A good predictive ability, with an \( r^2_\textpre = 0. 60 7 \), for the compounds in the test set was obtained in this calibration step. Table 2 reports that the predicted values fall close to the observed biological activity value, deviating by less than one logarithmic unit. The β2 CoMFA steric and electrostatic fields from the final non-cross-validated analysis are plotted R428 in vivo in Figs. 4b and 5b respectively. The most active compound, 20, was treated as the reference molecule. The graphical interpretation of the field contribution of the steric contour map is shown in Fig. 4b. The steric contour map shows three yellow regions surrounding the phenyl unit in the NHSO2Ph

group, and a small green at the para

position on the same ring. This indicates that it is preferable to reduce the steric bulk due to the Ph group. The presence of a simple thiophen ring, as in many other molecules in this series, is preferable for β2 activity. A very large yellow contour is noted near the C7 of the indole ring in Fig. 4b, indicating that the steric bulk should be reduced for improved β2 activity. The CoMFA electrostatic contour map displays a large blue region surrounding the SO2Ph group and two small red regions in close proximity, suggesting that a strong reduction in the electronegative groups is preferred in this region. There are two small blue regions and one small red region at the C7 of the indole ring of the reference compound. The distribution range of blue selleck chemicals llc is higher than that of red, indicating that electropositive groups in this region are very important for the β2 biological activity. CoMFA of the β3-adrenoceptor The β3 CoMFA analysis based on the fit atom alignment yielded acceptable cross-validated (\( r^2_\textcv = 0. 5 5 8 \)) and conventional results (\( r^2 = 0. 9 9 P-type ATPase 5,F – \texttest

value = 3 10. 7 1 7 \)), with the optimal number of components found to be six. In this model, steric and electrostatic fields contribute to the QSAR equation by 40.1% and 59.9%, respectively. The high bootstrapped (10 sampling) \( r^2_\textbs \) value of 0.999 (SEE = 0.033, std dev = 0.001) was found. Compounds 8, 10, 14, 18, and 20 (test set) were used to evaluate the predictive power of this CoMFA model. The predicted versus the actual values of biological activities obtained from the analysis are plotted in Fig. 3c. The β3 CoMFA model shows a very good predictive ability, with \( r^2_\textpre = 0. 7 5 8 \) for the compounds in the test set, as obtained for the calibration steps. Table 2 shows that the predicted values fall close to the observed biological activity value, deviating by less than one logarithmic unit. The steric and electrostatic contour maps obtained from the β3 CoMFA model are shown in Figs. 4c and 5c, respectively, along with compound 16. In Fig.

We have also found that statins induce Ulixertinib datasheet apoptosis by activation of caspase-3 through inhibition of GGPP biosynthesis. It has been reported that statins inhibit prenylation of small G proteins by suppressing the production of GGPP [4, 8]. Lovastatin is known to inhibit the mevalonic acid and MAPK pathways, thereby inducing apoptosis [9, 10]. It has been reported that the mechanism of action is inhibition of GGPP biosynthesis [10, 11]. These findings suggest that statins induce apoptosis by activation of caspase-3 through suppression

of GGPP biosynthesis. GGPP is an important membrane-anchoring molecule of Ras protein. A shortage of GGPP facilitates dissociation of Ras from the inner surface of the membrane, and decreases the Ras-mediated growth signal, thereby inhibiting cellular proliferation [12, 13]. Our results clearly demonstrate that statins induce a decrease in ERK1/2 and Akt activation of Ras downstream, Navitoclax clinical trial but the activation of JNK1/2 was not altered. We previously reported that mevastatin induces a decrease in phosphorylated ERK [3]. We also demonstrated that fluvastatin and simvastatin decrease the activation of ERK1/2 Akt [4]. These findings are in agreement with the results of the present study and indicate that

statins induce apoptosis via suppression of Ras/ERK and Ras/Akt pathways in our experimental model (Figure 5). Figure 5 Schematic representation of interacellular effects of statins in C6 glioma cells. As described above, statins are known to affect the

