01; b) T lim with selleck compound NaHCO3 (solid line) and placebo (dashed line) on the 5 days of testing are presented as group mean ± SD (n = 8). The NaHCO3 intervention resulted in a significantly higher [HCO3 -]

relative to placebo (F (1,7) = 118.71, P < 0.001, ηp 2 = 0.94; MK-4827 manufacturer Table 1). [Na+] increased after NaHCO3 (F (1,7) = 12.44, P = 0.012, ηp 2 = 0.68) but remained constant with placebo supplementation. [Na+] did not significantly change over time (F (1,7) = 0.49, P = 0.509, ηp 2 = 0.08) with either condition. The mean ABE were significantly higher during the NaHCO3 Selleck LDN-193189 compared to the placebo trials (F (1,7) = 100.42, P < 0.001, ηp 2 = 0.94), but not between days of testing (F (1,7) = 0.01, P = 0.920, ηp 2 = 0.00). Blood pH was increased with NaHCO3 supplementation (F (1,7) = 42.04, P < 0.001, ηp 2 = 0.86), showing no change between the testing days (F (1,7) = 1.11, P = 0.327, ηp 2 =

0.14). There was a main effect for a PV increase during interventions (F (1,7) = 19.22, P = 0.003, ηp 2 = 0.73; Table 1) and days of testing (F (1,7) = 18.12, P = 0.004, ηp 2 = 0.72), as well as a significant intervention x time interaction (F (1,7) = 22.05, P = 0.002, ηp 2 = 0.76). Table 1 [HCO 3 - ], [Na + ], ABE, pH and PV 75 min after supplement ingestion on the first and the fifth day of testing with either NaHCO 3 or placebo supplementation   NaHCO3 Placebo   Day 1 Day 5 Day 1 Day 5 [HCO3 -] (mmol &z.ccirf;l-1) 32.4 ± 1.8*** 32.6 ± 2.7*** 26.4 ± 1.8 26.0 ± 1.1

[Na+] (mmol &z.ccirf;l-1) 142.1 ± 3.9* 142.4 ± 3.0* 138.1 ± 1.2 139.3 ± 5.5 ABE (mmol &z.ccirf;l-1) 8.4 ± 1.7*** 8.3 ± 2.3*** 2.7 ± 1.7 2.0 ± 0.9 pH 7.49 ± 0.02*** 7.48 ± 0.02*** 7.44 ± 0.02 7.43 ± 0.02 PV (%) 55.5 ± 2.3 62.6 ± 3.8†† 56.0 ± 1.7 55.9 ± 3.3 Values are mean ± SD (n = 8). [HCO3 -], blood bicarbonate concentration; [Na+], blood sodium concentration; ABE, actual base excess; PV, plasma volume. *P < 0.05, *** P < 0.001 relative to placebo at the same time point; †† P < 0.01 relative to day 1. The NaHCO3 ingestion resulted in a significant intervention x time interaction for total lean body Apoptosis inhibitor mass (F (1,7) = 7.77, P = 0.027, ηp 2 = 0.53; Table 2). In addition, total lean body mass raised over the five consecutive testing days in both conditions (F (2,14) = 10.97, P = 0.001, ηp 2 = 0.61; Table 2). Lean soft tissue mass of the legs did not change neither during the interventions (F (1,7) = 3.16, P = 0.119, ηp 2 = 0.31) nor across the days of testing (F (2,14) = 1.38, P = 0.283, ηp 2 = 0.17; Table 2). Table 2 Total lean body mass and lean soft tissue mass of the legs on the different days of testing with either NaHCO 3 or placebo ingestion   NaHCO3 Placebo   Day 1 Day 3 Day 5 Day 1 Day 3 Day 5 Total lean soft tissue (kg) 60.7 ± 4.8 61.7 ± 5.3*†† 62.0 ± 5.3*†† 60.5 ± 5.3 61.3 ± 5.4†† 60.6 ± 5.

