MSP2 strain showed low expression of glnA1 gene as compared to the expression in other strains in low nitrogen condition because there was no regulation at transcriptional level due to lack of P1 promoter

hence lack of GlnR binding motif also. PLG layer has been known to be present in the cell wall of only virulent strains Vismodegib of mycobacteria [16, 23]. Harth and colleagues indicated that extracellular GS of pathogenic mycobacteria is involved in synthesis of this layer [10, 24, 25]. There has also been reports stating the involvement of PLG layer of M. bovis in cell wall strength and in providing resistance to various physical and chemical stress factors [8]. The absence of PLG layer from the cell wall of mycobacteria grown in high see more nitrogen condition indirectly suggest that PLG layer may be a form of nitrogen assimilation in pathogenic mycobacteria. In macrophages, mycobacteria encounter nitrogen stress which leads to high GS expression and PLG layer synthesis

in the cell wall. Immunogold localization and PLG isolation studies further validated the finding of no detectable PLG in the cell wall of M. bovis, MSFP, MSP1 and MSP2 strains when grown in high nitrogen conditions. The ability of the pathogenic mycobacteria to form biofilm adds on to their Torin 1 molecular weight virulence potential [26]. Biofilm formed at air liquid interface are popularly known as pellicle. Additionally, mycolic acids are the major component of the biofilms formed by mycobacterial species [26, 27] but it is not clearly known whether mycolic acid synthesis or its amount in cell wall is affected by PLG layer. However, there are few reports that suggest the involvement of PLG layer in biofilm formation [8]. A ∆glnA1 strain of M. bovis that

lack PLG layer in the cell wall was found to be defective in biofilm formation [8]. Additionally, our results showed that the biofilm and pellicle forming capability STK38 of M. smegmatis strain complemented with M. bovis glnA1 was enhanced than the wild type. This is due to the fact that higher expression of M. bovis glnA1 leads to the synthesis of PLG layer in the M. smegmatis complemented with M. bovis glnA1[8]. There are reports also suggesting that microbial amyloids play a significant role in biofilms of actinobacteria [28, 29]. Additionally, it was observed that biofilm was formed significantly much better in low nitrogen conditions which added to the involvement of PLG layer in biofilm formation. There is a gap in our understanding of the exact mechanisms and enzymes involved in the synthesis of PLG layer till date. In addition to it, characterization of PLG layer, can further help in our understanding of complex mycobacterial cell wall. Because of high molecular weight and inert nature of the polymer it may also act as an adjuvant. This needs further investigation.

Kim SK, Kim SA, Lee CH, Lee HJ, Jeong SY: The structural and optical behaviors of K-doped ZnO/Al 2 O 3 (0001) films. Appl Phys Lett 2004, 85:419–421. 10.1063/1.1773612CrossRef 37. Gopalakrishnan N, Shin BC, Lin HS, Balasubramanian T, Yu YS: Effect

of GaN doping on ZnO films by pulsed laser deposition. Materials Letters 2007, 61:2307–2310. 10.1016/j.matlet.2006.08.075CrossRef 38. Frenzel H, Wenckstern HV, Weber A, Schmidt H, Biehne G, Hochmuth H, find more Lorenz M, Grundmann M: Photocurrent spectroscopy of deep levels in ZnO thin films. Physical Review B 2007, 76:035214–035219.CrossRef 39. Wang XB, Song C, Geng KW, Zeng F, Pan F: Photoluminescence and Raman scattering of Cu-doped ZnO films prepared by magnetron sputtering. Appl Surf Sci 2007, 253:6905–6906. 10.1016/j.apsusc.2007.02.013CrossRef 40. Singh R, Kumar M, Chandra S: Growth and characterization of high resistivity c-axis oriented ZnO films on different substrates by RF magnetron sputtering for MEMS applications. J Mater Sci Res 2007, 42:4675–4683. 10.1007/s10853-006-0372-5CrossRef 41. Xiu FX, Yang Z, Mandalapu LJ, Liu JL: Donor

and acceptor competitions in phosphorus-doped ZnO. Appl Phys Lett 2006, 88:152116–152118. 10.1063/1.2194870CrossRef 42. Srinivasan G, Rajendra Kumar RT, Kumar J: Influence of Al dopant on microstructure and optical properties of ZnO thin films prepared by PD0332991 sol-gel spin coating method. Optical Materials 2007, 30:314–317. 10.1016/j.optmat.2006.11.075CrossRef 43. Zou J, Yip HL, Hau SK, Jen AKY: Metal grid/conducting LDC000067 research buy polymer hybrid transparent. Appl Phys Lett 2010, 96:203301–203303.