functions of Ras by inhibiting prenylation through the inhibition of GGPP synthesis; this enables localization of Ras at the plasma membrane [14, 15]. Ras is involved in the activation of the MEK/ERK and PI3K/Akt pathways [14, 16], suggesting the mechanism of action of statins. The treatment of C6 glioma cells with 5 μM mevastatin, 5 μM fluvastatin or 10 μM simvastatin for 72 h in vitro inhibited GGPP synthesis. PR-171 clinical trial We also found that the treatment of C6 glioma cells with 2.5 μM mevastatin, 1 μM fluvastatin or 5 μM simvastatin for 72 h inhibited cell proliferation. The peak plasma concentrations of fluvastatin or simvastatin achieved with standard doses were ≤ 1 μM or 2.7 μM, respectively [17, 18]. It has been reported that peak plasma concentration of fluvastatin achieved with high dose were ≤ 2 μM [19]. These findings indicate that 2 μM and 2.5 μM of fluvastatin and simvastatin, respectively, are within the peak plasma values of fluvastatin or simvastatin that are likely to be achieved in vivo. In addition, we found that 2.5 μM fluvastatin induced the apoptosis. Therefore, fluvastatin may be potentially useful as anti-cancer agents in the treatment of glioblastoma. Conclusion In conclusion, these results provide evidence of the specific molecular pathways via which statins induce apoptosis by increasing the activation of caspase-3 through inhibition of Ras/ERK and Ras/Akt pathways.

Cellular targeting efficiency of HA-MRCAs The targeting efficiency of HA-MRCAs was examined by MR imaging of breast carcinoma cell line MDA-MB-231 cells (high CD44 expression) and MCF-7 cells (low CD44

expression). First, target cells (1.0 × 107 cells) were harvested and washed three times with blocking buffer (FBS (0.2%) and NaN3 (0.02%) in phosphate-buffered solution (pH 7.4, 10 mM)) to inhibit non-specific binding effects. The solutions containing HA-MRCAs were applied to Selleck Adriamycin each cell line (1 and 0.5 μg, respectively) at 4°C for 30 min. The cells were then washed with blocking buffer three times to remove non-binding HA-MRCAs. Next, 200 μL of 4% paraformaldehyde was added to re-suspend the cells. After targeting efficiency was analyzed via MRI, the cells were dissolved in nitric acid for 2 h

at 180°C, and the concentrations of magnetic nanocrystals (Fe + Mn) were measured using inductively coupled plasma atomic emission spectrometry (ICP-AES). MR imaging procedures We performed in vitro MR imaging experiments with a 1.5-T clinical MRI instrument with a micro-47 surface coil (Intera, Philips Medical Systems, Best, The Netherlands). The T2 weights of the A-MNC- and HA-MRCA-treated cells (MDA-MB-231 and MCF-7 cells) were measured by the Carr-Purcell-Meiboom-Gill (CPMG) sequence at room temperature with the following parameters: TR = 10 s, 32 echoes with 12-ms even echo space, number of acquisitions = 1, point resolution of Crizotinib VDA chemical 156 × 156 μm, and section thickness of 0.6 mm. For acquisition of T2-weighted MR images of A-MNC- and HA-MRCA-treated cells, the following parameters were adopted: resolution of 234 × 234 μm, section thickness of 2.0 mm, TE = 60 ms, TR = 4,000 ms, and number of acquisitions = 1. Results and discussion Characterization of aminated P80 MNCs, soluble in non-polar organic solvent with high monodispersity, were made using the thermal decomposition method to serve as MR contrast agents. For the identification of optimal HA density for efficient CD44-overexpressed breast cancer cell imaging and phase transference of

hydrophobic MNCs into aqueous phase, the tri-hydroxyl groups of polysorbate 80 (P80) were modified with amine groups using spermine and the cross linker, 1,1′-carbonyldiimidazole (CDI) [32]. CDI was used to activate hydroxyl groups of P80 and generate reactive imidazole carbamate intermediates. When the amine group of spermine attacked the intermediate, imidazoles were released, and stable tri-urethane (N-alkyl carbamate) linkages were fabricated. After conjugation, the characteristic bands of aminated P80 were verified by FT-IR spectra, which represented N-H stretching of an amine group (3,550 cm−1), C-N stretching of an amide group (3,400 cm−1), and N-H bending of an amine group (1,600 cm−1) (Additional file 1: Figure S1).