SP conceived the low temperature deposition of SiNWs idea and their exploitation into devices. He supervised the work and reviewed the manuscript. All authors read and approved the final manuscript.”
“Background Electrochemical anodizing of bulk crystalline silicon (Si) at specific conditions causes the formation of chaotic or ordered pore channels in its volume [1]. The material formed by such artificial nanostructuring is called porous

silicon (PS). This porous morphological type of silicon presents an object of great interest of the scientific community because, in contrast to the bulk silicon, it demonstrates a number of peculiarities such as extremely developed surface, photo- and electroluminescence, and biocompatibility. Possession of these properties makes PS applicable to the areas selleck chemicals of optoelectronics and display technologies, micromechanical systems, biomedicine, etc. The challenge to develop and engineer novel devices and technologies based on PS forces researchers to actively seek methods to control and manage the PS properties. One way to realize it is the incorporation of metal nanoparticles (NPs) into the pores of PS by deposition from wet solutions. Unlike dry methods (evaporation or sputtering), wet deposition provides deep penetration of metal atoms into pore channels [2]. Moreover, wet Capmatinib concentration technologies are characterized by simplicity and low cost. Immersion deposition presents a less

complicated wet method of PS metallization. In contrast to electrochemical and chemical depositions, in this process, a source of the electrons for metal atoms reduction is PS itself. In aqueous solutions, the ions of metals,

which have redox potential greater than hydrogen, attract electrons from Si atoms and are reduced to the atomic form [3]. The immersion deposition of other metals can be carried out by the use of alkaline solutions [4]. During wet deposition, metal structures tend to grow as island films according to IKBKE the Volmer-Weber mechanism [5]. Penetration of metals into PS may be easily controlled by the alternation of PS porosity [6]. Therefore, it is possible to fabricate metal films on the outer surface of PS or metal/PS nanocomposites (NCs). Obviously, during the immersion process, the Si skeleton of PS is oxidized, and SiO2 is formed under deposited metal structures [3, 7]. The oxide’s interlayer prevents further redox reactions between Si and metal ions, and as a result, there reduction of metal stops. Epigenetics inhibitor Usually, to avoid the effect of oxidation, immersion deposition in the presence of fluoride species is performed [8, 9]. In this case, SiO2 removal followed by Si oxidation caused the dissolution of the PS skeleton. Proper conditions of the metal immersion deposition and PS parameters can lead to the complete conversion of PS to porous metal [10]. The structures formed by immersion deposition of metals on PS are widely studied to be successfully applied in some technologically important areas [11–15].

PSMB9, encoded in the major histocompatibility complex class II region, is another gene inducible by both Type I and II IFNs and is a constituent of the immunoproteosome [37–39]. This gene facilitates a link between the innate and adaptive immune response since

site directed mutagenesis studies have revealed a role for PSMB9 in antigen processing and presentation [40]. PSMB9 was the only ISG that was expressed at significantly see more higher levels in DBA/2 mice at both day 10 (Additional file 1: Figure S3A) and 14 (Figure 7), which click here suggests that the protein product of this gene may play a key role in resistance to C. immitis infection. IRGM1 is particularly noteworthy since it belongs to a family of immunity-related GTPases Selleckchem Ulixertinib whose other members, IRGM2 and IRGM3 (or IGTP), were also expressed to a greater extent in resistant DBA/2 compared to susceptible C57BL/6 mice (Figure 2). IRGM1-deficient mice are more susceptible to infection with Mycobacterium tuberculosis, M. avium, Listeria monocytogenes and Salmonella enterica serovar Typhimurium, as assessed by both mouse survival and bacterial loads in tissues, whereas IRGM3-deficient mice exhibit normal resistance [41, 42]. In contrast, both IRGM1 and 3 are required

for IFN-γ modulated control of Toxoplasma gondii in murine macrophages [43]. It appears that IRGM1 is critical for normal motility of activated macrophages in mouse models suggesting a pivotal role for this protein in the innate response to infection in vivo[44]. The relevance of the IRGM family to human coccidioidomycosis is unclear because the single gene in this family in humans, IRGM, is considerably truncated and is not regulated triclocarban by IFN-γ [41]. However, IRGM does play a role in human innate immunity since it is necessary for the execution of the autophagic pathway in macrophages and the control of intracellular Mycobacteria[45]. Greater expression of IFNG and IL17A were detected in DBA/2 mice at day 15 post-infection using

the Mouse Common Cytokines Gene Array (Additional file 1: Figure S2). It was therefore surprising that microarray analysis did not detect differential expression of these cytokines between mice strains at days 14 and 16 (Figures 2 and 3), but RT-qPCR analysis was able to do so (Figure 7 and Additional file 1: Figure S3). It is unclear why microarray analysis was unable to detect the expression of these cytokines especially since IFNG expression had been detected using the same array platform (MGU74Av2) in lung tissue from C57BL/6 mice exposed to lipopolysaccharide (LPS) [46]. This array platform was designed using the C57BL/6 genome and thus it is possible that these cytokines were not detected because they were not expressed to high levels in C57BL/6 by C.