Dipeptidyl peptidase 10.1063/1.3394679CrossRef 44. Huang J, Li G, Yang Y: A Semi-transparent plastic solar cell fabricated by a lamination process. Adv Mater 2008, 20:415–419. 10.1002/adma.200701101CrossRef 45. Yu BY, Tsai A, Tsai SP, Wong KT, Yang Y, Chu CW: Efficient inverted solar cells using TiO 2 nanotube arrays, J. J Shyue Nanotechnology 2008, 19:255202–255206. 10.1088/0957-4484/19/25/255202CrossRef 46. Li G, Chu CW, Shrotriya V, Huang J, Yang Y: Efficient inverted polymer solar cells. Appl Phys Lett 2006, 88:253503–253505. 10.1063/1.2212270CrossRef 47. Zhou Y, Li F, Barrau S, Tian W, Inganas O, Zhang F: Inverted and transparent polymer solar cells prepared with vacuum-free processing. Sol Energ Mater Sol Cell 2009, 93:497–500. 10.1016/j.solmat.2008.11.002CrossRef 48. Huang J, Xu Z, Yang Y: Low-work-function surface formed by solution-processed and thermally deposited nanoscale layers of cesium carbonate. Adv Funct Mater 2007, 17:1966–1973. 10.1002/adfm.200700051CrossRef 49. Briere TR, Sommer AH: Low‒work‒function surfaces produced by cesium carbonate decomposition. Journal of Applied Physics 1977, 48:3547–3550. 10.1063/1.324152CrossRef 50. Wu CI, Lin CT, Chen YH, Chen MH, Lu YJ, Wu CC: Electronic structures and electron-injection mechanisms of cesium-carbonate-incorporated cathode structures for organic light-emitting devices. Appl Phys Lett 2006, 88:152104–152106. 10.1063/1.2192982CrossRef 51.

Microb Ecol 2003, 45:455–463.PubMedCrossRef 14. Heilig HG, Zoetendal EG, Vaughan EE, Marteau P, Akkermans AD, de Vos WM: Molecular diversity

of Lactobacillus spp. and other lactic acid bacteria in the human intestine as determined by specific amplification of 16S ribosomal DNA. Appl Environ Microbiol 2002, 68:114–123.PubMedCrossRef 15. Walter J, Hertel C, Tannock GW, Lis CM, Munro K, Hammes WP: Detection of Lactobacillus , Pediococcus , Leuconostoc , and Weissella species in human feces by using group-specific PCR primers and denaturing gradient gel electrophoresis. Appl Environ Microbiol 2001, 67:2578–2585.PubMedCrossRef 16. Chaillou S, Champomier-Vergès IWR-1 concentration MC, Cornet M, Crutz-Le Coq AM, Dudez AM, Martin V, Beaufils S, Darbon-Rongere E, Bossy R, Loux V, MAPK inhibitor Zagorec M: The complete genome sequence of selleck kinase inhibitor the

meat-borne lactic acid bacterium Lactobacillus sakei 23K. Nat Biotechnol 2005, 23:1527–1533.PubMedCrossRef 17. Stentz R, Cornet M, Chaillou S, Zagorec M: Adaption of Lactobacillus sakei to meat: a new regulatory mechanism of ribose utilization? INRA, EDP Sciences 2001, 81:131–138. 18. Lauret R, Morel-Deville F, Berthier F, Champomier Vergès MC, Postma P, Erlich SD, Zagorec M: Carbohydrate utilization in Lactobacillus sake . Appl Environ Microbiol 1996, 62:1922–1927.PubMed 19. Champomier-Vergès MC, Chaillou S, Cornet M, Zagorec M: Erratum to “” Lactobacillus sakei : recent developments and future prospects”". Resveratrol Res Microbiol 2002, 153:115–123.PubMedCrossRef 20. Naterstad K, Rud I, Kvam I, Axelsson L: Characterisation of the gap operon