Direction

of microbiological MI-503 manufacturer processes The study of microbiological processes in the soil allows deeper analysis of changes in the structure of soil and biotic system. The focus of microbiological processes was determined using the mineralization coefficient, which permits to characterize the intensity of mineralization processes and oligotrophic index of microbial communities. It was noted that the intensity of mineralization processes was higher in variants with colloidal solution of nanoparticles of molybdenum. It should be noted that this tendency was observed in both variants with CSNM application (3.93 to 1.94). The intensity had decreased in the flowering stage, but still the figure in experimental variants was higher than in the control (1.75 to 1.35) (Figure 1). The oligotrophic index of soils in variants with application of CSNM and microbial preparation was lowest (0.16) indicating the optimal conditions for the formation of soil microcoenosis. At this, the significant increase of number of oligotrophic microorganisms developed due to the minimal amount of organic matter in the soil and typical for the last stages of mineralization is of big interest. Thus, the oligotrophic index of soil during the flowering stage was two times higher and reached 1.35 (Figure 2). Doubling of oligotrophic

index had reflected the changes in the structure of soil microbial coenosis. Figure RXDX-106 in vitro 1 Performance orientation of microbial processes in those rhizosphere soil of chickpea plants. Plant emerging stage: (1) Control (water treatment), (2) colloidal solution of nanoparticles of molybdenum (CSMN), (3) microbial preparation, (4) microbial preparation + CSMN. Figure 2 Performance orientation of microbial processes in rhizosphere soil of chickpea

plants. Plant flowering stage: (1) Control (water treatment), (2) colloidal solution of nanoparticles of molybdenum (CSMN), (3) microbial preparation, (4) microbial preparation + CSMN. The application of colloidal solution of nanoparticles of molybdenum had enhanced the development of almost all groups of microorganisms two to three times relative to the control, mainly due to bacteria that metabolize mineral nitrogen, associative nitrogen fixation and associative oligotrophic microorganisms, that was also confirmed by the mineralization and oligotrophic indices. The application of CSNM in combination with bacterial preparation had a positive effect on the rate of transformation of organic matter, which increased threefold compared to that of the control, followed by the enhancement of mineralization processes and oligotrophic rates, indicating the improvement of trophic regime of the soil.

PubMedCrossRef 8. Li PL, Hwang I, Miyagi H, True H, Farrand SK: Essential components of the Ti plasmid trb system, a type IV macromolecular transporter. J Bacteriol 1999,181(16):5033–5041.PubMed

find more 9. Christie PJ: Type IV secretion: intercellular transfer of macromolecules by systems ancestrally related to conjugation machines. Mol Microbiol 2001,40(2):294–305.PubMedCrossRef 10. Hofreuter D, Odenbreit S, Haas R: Natural transformation competence in Helicobacter pylori is mediated by the basic components of a type IV secretion system. Mol Microbiol 2001,41(2):379–391.PubMedCrossRef 11. Christie PJ, Atmakuri K, Krishnamoorthy V, Jakubowski S, Cascales E: Biogenesis, architecture, and function of bacterial type IV secretion systems. Annu Rev Microbiol 2005, 59:451–485.PubMedCrossRef 12. Christie PJ, Vogel JP: Bacterial type IV secretion: conjugation systems adapted to deliver effector molecules to host cells. Trends Microbiol 2000,8(8):354–360.PubMedCrossRef 13. Hofreuter D, Odenbreit S, Henke G, Haas R: Natural competence for DNA transformation in Helicobacter pylori: identification and genetic characterization of the

