilms on disks in batch culture were examined by epifluorescence microscopy using the BacLight viability staining kit (L-7012, Invitrogen). Staining was performed by covering the inward face of the glass coupon in the stain mix in a sterile 12 well plate, and washing with sterile water after the appropriate time. Five minutes with a

concentrated stain mix (1.5 μl of each stain per ml) was found to be sufficient. Stained glass coupons were mounted on cleaned glass slides, and observed by epifluorescence microscopy using an Axioplan 2 microscope (Carl Zeiss, NY) equipped with appropriate filter sets (41002, 41017, Chroma Technologies), and an Xcite-120 illuminator (Exfo Life Sciences, Ontario, Canada). Images were captured using an SBIG 1402-XME (Santa Barbara Instruments, Santa Barbara, CA mounted on a 1× NU7026 ic50 c-mount adapter, with a 0.2 second exposure. The monochrome images were captured using the CCDops software supplied with the camera. Captured images were merged using ImageJ http://​rsb.​info.​nih.​gov/​ij/​. The camera ccd was cooled maximally for all fluorescence imaging (20°C below ambient). Whole image contrast and brightness enhancement was used to optimize for publication only. Visible light

imaging Still images from swarming plates and time lapse movies were captured with a CoolSnapFX (Roper Scientific) cooled ccd camera using ImagePro MC Express on a Zeiss Axioplan 2. Biofilms were examined using 1% Crystal Violet as a simple stain. Color images were captured using a Kodak DC290 digital camera, using the Kodak image capture software provided. Macroscopic colony images and wetting Tenoxicam agent images were collected using a Fuji FinePix 5700 digital camera. Colonies were photographed using a black velvet cloth to damp reflection. To capture images of the wetting agent, the plate was illuminated using diffuse reflected light, and angled to capture the refractive quality of the layer. For all microscopy, calibration images were captured with all microscope lenses of a stage micrometer, and Image J was used for measurement and scaling. Results Swarming motility Our laboratory developed a swarming agar plate based on previous growth and swarming experiments in V. paradoxus and P aeruginosa. Our swarming agar used for initial studies used 0.5% agarose to solidify the plate, the freshwater media (FW) base previously used by Leadbetter and Greenberg [5], with 0.2% glucose as a carbon source. Previous work in P.

Therefore, titanium alkoxides, in this case TBT, can be readily grafted onto the surface of GO through chemical adsorption at the molecular level [28]. On the other hand, it is widely known that titanium alkoxides BAY 11-7082 are extremely sensitive to water. Rapid decomposition

of the titanium precursor would result in the agglomeration of TiO2 crystals as well as hinder the homogeneous growth of TiO2 onto GO. Hence, EG and HAc were introduced into the mixture to co-control the hydrolysis rate of TBT [29]. In addition, the mixtures were also prechilled in an ice bath to further reduce the hydrolysis rate. During the solvothermal treatment, GO was reduced to rGO, and TiO2 nanoparticles formed on the rGO surface simultaneously. The preparation strategy is illustrated in Figure 1. Figure 1 Procedure for the synthesis of rGO-TiO 2 nanocomposites. Characterization of reduced graphene oxide-TiO2 composites The surface morphology and structure of the rGO-TiO2 nanocomposite were characterized using FESEM and HRTEM. From Figure 2a, b, it is observed that the surface of rGO sheets was packed densely with TiO2 nanoparticles, which displayed a good combination of rGO and

TiO2. Despite that, MI-503 clinical trial the profile of a single TiO2 nanoparticle could be clearly distinguished, indicating that the aggregation of TiO2 was well prevented during the preparation process. The TiO2 particles were also found to exhibit a narrow size distribution with an average crystallite size of 12 nm. The corresponding