from Lactobacillus plantarum and Lactobacillus sakei . Curr Microbiol 2007, 54:180–185.PubMedCrossRef 21. Stentz R, Zagorec M: Ribose utilization in Lactobacillus sakei : analysis of the regulation of the rbs operon and putative involvement of a new transporter. J Mol Microbiol Biotechnol 1999, 1:165–173.PubMed 22. Stentz R, Lauret R, Ehrlich SD, Morel-Deville F, Zagorec M: Molecular cloning and analysis of the ptsHI operon in Lactobacillus sake . Appl Environ Microbiol 1997, 63:2111–2116.PubMed 23. Stulke J, Hillen W: Carbon catabolite repression in bacteria. Curr Opin Microbiol 1999, 2:195–201.PubMedCrossRef 24. Titgemeyer F, Hillen W: Global control of sugar metabolism: a gram-positive solution. Antonie Van Leeuwenhoek 2002, 82:59–71.PubMedCrossRef 25. Rodionov DA, Mironov AA, Gelfand MS: Transcriptional regulation of pentose utilisation systems in the Bacillus/Clostridium group of bacteria. FEMS Microbiol Lett 2001, 205:305–314.PubMedCrossRef 26.

Stat3C tumor study. JNG conducted the in vitro studies and assisted in the tumor study. MAC prepared and analyzed the galanga extracts. PA conducted the histopathological analyses. JD supplied the K5.Stat3C transgenic mice and assisted in the design and interpretation of the tumor study. All authors read and approved the final manuscript, which was revised by HKH.”
“Background Proteases play an important role in different biological processes including cell check details differentiation, inflammation

and tissue remodelling, haemostasis, immunity, angiogenesis, apoptosis and malignant disease [1]. Specifically, proteases are well known factors to promote local progression and distant metastasis of colorectal cancer and many other solid tumors [2, 3]. Furthermore, there is increasing evidence that proteases also SN-38 manufacturer have key functions in early stages of tumor development [4]. The tumor-associated proteases are either secreted

directly by the tumor or originate from surrounding connective tissue and infiltrating leucocytes as a result of tumor-stroma interaction [5]. Some tumor-associated proteases like cathepsins, matrix-metalloproteases, kallikreins and cancer procoagulant (CP) are released into the bloodstream and can be used for diagnostic and prognostic purposes [6–10]. Tumor-associated protease activity in serum specimens of cancer patients can be monitored using synthetic substrates that are selectively cleaved by the protease of interest [6–9]. With the use of appropriate synthetic

reporter-peptides (RPs) for spiking of serum specimens, the reaction conditions that comprise substrate concentration, incubation time and buffer composition can be optimized and standardized accordingly [11]. Furthermore, the proteolytic fragments accumulate to the level that they become readily detectable by mass spectrometry [8]. This approach is similar to established diagnostic assays measuring the proteolytic activity of distinct enzymes, e.g., coagulation factors [12]. Recently, we have described a functional protease profiling approach using a reporter peptide that is cleaved by the tumor associated protease cancer procoagulant (EC 3.4.22.26) [8]. However, the analysis of proteolytic fragments was performed with MALDI-TOF mass spectrometry GPX6 that is only a semi-quantitative method [13] with limited inter-day reproducibility [8]. Furthermore, proteolytic fragments had to be extracted from serum specimens with serial affinity purification that is a rather laborious method with limited throughput and reproducibility. To alleviate these restrictions, we have developed a robust and highly selleck chemical reproducible liquid chromatography-mass spectrometry (LC-MS) assay for the absolute quantification of a targeted proteolytic fragment. Serum has a high intrinsic proteolytic activity that leads to continuous processing of proteins and peptides [14].

We also detected the antitumor effect of human monocytes on gene modified ovarian cells by MTT: There were 3 experimental groups including SKOV3/MCP-1, SKOV3/tk-MCP-1

and SKOV3/neo. Mononuclear cells were used as effectors, and tumor cells above-mentioned were used as target. Cells were seeded in the 96-well plates at the density of 5 × 103 Selleck OICR-9429 cells/well. Then mononuclear were added at different ratio of effector to this website target (20:1, 10:1, 5:1), incubated at 37°C in 5% CO2 incubator for 4 days, cytotoxicity were determined. The surviving rate of mixed tumor cell under the action of GCV only was determined by MTT. Briefly, there were 3 experimental groups (including SKOV3/tk, SKOV3/tk-MCP-1 and SKOV3/neo). The above cells infected by different gene at different proportion (100%, 90%, 70%, 50%, 30%, 10%, 0) were mixed with wild SKOV3, and then were added in 10 μg/ml GCV