comB locus. Mol Microbiol 1998,28(5):1027–1038.PubMedCrossRef 14. Lawley TD, Klimke WA, Gubbins MJ, Frost LS: F factor conjugation is a true type IV secretion system. FEMS Microbiol Lett 2003,224(1):1–15.PubMedCrossRef 15. Marra A, Blander SJ, Horwitz MA, Shuman HA: Identification of a Legionella pneumophila locus required for intracellular multiplication in human macrophages. Proc Natl Acad Sci USA 1992,89(20):9607–9611.PubMedCrossRef L-gulonolactone oxidase 16. Zamboni DS, McGrath S, Rabinovitch M, Roy CR: Coxiella burnetii express type IV secretion Doxorubicin order system proteins that function similarly to

components of the Legionella pneumophila Dot/Icm system. Mol Microbiol 2003,49(4):965–976.PubMedCrossRef 17. Juhas M, Crook DW, Dimopoulou ID, Lunter G, Harding RM, Ferguson DJ, Hood DW: Novel type IV secretion system involved in propagation of genomic islands. J Bacteriol 2007,189(3):761–771.PubMedCrossRef 18. Kurenbach B, Bohn C, Prabhu J, Abudukerim M, Szewzyk U, Grohmann E: Intergeneric transfer of the Enterococcus faecalis plasmid pIP501 to Escherichia coli and Streptomyces lividans and sequence analysis of its tra region. Plasmid 2003,50(1):86–93.PubMedCrossRef 19. Lipps G: Plasmids and viruses of the thermoacidophilic crenarchaeote Sulfolobus. Extremophiles 2006,10(1):17–28.PubMedCrossRef 20. Alvarez-Martinez CE, Christie PJ: Biological diversity of prokaryotic type IV secretion systems. Microbiol Mol Biol Rev 2009,73(4):775–808.PubMedCrossRef 21. Cascales E, Christie PJ: Definition of a bacterial type IV secretion pathway for a DNA substrate. Science 2004,304(5674):1170–1173.PubMedCrossRef 22. Segal G, Russo JJ, Shuman HA: Relationships between a new type IV secretion system and the icm/dot virulence system of Legionella pneumophila. Mol Microbiol 1999,34(4):799–809.PubMedCrossRef 23.

Then, cells were stimulated again with Lr1505 or Lr1506 in the presence or absence of blocking anti-TLR2 or anti-TLR9 antibodies (Figure 5A). When analyzing cytokines transcripts in PIE cells, it was evident that neither TLR2 nor TLR9 were involved in the up-regulation of type I IFNs induced by Lr1505 and Lr1506. In contrast, in the presence of anti-TLR2

blocked the increase of IL-6 and TNF-α transcripts induced by Lr1505 and Lr1506 in PIE cells (Figure 5A). In addition, anti-TLR2 antibodies significantly blocked the increase of IL-1β, IL-6, IFN-γ, and IL-10 transcripts induced by Lr1505 and Lr1506 in PPs adherent cells while anti-TLR9 antibodies did not modified the Selleck HM781-36B immunomodulatory activities of lactobacilli (Figure 5A). We confirmed the involvement of TLR2 but not TLR9 in the activation of PPs adherent cells using flow cytometry. In CD172a+CD11R1−, CD172a−CD11R1low and CD172a+CD11R1high adherent cells the addition of anti-TLR2 significantly reduced the capacity of both Lr1505 and Lr1506 to up-regulate Cisplatin nmr the expression of MHC-II, CD80/86, IL-1β, IL-6, IFN-γ, and IL-10 (Figure 5B). Figure 5 Role of toll-like

receptor (TLR)-2 and TLR9 in the immunoregulatory effect of immunobiotic lactobacilli in porcine intestinal epithelial (PIE) cells and antigen presenting cells (APCs) from Peyer’s patches. Monocultures of PIE cells or adherent cells from Peyer’s patches were stimulated with Lactobacillus rhamnosus CRL1505 (Lr1505) or L. rhamnosus CRL1506 (Lr1506) with or without the addition of anti-TLR2 or anti-TLR9 blocking antibodies. The mRNA expression of IFN-α, IFN-β,