J Mater

Chem 2004, 14:2575–2591. 35. Zgura I, Beica T, Mitrofan IL, Mateias CG, Pirvu D, Patrascu I: Assessment of the impression materials by investigation of the hydrophilicity. Dig J Nanomater Biostruct 2010, 5:749–755. 36. Gao M, Liu J, Sun H, Wu X, Xue D: Influence of cooling rate on optical properties and electrical properties of nanorod ZnO films. J Alloys Compd 2010, 500:181–184.CrossRef 37. Tiana Q, Li J, Xie Q, Wang Q: Morphology-tuned synthesis of arrayed one-dimensional ZnO nanostructures from Zn(NO 3 ) 2 and dimethylamine borane solutions and their photoluminescence and photocatalytic properties. Mater Chem Phys 2012, 132:652–658. 38. Tam KH, Cheung CK, Leung YH, Djurisic AB, Ling CC, Beling CD, Fung S, Kwok WM, Chan WK, Phillips DL, Ding L, Ge WK: Defects in ZnO nanorods prepared by a hydrothermal Syk inhibitor method. J Phys Chem LY294002 supplier B 2006, 110:20865–20871. 39. Li D, Leung YH, Djurisic AB, Liu ZT, Xie MH, Shi SL, Xu SJ, Chan WK: Different origins of visible luminescence in ZnO nanostructures fabricated by the chemical and evaporation methods. Appl Phys Lett 2004, 85:1601–1603.CrossRef 40. Zhou H, Alves H, Hofmann DM, Kriegseis W, Meyer BK, Kaczmarczyk G, Hoffmann A: Behind the weak excitonic emission if ZnO quantum dots: ZnO/Zn(OH) 2 core-shell structure. Appl Phys Lett 2002, 80:210–212.CrossRef 41. Khoang ND, Hong HS, Trung DD, Van Duy N, Hoa ND, Thinh DD, Van Hieu N: On-chip growth of wafer-scale planar-type ZnO nanorod sensors

for effective detection of CO gas. Sensor Actuat B 2013, 181:529–536.CrossRef 42. Tulliani JM, Cavalieri A, Musso S, find more Sardella E, Geobaldo F: Room temperature ammonia

sensors based on zinc oxide and functionalized graphite and multi-walled carbon nanotubes. Sensor Actuat B 2011, 152:144–154.CrossRef 43. Yang MZ, Dai CL, Wu CC: A zinc oxide nanorod ammonia microsensor integrated Bacterial neuraminidase with a readout circuit on-a-chip. Sensors 2011, 11:11112–11121.CrossRef 44. Watson J: The tin oxide gas sensor and its applications. Sensor Actuat B 1984, 5:29–42. 45. Nanto H, Minami T, Takata S: Zinc-oxide thin-film ammonia gas sensors with high sensitivity and excellent selectivity. J Appl Phys 1986, 60:482–484.CrossRef 46. Verplanck N, Coffinier Y, Thomy V, Boukherroub R: Wettability switching techniques on superhydrophobic surfaces. Nanoscale Res Lett 2007, 2:577–596.CrossRef 47. Autumn YA, Liang ST, Hsieh W, Zesch WP, Chan TW, Kenny R, Fearing RJ: Full, adhesive force of a single gecko foot-hair. Nature 2000, 405:681–685.CrossRef 48. Geim K, Dubonos SV, Grigorieva IV, Novoselov KS, Zhukov AA, Shapoval SY: Microfabricated adhesive mimicking gecko foot-hair. Nat Mater 2003, 2:461–463. 49. Jin M, Feng X, Feng L, Sun T, Zhai J, Li T, Jiang L: Superhydrophobic aligned polystyrene nanotube films with high adhesive force. Adv Mater 2005, 17:1977–1981.CrossRef 50. Hong X, Gao X, Jiang L: Application of superhydrophobic surface with high adhesive force in no lost transport of superparamagnetic microdroplet. J Am Chem Soc 2007, 129:1478–1479.