The surviving rate of cells were determined by MTT incubated in 96-well plates for 4 days at 37°C in 5% CO2 incubator. Next we detect the surviving rate of mixed tumor cell under the action of GCV plus human monocytes by MTT. Each kind of cells and wild SKOV3 were seeded in 96-well plates as the same way. Then 5 × 104 human monocytes were added at the ratios of 10:1(effectors: target). All cells were incubated for 4 days at 37°C in 5% CO2 incubator after supplied 10 μg/ml GCV. Cells without GCV were used as control group. Detection of cell apoptosis rate, cell cycle and the expression of CD25 (IL-2R) and CD44v6 by flow cytometer: SKOV3/tk, SKOV3/tk-MCP-1 and SKOV3/neo were seeded in 25 cm flask. After cells adherenced, we added human monocytes at the ratios of 10:1(effectors: target) and Cell Cycle inhibitor 0.5 μg/ml GCV, and then incubated cells for 48 h at 37°C in 5% CO2 incubator. Animal experiments The present study was approved by the local animal Care Committee and is in compliance with Chinese laws for animal protection. 6 to 8 weeks old, weight-matched female combined immune deficiency mice (C.B17/SCID) were purchased from Weitonglihua experimental animal limited company. Animals were housed in the animal facility of

the Medical College of Shandong university Thiamet G of China. Enzyme-linked immunosorbent assay (ELISA) for the IgG of C.B17/SCIDs in serum was performed to eliminate immune leakage according to the manufacturer’s protocol. Human mononuclear cells were isolated from human peripheral blood mononuclear cells by Ficoll-Hypaque discontiguous density gradient centrifugation technique and were re-suspended in fresh RPMI 1640 medium without NBS at a density of 8 × 107cells/ml. 0.5 ml cell suspension was injected into abdominal cavity of per C.B17/SCID for immunologic reconstitution. Twenty-four hours after celiac immunologic reconstitution, SKOV3/neo, SKOV3/tk, SKOV3/MCP-1 and SKOV3/tk-MCP-1 cell lines were inoculated by intraperitoneal injection at a density of 2 × 107 cell/SCID. According to the cells inoculated, all experimental C.B17/SCIDs were divided into 4 groups, i.e.

(B) The DNA-binding assays for MtrA on different DNA substrates. The EMSA reactions (10 μl) for measuring the mobility shift contained 200 fmol 32P-labeled DNA and increasing amounts of MtrA proteins (100 nM-600 nM). The protein/DNA complex is indicated by arrows on the right of the panels. (C) Schematic representation of conserved motifs

located downstream of two dnaA promoters. The base-pair numbers far from the start codon of the dnaA gene are indicated. selleck screening library The interaction between MtrA and these two sequence boxes was further confirmed by DNase I footprinting assays (Fig. 3). Regions that contain these two boxes were significantly protected when MtrA was present. Protection at S6 occurred at all MtrA concentrations while the protection of S7 was dependent on the concentration of MtrA. This suggests that MtrA has different binding affinities with these regions. Figure 3 MtrA footprinting analysis in the M. tuberculosis dnaA HMPL-504 promoter PLX3397 purchase region. (A) DNase I footprinting assay of the

protection of two short dnaA promoter regions (S6 and S7) against DNase I digestion by MtrA. The substrate S6 contains S1 and S2 sequences, and the substrate S7 contains S5 sequences. The ladders are shown in the right panel and the obtained nucleotide sequences are listed. The protected regions are indicated. The two specific sequence boxes are indicated by “”*”". (B) Summary of MtrA footprinting analysis in the M. tuberculosis dnaA promoter Molecular motor region. The DNA sequence correspond with

the dnaA promoter region from -303 to -1. The position of two transcription start sites (P1dnaA and P2dnaA), two footprint regions, and two MtrA binding boxes are indicated. We characterized two sequence boxes for the recognition of MtrA within the dnaA promoter, situated immediately downstream of promoters P1 and P2. The binding sequence boxes and their situation within the dnaA promoter are summarized in Fig. 2C. Characterization of potential target genes regulated by MtrA in mycobacterial genomes We searched the intergenic regions of the M. tuberculosis and M. smegmatis genomes extensively based on the two sequence motifs for MtrA in the dnaA gene promoter region. To validate the target genes, several regulatory regions of the genes were amplified. The DNA-binding activities of MtrA were examined using EMSA assays. As shown in Fig. 4, the regulatory sequence of a predicted target gene, isoniazid inducible gene iniB (rv0341), could be recognized by MtrA. A specific DNA/protein complex band was also observed. In addition, MtrA was able to bind with two target promoter DNA sequences of Rv0574 (a hypothetical protein) and Rv3476 (KgtP), producing a corresponding DNA/protein band (Fig. 4A). The positive target DNA was shown to bind with MtrA, while the negative DNA was not. The 7 bp sequence motif could also be found in the promoter regions of two previously characterized target genes, CgmepA and CgproP, in C. glutamicum. Interestingly, M.