IL-6, MCP-1 and TNF-α was studied in PIE cells after 48 hours of stimulation (A). The mRNA expression of IFN-α, IFN-β, IL-1β, TNF-α, IFN-γ, IL-6, IL-2, IL-12, IL-10 and TGF-β was studied in adherent cells after 12 hours of stimulation (A). Cytokine mRNA levels were calibrated by the swine β-actin level and normalized by common logarithmic transformation. In addition, expression of MHC-II and CD80/86 molecules as well as intracellular levels of IL-1β, IL-10, IFN-γ and IL-10 (B) were studied much in the three populations of APCs within adherent cells defined with CD172a and CD11R1 markers. Values represent means and error bars indicate the standard deviations. The results are means of 3 measures repeated 4 times with independent experiments. The mean differences among different superscripts letters were significant at the 5% level. Finally we evaluate the role of TLR2 and TLR9 in the modulation of the response against poly(I:C) challenge induced by lactobacilli (Figure 6A). Again, anti-TLR2 antibodies blocked the increase of IL-6 and TNF-α transcripts induced by Lr1505 and Lr1506 in PIE cells while no modification was observed for type I IFNs mRNA expression (Figure 6A).

Search strategy and study selection Studies were included in the review if: 1. click here a cross-sectional or longitudinal design was used;   2. the study population concerned patients

with somatic diseases or complaints at inclusion;   3. illness perceptions were measured using a questionnaire that contained at least four dimensions of the CSM-model of self-regulation such as identity of the illness, beliefs about cause of the illness and about how long it will last, beliefs about personal consequences of the condition, and/or beliefs about personal control; and,   4. the study used work participation as an outcome of interest, including employment status (employed versus not employed, sick listed or work disabled), return to work or days absent from work.   In the first round, two investigators independently reviewed all titles and abstracts of the identified publications and excluded all studies that did not fulfill one or more selection criteria. If the abstract

was non-informative but potentially relevant, the full text article was read. In the second round, full text articles were ordered and studies were selected if they fulfilled all four criteria. Selection was performed independently by two reviewers. Data extraction and study quality Data extraction was performed by one reviewer and checked by another and was performed using a checklist that included items on social demographic characteristics of the study population (age, gender, diagnosis or somatic diseases or complaints and employment status), sample size, outcome measures concerning www.selleckchem.com/products/MDV3100.html work participation, duration of follow-up and results of the most important illness perception categories reported in the studies obtained from the descriptive analyses or regression analyses. Study quality was independently assessed by two reviewers using a methodology

checklist from NICE (National D-malate dehydrogenase Institute for Health and Clinical Excellence) adapted from Hayden et al. (2006) to assess whether key study information was reported and the risk of bias was minimized (scoring yes, no or unclear), based on the following topics: (a) study sample representativeness (description key characteristics, source population, sampling and recruitment methods), (b) loss to follow up/response rate (description of: rate of drop outs and reasons, loss to follow up and reasons, differences in key characteristics), (c) measurement of illness perceptions/dimensions (valid and well defined, used well-developed measurement tool to measure factor of interest), (d) measurement of work participation (well defined, methods for assessing outcome are valid and reliable) (e) accounting for potential confounders (confounders are described, measured and accounted for in analyses). The quality scores will be presented and discussed separately. A full description of all items is available from the authors. Only items fulfilling a criterion received a plus (“yes”) score.

eutropha system, was indeed able to bind the cofactor precursor with the cyano- and carbonyl ligands bound to a Fe atom, thus assigning a key role to this protein in the incorporation of the cofactor into hydrogenase [20]. In the same Selleckchem Dinaciclib system, the existence of HoxL-HoxG and HypC-HoxV complexes was inferred from SDS-PAGE analysis of proteins obtained in co-purification experiments [20]. The data from immunoblot analysis under native conditions and from mass spectrometry analysis presented here provide a direct evidence of the existence of two such complexes