Entire dried shoots were ground and processed for carbon isotope analysis at the UC Davis Stable Isotope Facility (http://​stableisotopefac​ility.​ucdavis.​edu/​). LWC (%) was this website calculated as 100 × (FW − DW)/DW. Mesophyll conductance

(Experiment 4) Arabidopsis seeds of ecotype Columbia and the abi4 mutant provided by the Arabidopsis Biological Resource Center (Columbus, OH, USA) were used for leaf mesophyll conductance to CO2 (g m) experiments. Seven replicates of each genotype were grown in a growth chamber in a randomized block design. Photoperiod was 12 h with 350 μmol m−2 s−1 PPFD and temperature was cycled 23/20 °C (light/dark). A LI-6400 (Li-Cor Inc., Lincoln, NE, USA) with whole-shoot Arabidopsis cuvette (Fig. 1) was coupled with online isotopic measurements of CO2 entering and leaving the shoot chamber to determine instantaneous carbon isotope discrimination and g m using TDL (Flexas Selleck CP-690550 et al. 2006; Barbour et al. 2007; Heckwolf et al. 2011). Calculations for

g m were based on whole-shoot gas exchange measurements at 350, 700, and 175 (μmol m−2 s−1) PPFD using the slope-based approach given in Evans et al. (1986). Shoots were harvested after gas exchange, leaf area was determined from rosette photographs using Scion Image (Scion Corporation, Frederick, MD, USA), and shoots were dried and weighed Protein Tyrosine Kinase inhibitor (DW). LWC (%) was calculated as above and SLA was calculated as rosette area/DW. Statistical analysis We analyzed phenotypic data for physiological traits using standard fixed effect ANOVAs with the Proc GLM in SAS (SAS Institute 1999). We estimated correlations Staurosporine among physiological traits as the standard Pearson product-moment correlation between genotype means. In the case of the TE experiment, we analyzed phenotypic data for physiological traits using a linear mixed model analysis with the Proc Mixed procedure in SAS (SAS

Institute 1999). We fit a model including accessions as a random effect and chamber, experiment, and their interaction as fixed effects. The variance component for the random effect was estimated using restricted maximum likelihood (REML) and assessments of significance were based on likelihood ratio tests (Little et al. 1996). We obtained empirical best linear unbiased predictors (BLUPs) associated with the random effects and consider these breeding values for each accessions. BLUPs are robust estimates of the impact of a particular accession on the measured trait while controlling for the fixed effects (chamber and experimental run). For TE, we fit a model that included both chamber and experimental run as a fixed effect. For δ13C, we fit a simpler model including accession as a random variable and experimental run as a fixed effect. In this case, factors associated with chamber could not be included because replicates within each experimental run were pooled for mass spectroscopy analysis. All subsequent analyses involving TE and δ13C rely on BLUP estimates.

J Proteome Res 2009, 8:5347–5355.PubMedCrossRef Authors’ contributions NH aided in experimental design and carried out the protein analyses, including 2-DE, https://www.selleckchem.com/products/17-DMAG,Hydrochloride-Salt.html 2-DLC-MS/MS and data analysis, and drafted the manuscript. NS and NBM undertook LC-MS and peptide mass mapping experiments and data analysis. NH and CHa performed phenotypic analyses. BR, CH, and

JM contributed to the coordination of the study and data interpretation. BC provided MS instrument-specific training see more and guidance on experimental design. SJC conceived the study, aided in the experimental design and, coordination, undertook data analysis and interpretation, and drafted the manuscript. All authors approved the final manuscript.”
“Background Many bacterial diseases, including urinary tract infections (UTIs) are initiated by microorganisms adhering to and colonizing the epithelium.

Epithelial cells of the urinary tract (urothelial cells) respond to pathogens by producing various immune activating substances including compounds that recruit immune cells such as macrophages. Epithelial cells express a number of different pattern recognition receptors such as toll-like receptors (TLRs) that are able to trigger the expression of inflammatory mediators and subsequent inflammation in the presence of pathogenic microbes. One of the most studied TLRs is TLR4, which binds lipopolysaccharides (LPS) found on the cell wall of Gram-negative bacteria [1]. Key proteins involved in inflammation are the Rel/Nuclear Factor (NF)-κB proteins, which once activated can induce the transcription CB-5083 mouse of several immunologically essential molecules, such as