HRTEM images (Figure 2c, d) clearly showed the lattice fringes of rGO, which were parallel to the edges of the TiO2 nanoparticles. The lattice spacing of TiO2 was measured to be ca. 0.35 nm, which corresponds to the (101) plane of anatase TiO2 (JCPDS no. 2101272). The rGO sheets were composed of a mixture of two to five layers based on HRTEM observations. Figure 2 Electron microscopy of the rGO-TiO 2 composites. (a) FESEM image, (b, c) HRTEM images, and (d) enlarged HRTEM image of a selected rGO-TiO2 heterojunction. It is known that few-layer rGO sheets have the tendency to aggregate back to the graphite structure due to strong van der Waals interaction [30]. Therefore, the crystallization selleck chemicals llc of TiO2 on the surface of rGO was particularly helpful in overcoming this interaction, which could ultimately alleviate the agglomeration and restacking of the graphene sheets. In addition, the intimate connection would allow the electrons to transfer easily from TiO2 to rGO sheets during the photoexcitation process, which could significantly increase the separation of photoinduced charges and enhance the photocatalytic activity. Raman spectroscopy has been accepted to be a powerful and nondestructive tool to characterize the quality of graphitic materials.

The most dramatic change made by the addition of PP was the reduced H2O content in bio-oil. As shown in Table 3, the H2O content in the bio-oil obtained from co-pyrolysis was 4.63 wt% (non-catalytic) and 8.93 wt% (catalytic), while that in the bio-oil from the pyrolysis of L. japonica only was 42.03 wt% (non-catalytic) and 50.32 wt% (catalytic). The addition of PP enhanced the selleck chemicals supply of C and H, resulting in the substantially decreased H2O content in bio-oil. Catalytic co-pyrolysis produced more CO, CO2, and C1-C4 hydrocarbons, compared to non-catalytic co-pyrolysis, indicating that deoxygenation reactions were promoted by catalyst.

The increase in the water content (from 4.63 to 8.93 wt%) by catalytic reforming suggests the enhancement of dehydration by catalyst. Figure 6 Product yields of catalytic co-pyrolysis of Laminaria japonica and polypropylene. Table 3 Yield of gas composition from catalytic co-pyrolysis of Laminaria japonica and polypropylene Catalyst

Without catalyst Al-SBA-15 Yield (wt%) CO 1.63 2.10 CO2 12.61 13.88 C1 ~ C4 5.37 6.46 Water contents in bio-oil (wt%) 4.63 8.93 Figure 7 shows the species distribution of the bio-oil obtained from the catalytic co-pyrolysis using Py-GC/MS. Compared to the Androgen Receptor Antagonist clinical trial result of the catalytic pyrolysis of L. japonica only (Figure 3), the addition of PP increased the content of hydrocarbons enormously, making it the most abundant species in the bio-oil, because the main product species of the cracking of polypropylene are hydrocarbons. Catalytic co-pyrolysis reduced the content of oxygenates considerably compared to non-catalytic co-pyrolysis. This was attributed to the conversion of oxygenates into mono-aromatics or PAHs on the acid sites of Al-SBA-15. Figure 7 Product distribution of bio-oil from catalytic co-pyrolysis of Laminaria japonica and polypropylene. Total hydrocarbon content was reduced a little by catalytic reforming. According to the carbon number distribution of hydrocarbons shown in Figure 8, non-catalytic co-pyrolysis produced mainly large-molecular-mass hydrocarbons (≥C17). These wax species must be decomposed using adequate catalysts because they cause process blockage

and deteriorate Buspirone HCl the oil quality. In this study, most large-molecular-mass hydrocarbons were removed by Al-SBA-15. They are believed to have been cracked into gasoline-range hydrocarbons (C5-C9) and diesel-range hydrocarbons (C10-C17) on the acid sites of Al-SBA-15. A previous study on the catalytic pyrolysis of PP over Al-SBA-15 reported that Al-SBA-15 decomposed PP into C5-C17 hydrocarbons [19]. Figure 8 Carbon number distribution of hydrocarbons from catalytic co-pyrolysis of Laminaria japonica and polypropylene. Conclusions The catalytic co-pyrolysis of L. japonica and polypropylene resulted in the production of bio-oil with significantly higher quality compared to the catalytic pyrolysis of L. japonica only or the non-catalytic co-pyrolysis.