in R. leguminosarum: a major HupL-HupF complex and a much less abundant one involving HupF and HupK. The high recovery of HupL with HupFST points towards a strong interaction between both proteins in the ΔhupD mutant, where the NiFe cofactor is supposed to be inserted into HupL but the protein is still unprocessed. In this situation HupF is firmly attached to unprocessed HupL, and we hypothesize that this immature protein might require the oxygen-protective function of HupF to protect the labile NiFe cluster prior to proteolytic processing, when the protein is still in an open conformation. Following the model described for the R. eutropha system [24] we propose that R. leguminosarum proteins in these complexes

interact to transfer the iron-containing hydrogenase cofactor precursor from HupK to HupL, CB-839 datasheet prior to the final HupD-mediated proteolytic step. But HupF protein also Adenosine triphosphate contributes to the stability of hydrogenase large subunit at high oxygen tensions. Data from experiments performed in a ΔhupS background indicate that HupF is not bound to HupL after HupD-mediated proteolytic processing (our unpublished results), indicating that mature HupL is stable enough to not require any additional chaperones, as suggested also by the results on stability of mature enzyme under 21% O2 presented in this paper. This model might not be the only possibility for the biosynthesis of oxygen-tolerant hydrogenases, since recent evidences indicate that hydrogenase-1 from this E. coli is an oxygen-tolerant hydrogen uptake

hydrogenase [37], and neither HupF- nor HupK-like proteins are present in this bacterium. Previous data from our lab and from other laboratories suggest that adaptations to the presence of oxygen also exist for the synthesis of hydrogenase small subunit HupS through the participation of HupGHIJ proteins or their homologues [19, 38]. In the case of endosymbiotic bacteria, such as R. leguminosarum, the synthesis of hydrogenase under the ultra-low oxygen tensions prevalent in symbiotic conditions is less severely dependent on such auxiliary proteins [19]. The low, although significant, levels of hydrogenase activity detected in bacteroids induced by the ΔhupF mutant, but not in vegetative cells, might indicate that for R.

Then, the cells were harvested by centrifugation, washed twice in PBS (pH 7.2), re-suspended in RPMI 1640 medium (buffered to a pH of 7.0 with 0.165 M morpholinepropanesulfonic acid), and counted after serial dilution by a hemocytometer. Human serum Human serum (HS) was pooled from healthy blood donors, and heat-inactivated serum was prepared by heating at 56°C for 30 min. Proteinase K-treated serum was prepared by incubating with 50 mg/mL proteinase K at 58°C for 1 h

followed by incubation at 85°C for 1 h to inactivate the protease. All fractions were filter-sterilized (0.22-mm pore size filter). Biofilm formation Fungal biofilms were prepared as described on commercially available, pre-sterilized, flat-bottomed 96-well Galunisertib research buy polystyrene microtiter plates (Corning) [39]. Briefly, a cell suspension of 1.0 × 106 cells/ml was prepared in RPMI 1640 and RPMI

1640 + 50%, 10%, 5% or 3% HS. From those suspensions, 100 μl was introduced into wells and incubated at 37°C for 24 h without agitation, which allowed the cells to attach to the surface of the plate and form the biofilm structure. To investigate the effect of HS on pre-adhered biofilms, C. albicans biofilms were prepared for 90 min (the adhesion phase) at 37°C as described above. The wells were washed twice with PBS to remove loosely adherent cells. Then, fresh RPMI 1640 (100 μl), containing different concentrations (3–50%) of HS were added and the plate was further incubated for 24 h at 37°C. RPMI 1640 medium without HS was included in control wells. The metabolic activity of the C. albicans Protease Inhibitor Library solubility dmso biofilms was determined quantitatively using XTT reduction assay. Dynamic monitoring of the adhesion process Standard cell suspension of C. albicans was prepared in RPMI1640 or RPMI1640 containing different concentrations selleck kinase inhibitor (3% to 50%) of HS, and 100 μl of those suspensions was introduced into 96-well polystyrene microtiter plates. After standing for 3 min, the plates were placed on Live Cell Movie Analyzer (JuLI™ Br., NanoEnTek Inc., Seoul, Korea) and incubated at 37°C. The instrument was set to continuous photographing mode with exposure 5%, brightness 13%, zoom level 4, interval 1 min, and total time 2 h (the experimental