tumor necrosis factor (TNF), interleukin (IL)-6 and CXCL8 [2–4]. These cytokines are very important in the antimicrobial and inflammatory process and they effectively Farnesyltransferase recruit immune cells to the infected site. In its inactive form, the NF-κB transcription factor is located within the cytosol, where inhibitory proteins masking the nuclear localization signal impair its nuclear migration. During NF-κB activation, the inhibitory proteins are disassociated from the transcription factor dimer, which is subsequently transported into the nucleus [5]. Nuclear translocation of NF-κB during infectious processes is important for the subsequent activation of immune responses. The most prevalent cause of UTI is uropathogenic Escherichia coli (UPEC), which expresses numerous virulence factors including toxins and fimbriae used for adhesion. Eukaryotic cells can identify pathogens, for example when type 1 fimbriae, P-pili, or LPS bind to TLR4 and elicit an inflammatory response, albeit via different intracellular pathways [6]. However, some UPEC are equipped with virulence factors that can block immune responses allowing the organisms to freely multiply.

0, containing 0 mM and 1 mM linoleic acid, 1% ethanol. The neat to 10-6 dilutions are as indicated. Shown are representative images from one of multiple experiments. (B) Graph showing the relative survival of S. aureus SH1000 and SH1000 derivates using data from Figure 5A. Colonies

were counted after overnight incubation. Error bars represent ± SEM. Results from multiple experiments were analysed with Student’s t test. Discussion and conclusion S. saprophyticus is a major cause of community-acquired UTI in young women. Knowledge of the virulence mechanisms of S. saprophyticus has advanced in recent years, particularly with the acquisition and analysis of whole genome selleck compound sequence data. The majority of acknowledged virulence factors of S. saprophyticus are proteins tethered to the cell surface, which

with the exception of the Ssp lipase [12], are all involved in adhesion: Aas is an autolysin Ulixertinib price that also binds to fibronectin [10]; UafA adheres to uroepithelial cells via an unidentified ligand [8]; SdrI binds to collagen I and fibronectin [9, 31] and UafB binds to fibronectin, fibrinogen and urothelial cells [7]. Here we have identified another cell wall-anchored protein produced by S. saprophyticus that we have termed SssF – the sixth surface protein described for this species. The sssF gene was identified in the sequence of ZD1839 the pSSAP2 plasmid of S. saprophyticus MS1146 due to the presence of the canonical LPXTG sortase motif in the translated protein sequence. A copy of the sssF gene is also located on the pSSP1 plasmid of S. saprophyticus ATCC 15305 (99% nucleotide identity; Figure Olopatadine 1), but it was not acknowledged as encoding an LPXTG motif-containing protein [8]. We recently characterised another plasmid-coded LPXTG motif-containing protein of S. saprophyticus MS1146, UafB, as an adhesin [7]. We first sought to investigate whether SssF was another adhesin, since a considerable proportion of characterised Gram-positive covalently surface anchored proteins have adhesive functions [32], including every other known S. saprophyticus LPXTG motif-containing protein. No evidence of an adhesion phenotype for SssF was

detected. SssF protein sequence searches with the BLAST database provided an output of uncharacterised staphylococcal proteins with a maximum 39% amino acid identity to SssF across the entire protein sequence, mostly annotated as hypothetical cell wall-anchored proteins. In contrast to S. saprophyticus, the genes encoding these SssF-like proteins are located on the chromosome, rather than on a plasmid, in every other sequenced staphylococcal species. Some of these staphylococcal SssF-like proteins contain atypical sortase motifs. At this stage it is not known whether all of these proteins are sorted to the cell surface efficiently, but SasF has been shown to be associated with the cell wall of S. aureus 8325-4 even with the non-classical LPKAG sortase motif [33].

Substitutions may occur on oligosaccharides that extend from any one of the three conserved inner-core heptose residues (heptose I, II, and III) or, alternatively, directly to heptose IV, an outer core heptose that extends from heptose I [34, 35]. These substitutions Vadimezan datasheet are dictated largely by the diphosphonucleoside choline transferase

encoded by the licD gene. Three licD gene alleles mediate ChoP substitutions at different positions within LOS and, for simplification, we have named the alleles to reflect their selleck kinase inhibitor association with a given heptose-residue: licD I , licD III , and licD IV . Although ChoP has been associated with heptose II residues in selected strains, a specific licD allele mediating these substitutions has not been experimentally documented [35]. The deduced LicD proteins are 265-268 amino acids in length and range in sequence identity from 74-88% with much of the variation occurring in the central part of the primary structure [28, 35]. Although most NT H. influenzae strains possess a single licD PF-4708671 solubility dmso allelic gene that facilitates one ChoP substitution, Fox et al [35] recently reported that 4/25 (16%) of NT H. influenzae middle ear strains possessed two different licD alleles, each present in a separate, phase-variable lic1 locus, that together could produce up to two ChoP substitutions in the strain’s LOS. Both

the number and position of ChoP substitutions within LOS may affect binding of host clearance molecules such as CRP or natural ChoP antibodies [26, 28]. For instance, H. influenzae strains with dual ChoP substitutions bind more CRP, and H. influenzae strains with ChoP substitutions positioned from the distal heptose III residue are