Cell 2002,110(1):119–131.PubMedCrossRef 17. Wagner D, Maser J, Lai B, Cai Z, Barry CE, Honer Zu, Bentrup K, Russell DG, Bermudez LE: Elemental analysis of Mycobacterium avium -, Mycobacterium tuberculosis -, and Mycobacterium smegmatis -containing phagosomes indicates pathogen-induced microenvironments within the host cell’s endosomal system. J Immunol 2005,174(3):1491–1500.PubMed 18. Shrive AK, Tharia HA, Strong P, Kishore U, Burns

TEW-7197 in vitro I, Rizkallah PJ, Reid KB, Greenhough TJ: High-resolution structural insights into ligand binding and immune cell recognition by human lung surfactant protein D. J Mol Biol 2003,331(2):509–523.PubMedCrossRef 19. Ramakrishnan L, Federspiel NA, Falkow S: Granuloma-specific expression of Mycobacterium virulence proteins from the PHA-848125 order glycine-rich PE-PGRS family. Science 2000,288(5470):1436–1439.PubMedCrossRef

20. Sampson SL, Lukey P, Warren RM, van Helden PD, Richardson M, Everett MJ: Expression, characterization and subcellular localization of the Mycobacterium tuberculosis PPE gene Rv1917c. Tuberculosis (Edinb) 2001,81(5–6):305–317.CrossRef 21. Camacho selleckchem LR, Ensergueix D, Perez E, Gicquel B, Guilhot C: Identification of a virulence gene cluster of Mycobacterium tuberculosis by signature-tagged transposon mutagenesis. Mol Microbiol 1999,34(2):257–267.PubMedCrossRef 22. Vergne I, Chua J, Singh SB, Deretic V: Cell biology of Mycobacterium tuberculosis phagosome. Annu Rev Cell Dev Biol 2004, 20:367–394.PubMedCrossRef 23. Malik ZA, Denning GM, Kusner DJ: Inhibition of Ca(2+) signaling by Mycobacterium tuberculosis is associated with reduced phagosome-lysosome fusion and increased survival within human macrophages. J Exp Med 2000,191(2):287–302.PubMedCrossRef 24. Malik ZA, Thompson CR, Hashimi S, Porter B, Iyer SS, Kusner DJ: Cutting edge: Mycobacterium

tuberculosis blocks Ca2+ signaling and phagosome maturation in human macrophages via specific inhibition of sphingosine kinase. J Immunol 2003,170(6):2811–2815.PubMed 25. Clemens DL, Horwitz MA: Characterization of the Mycobacterium tuberculosis phagosome and evidence that Loperamide phagosomal maturation is inhibited. J Exp Med 1995,181(1):257–270.PubMedCrossRef 26. Fratti RA, Backer JM, Gruenberg J, Corvera S, Deretic V: Role of phosphatidylinositol 3-kinase and Rab5 effectors in phagosomal biogenesis and mycobacterial phagosome maturation arrest. J Cell Biol 2001,154(3):631–644.PubMedCrossRef 27. Schlesinger LS: Macrophage phagocytosis of virulent but not attenuated strains of Mycobacterium tuberculosis is mediated by mannose receptors in addition to complement receptors. J Immunol 1993,150(7):2920–2930.PubMed 28. Bermudez LE, Young LS, Enkel H: Interaction of Mycobacterium avium complex with human macrophages: roles of membrane receptors and serum proteins. Infect Immun 1991,59(5):1697–1702.PubMed 29.