group was prolonged to 3 h). When it was finished, a total of 121 or 181 photos were obtained for the control and experimental groups, respectively. Then, those pictures were played back in rapid succession to observe the dynamic changes of the fungal cells (playing at a speed of 10 frames/s). Quantitation of biofilms At the end of the incubation, the supernatant was aspirated and the wells washed twice with PBS. The quantitation of biofilms was determined using 2,3-bis (2-methoxy-4-nitro-5-sulfo-phenyl)-2H-tetrazolium-5-carboxanilide (XTT) reduction assay that measures the activity of mitochondrial dehydrogenase [40]. XTT solution (1 mg/ml) was prepared by dissolving XTT powder (Sigma, Shanghai, China) in PBS, and the solution was filter-sterilized (0.22-mm pore size filter).

The scanning electron microscope (SEM) pictures of

the molten salt and nanofluids and corresponding energy dispersive spectrometer (EDS) are shown in Figure 2. Figure 2a,b shows the SEM images for the molten salt under two different magnifications (×5,000 and × 30,000), and Figure 2c is the EDS analysis results at the scanned area outlined in Figure 2b. The EDS results confirm the SCH772984 research buy chemical composition of the molten salt (60-wt.% NaNO3 and 40-wt.% KNO3). The Pt peak in Figure 2c is from the Pt coating for taking the SEM images while the C peak in Figure 2c is from the carbon paste for SEM sample preparation. Figure 2d,e,g,h,j,k shows the SEM images of the nanofluids containing 13-nm alumina NPs at 0.9, 2.7, and 4.6 vol.%, respectively, under the two different magnifications. Meanwhile, Figure 2f,i,l shows the EDS analysis results at the scanned areas outlined at Figure 2e,h,k. Furthermore, Figure 2m,n,p,q,s,t

shows the SEM images of the nanofluids containing 90-nm alumina NPs at 0.9, 2.7, and 4.6 vol.%, respectively, under the two different magnifications. The chemical composition of alumina NPs could RXDX-106 chemical structure be verified by the EDS results shown in Figure 2f,i,l,o,r,u. It is worth noting that the aggregation of NPs was found in the nanofluids when they are in solid state. Meanwhile, the sizes of the clusters formed from the Thiamet G aggregated NPs for the nanofluids in solid state are on the order of 1 μm (see Figure 2d,g,j,m,p,s). Figure 2 SEM images and EDS results. (a,b) molten salt (×5,000 and × 30,000, respectively); (d,e) molten salt-based nanofluid containing 13-nm alumina NPs at 0.9 vol.% (×5,000 and × 30,000, respectively); (g,h) molten salt-based nanofluid containing 13-nm alumina NPs at 2.7 vol.% (×5,000 and × 30,000, respectively); (j,k) molten salt-based nanofluid containing 13-nm alumina NPs at 4.6 vol.% (×5,000 and × 30,000, respectively); (m,n) molten salt-based nanofluid containing 90-nm

alumina NPs at 0.9 vol.% (×5,000 and × 30,000, respectively); (p,q) molten salt-based nanofluid containing 90-nm alumina NPs at 2.7 vol.% (×5,000 and × 30,000, respectively); (s,t) molten salt-based nanofluid containing 90-nm alumina NPs at 4.6 vol.% (×5,000 and × 30,000, respectively), and (c,f,i,l,o,r, and u) EDS analysis results at the scanned areas. Figure 3 shows the images of the nanofluids in their liquid state. The images were taken from an optical microscope (OM) with a × 600 magnification when heating the nanofluids at 300°C (the melting point of the molten salt is about 222°C). Figure 3a,c shows the OM images of the nanofluids containing 13-nm alumina NPs at 0.9, 2.7, and 4.6 vol.%, respectively. Meanwhile, Figure 3d,f show the OM images of the nanofluids containing 90-nm alumina NPs at 0.9, 2.7, and 4.6 vol.%, respectively.