10-fold more sensitive to CRP-initiated bactericidal killing than ChoP associated with the proximal heptose I in the same strains [28, 35]. Consequently, strains with proximal ChoP substitutions (i.e. heptose I) may Amrubicin be more protected from CRP-mediated clearance, and LOS structural studies on selected NT H. influenzae strains have found that ChoP predominate at this position [34]. The overall prevalence of these substitutions in the NT H. influenzae population, however, is not known. Differences in the prevalence of single or combined licD gene alleles between NT H. influenzae and H. haemolyticus may reflect the importance of ChoP structures in NT H. influenzae virulence. The presence of a licA gene in H. haemolyticus suggests that it may contain a lic1 locus and express ChoP in a manner similar to H. influenzae [10]. Since ChoP expression among NT H. influenzae strains can vary greatly due to genetic factors listed above, we speculated that differences in the prevalence of these factors between strain populations of H. influenzae and H. haemolyticus may highlight, in part, which ones provide an advantage to H. influenzae in transcending from commensal to disease-related growth. Results ChoP expression in H. haemolyticus Although H.

Characterization and measurements The sample morphologies were examined by field emission scanning electron microscopy (FESEM) with a Hitachi S-4800 microscope (Dallas, TX, USA). The crystal structures of ZnO and ZnSe in the samples were characterized by X-ray diffraction (XRD) with a Rigaku D/MAX 2550 VB/PC X-ray diffractometer (Shibuya, Tokyo, Japan) using Ni-filtered Cu Kα radiation (λ = 0.15406 nm). Fourier-transform infrared (FTIR) spectroscopy and Raman

scattering spectroscopy were also used to characterize the structures of Gemcitabine ZnO and ZnSe through vibrational mode analysis and phase identification. FTIR spectroscopy was carried out with a Bruker Vertex 80 V spectrometer (Saarbrucken, SL, Germany). Raman measurements were performed with a Jobin-Yvon LabRAM HR 800 UV micro-Raman spectrometer (Villeneuve d’Ascq, France) using a 488-nm Ar+ laser beam or 325-nm He-Cd laser beam as the exciting INCB28060 concentration sources. The photoluminescence (PL) of the samples was measured by exciting the samples with 325-nm laser light from a continuous wave He-Cd laser at room temperature to examine the influences of the ZnSe shells on the luminescence from the ZnO cores. The luminescence was detected by an intensified charge-coupled device (ICCD) (iStar DH720, Andor Technology, Belfast, UK) after being dispersed by a 0.5-m spectrometer

(Spectra Pro 500i, Acton Research, Acton, MA, USA). The optical properties were also characterized by comparing the optical transparency of ZnO/ZnSe Gemcitabine supplier core/shell NRs with that of bare ZnO NRs. The transmission spectra of the bare ZnO NRs and

the ZnO/ZnSe core/shell NRs prepared on transparent fused silica plates were measured in the UV-near IR range using a Shimutsu UV3101PC Photo-Spectrometer (Nakagyo, Kyoto, Japan). Results and discussion Morphology The FESEM images in Figure 1 illustrate the morphologies of the samples. As shown in Figure 1a for sample A, the bare ZnO NRs grew almost vertically on the substrate, nearly in the shape of hexagonal prisms with a mean diameter of approximately 60 nm and an average length of approximately 1 μm. As will be described below, structural characterization reveals that the hydrothermally grown ZnO NRs are hexagonal wurtzite in crystal structure with P505-15 chemical structure preferentially c-axis-oriented growth. After the deposition of ZnSe whether at RT or at 500°C, the NRs increase in diameter with rough surfaces (Figure 1b,c), indicating the covering of the ZnO rods with ZnSe shells. However, the NRs in sample B show larger diameters and rougher surfaces than the NRs in sample C. The NRs in sample B are connected together at the rod tips and near the top surfaces, while those in sample C are generally separated from each other from the top to the bottom.