Secondary antibody conjugated to horseradish

peroxidase was obtained from Bio-Rad. Visualisation was done by the enhanced chemiluminescent reaction (Stratagene). Non-denaturating PAGE was performed using 7.5% (w/v) polyacrylamide gels pH 8.5 and included 0.1% (w/v) Triton-X100 in the gels [14]. Samples (25 μg of protein) were incubated with 5% (v/v) Triton X-100 prior to Selleckchem 4EGI-1 application to the gels. Where indicated, the relative intensity PI3K Inhibitor Library in vitro of hydrogenase staining and protein amount from immunoblots was quantified using ImageJ from the National Institutes of Health [36]. Hydrogenase activity-staining was done as described in [14] except that the buffer used was 50 mM MOPS pH 7.0. Acknowledgements We are grateful to Nadine Taudte and Gregor Grass for supplying strains and the plasmid pFEO and to Frank Sargent for supplying anti-hydrogenase antisera. This work was supported by a grant from the Deutsche Forschungsgemeinschaft (DFG SA494/3-1). Electronic supplementary

material Additional file 1: Plasmid-encoded FeoB synthesis in MC4100 and PM06 ( feoB ::Tn 5 ). Extracts (25 μg protein in membrane sample buffer) from Daporinad MC4100 and PM06, transformed with pECD1079 bearing feoB and pFEO bearing the whole feo operon, both cloned behind a tetracycline promotor and encoding an N-terminal StrepII-tag on FeoB encoded on pECD1079 were separated by SDS-PAGE (10% w/v polyacrylamide) and after transfer to nitrocellulose detected by incubation with Strep-tactin conjugated to horseradish peroxidase. Strains were grown either with or without aeration in TGYEP, pH 6.5 and

gene expression was induced with 0.2 μg ml-1 AHT (anhydrotetracycline) as indicated. Biotin carboxyl carrier protein (BCCP) served as a loading control. The sizes of the protein standards are shown on the right side of the gel. The angled arrow indicates the position of the Strep-FeoB polypeptide. Extracts Flucloronide derived from MC4100 and PM06 transformed with pFEO did not synthesize Strep-tagged FeoB and therefore acted as a negative control. (TIFF 371 KB) References 1. Vignais P, Billoud B: Occurrence, classification, and biological function of hydrogenases: an overview. Chem Rev 2007, 4206–4272. 2. Forzi L, Sawers RG: Maturation of [NiFe]-hydrogenases in Escherichia coli . Biometals 2007, 20:565–578.PubMedCrossRef 3. Pinske C, Krüger S, Soboh B, Ihling C, Kuhns M, Braussemann M, Jaroschinsky M, Sauer C, Sargent F, Sinz A, Sawers RG: Efficient electron transfer from hydrogen to benzyl viologen by the [NiFe]-hydrogenases of Escherichia coli is dependent on the coexpression of the iron-sulfur cluster-containing small subunit. Arch Microbiol 2011, in press. 4. Lukey MJ, Parkin A, Roessler MM, Murphy BJ, Harmer J, Palmer T, Sargent F, Armstrong FA: How Escherichia coli is equipped to oxidize hydrogen under different redox conditions. J Biol Chem 2010, 285:3928–3938.PubMedCrossRef 5. Böck A, King P, Blokesch M, Posewitz M: Maturation of hydrogenases. Adv Microb Physiol 2006, 51:1–71.

When the film thickness is less than 10 nm, thermal energy interrupts the Protein Tyrosine Kinase inhibitor Magnetic moment orientation due to small grain size, which shows superparamagnetic effect. With increasing film thickness, spinel structure selleck products is formed and crystallite size increases, which results in the decrease in the full width at half maximum of the X-ray spectral peaks and the increase of M s. Figure 4 TEM images of the 500-nm ferrite film. Dark-field cross-section image (a) and the HRTEM

image (b). Conclusions Ni ferrite films with different thicknesses were fabricated under RT. Structure and magnetic properties of Ni ferrite films were investigated as functions of thickness: the 10-nm film exhibits superparamagnetism; M s increases monotonically, while H c first increases then Adriamycin cell line decreases as the film thickness increases. The SEM and TEM images were taken to investigate the underlying magnetic mechanism. A disordered layer at the bottom of the ferrite layer can be seen in the TEM image; this layer may probably be responsible for the superparamagnetic behavior of the 10-nm film. Acknowledgments This work is supported by

the National Basic Research Program of China (grant no. 2012CB933101), the National Science Fund for Distinguished Young Scholars (grant no. 50925103), the Key Grant Project of Chinese Ministry of Education (grant no. 309027), the National Natural Science Foundation of China (grant no. 11034004 and no. 50902064), and the Fundamental Research Funds for Central Universities (lzujbky-2012-31). References 1. Ramos A, Matzen S, Moussy J-B, Ott F, Viret M: Artificial antiphase boundary at the interface of ferrimagnetic spinel bilayers. Phys Rev B 2009, 79:014401.CrossRef 2. Masoudpanah SM, Seyyed Ebrahimi SA, Ong CK: Magnetic properties of strontium

hexaferrite films prepared by pulsed laser deposition. J Magn Magn Mater 2012, 324:2654–2658.CrossRef 3. Foerster M, Rebled J, Estradé S, Sánchez F, Peiró F, Fontcuberta J: Distinct magnetism in ultrathin epitaxial NiFe 2 O 4 films on MgAl 2 O 4 and SrTiO 3 single crystalline substrates. Phys Rev B 2011, 84:144422.CrossRef 4. Hai TH, Van HTB, Phong TC, Abe M: Spinel ferrite over thin-film synthesis by spin-spray ferrite plating. Physica B 2003, 327:194–197.CrossRef 5. Kondo K, Chiba T, Ono H, Yoshida S, Shimada Y, Matsushita N, Abe M: Conducted noise suppression up to GHz range by spin-sprayed Ni 0.2 Zn x Fe 2.8- x O 4 ( x = 0.3, 0.6) films having different natural resonance frequencies. J Magn Magn Mater 2006, 301:107–111.CrossRef 6. Chen D-H, He X-R: Synthesis of nickel ferrite nanoparticles by sol–gel method. Mater Res Bull 2001, 36:1369–1377.CrossRef 7. Sartale SD, Lokhande CD, Ganesan V: Electrochemical deposition and characterization of CoFe 2 O 4 thin films. Phys Status Solidi A 2005, 202:85–94.CrossRef 8. Chen L, Xu J, Tanner DA, Phelan R, Van der Meulen M, Holmes JD, Morris MA: One-step synthesis of stoichiometrically defined metal oxide nanoparticles at room temperature. Chem Eur J 2009, 15:440–448.

56 and 150 MHz and with different power application positions. A two-dimensional (1 m × 0.2 m) plane electrode was modeled, and the impedances of the atmospheric-pressure click here plasma obtained from IV (current and voltage) measurements and analysis [7] were used for the calculation. Methods Modeling A one-dimensional model of electrodes and plasma (including

sheath) is shown in Figure 1. Radio-frequency voltage is applied to the upper electrode, and the lower electrode is grounded. We assume that only the upper electrode has resistance and inductance for simplicity. This simplified model is useful enough to calculate a relative voltage between two electrodes, because only relative voltage is important for plasma. Figure 1 One-dimensional model of electrodes SC75741 and plasma (including sheath). Plasma will be generated in the space between the upper and lower electrodes. In this model, electrodes (upper and lower) and plasma are divided into small elements of length ΔX. The voltage U is assumed to be constant within the elements. Symbol δ is the thickness of current flow (skin depth). The currents flowing into and out from the element BX-795 are shown by the arrows in Figure 1. The plasma is assumed to be able to be represented by the parallel connection of the capacitance C p and the conductance G p. One can derive a one-dimensional

wave equation from the above mentioned one-dimensional model and extend it to the following two-dimensional wave equation. In the case of a two-dimensional model, the electrode will be divided in two directions, and the widths of the element will be ΔX and ΔY. For simplicity, the element widths ΔX and ΔY were set to be equal. (1) Here, L and R are inductance and resistance per unit length (in current flow direction) of the electrodes of element width (ΔX or ΔY), and C p and G p are Gemcitabine chemical structure the capacitance and conductance of plasma per unit length of element width, respectively. F(x,y,t) is the external force (causes voltage to change) applied to the upper electrode

at position (x,y). Electrode resistance R and inductance L When radio-frequency power is applied to the electrodes, the current will flow only on the surface of the electrodes owing to the skin effect. The effective electrode resistance per unit length R (of width w) is determined by the following equation [8]: (2) where σ is the conductivity of the electrode material, δ is the skin depth, and w is the width of the current flow. The skin depth δ is determined by (3) where ω is the angular frequency, and μ is the magnetic permeability of the electrode material. The inductance of a pair of two parallel plates (electrodes) per unit length (of width w) can be calculated using [8] (4) where d is the distance between the upper and lower electrodes, and w is the width of the current flow. When aluminum is used as the electrode material, the conductivity σ is 0.