Synthesis of Au@Ag Core–Shell Nanocubes Containing Varying Shaped Cores and Their Localized Surface Plasmon Resonances

We have synthesized Au@Ag core–shell nanocubes containing Au cores with varying shapes and sizes through modified seed-mediated methods. Bromide ions are found to be crucial in the epitaxial growth of Ag atoms onto Au cores and in the formation of the shell’s cubic shape. The Au@Ag core–shell nanocubes exhibit very abundant and distinct localized surface plasmon resonance (LSPR) properties, which are core-shape and size-dependent. With the help of theoretical calculation, the physical origin and the resonance mode profile of each LSPR peak are identified and studied. The core–shell nanocrystals with varying shaped cores offer a new rich category for LSPR control through the plasmonic coupling effect between core and shell materials

Analysis of the Application Value of HPV mRNA and DNA Detection in Early Screening of Cervical Lesions - Supplementary material

Table 1 Positive rates of Aptima HPV and COBAS HPVTable 2 Age distribution of HPV 16Table 3 Age distribution of HPV 18Table 4 Age distribution of HPV other risk typesTable 5 Colposcopy examination of HPV 18Table 6 Colposcopy examination of HPV 16Table 7 Colposcopy examination of HPV other risk typesTable 8 Pathological biopsy of HPV 18Table 9 Pathological biopsy of HPV 16Table 10 Pathological biopsy of HPV other risk typesTable 11 Pathological biopsy of HPV 16 (≥CIN2)Table 12 Pathological biopsy of HPV 18 (≥CIN2)Table 13 Pathological biopsy of HPV other risk types (≥CIN2)</p

4,5-Cis Unsaturated α‑GalCer Analogues Distinctly Lead to CD1d-Mediated Th1-Biased NKT Cell Responses

The total synthesis of 4,5-cis unsaturated α-GalCer analogues was achieved, and their immune-response altering activity was assessed <i>in vitro</i> as well as <i>in vivo</i> in mice. Using glycosyl iodide as a glycosyl donor, construction of the sphingosine unit was shortened by four steps and single α-stereoselectivity was achieved in good yield (67%). With regard to the therapeutic use of α-GalCer, the novel analogues (<b>1b</b> and <b>1c</b>) distinctly induced a Th1-biased cytokine response, avoiding induction of a contradictory response and overstimulation

Supplementary document for Programmable Photoacoustic Manipulation of Microparticles in Liquid - 6946175.pdf

Supplemental documen

Double mutant cycle analysis for His33 and Ser345.

<p>(A) Mutant cycle analysis shows free energy changes between H33C and S345C. (B) Mutant cycle analysis shows free energy changes between V48C and I328C. (C) Mutant cycle analysis shows free energy changes between H33A and S345A. (D) Mutant cycle analysis shows free energy changes between V48A and I328A. (E) Histogram showing the calculated coupling energy (ΔΔG_INT) for the indicated pairs, H33C/S345C, V48C/I328C, H33A/S345A, V48A/I328A and F44C/A337C. The dashed line indicates the experimental error (2σ), which corresponds to ± 0.14 kcal/mol. ** (<i>P</i>< 0.01), values are significantly different from those observed for negative control F44C/A337C.</p

Functional properties of cysteine mutant receptors.

<p>The data represent the mean ± S.E.M. of the numbers of cells studied (n).</p

Coordinating residues at Ser345 for metal bridge formation.

<p>(A) Superimposed scaled current traces show that rP2X2R-T currents are not inhibited by applying 20 μM CdCl₂. The control current trace (black) is evoked only by 30 μM ATP. For the test current trace (blue), 30 μM ATP was applied for 5 s, after which the solution was switched to one containing 30 μM ATP plus 20 μM Cd²⁺ for 10-20 s. Following this, we returned the cell to a solution containing only 30 μM ATP for 5 s. The same protocol was applied to the other constructs in (B), (C), (D), and (E). In (B), (C), and (D), the superimposed scaled current traces are for the S345C trimers C-S-S, C-C-S, and C-C-C. (E) Superimposed scaled current traces for double mutant S345C/H33Y. Control recordings were made for all mutants to monitor their degrees of densensitization (30 μM ATP was applied for 20-30 s). (F) Summary of percentage of block current in (A), (B), (C), (D) and (E) after applying 20 μM CdCl₂. ** (<i>P</i>< 0.01), values are significantly different from those observed for rP2X2R-T and trimer C-S-S. * (<i>P</i>< 0.05), values are significantly different from those observed for rP2X2R-T and trimer C-S-S.</p

Functional Identification of Close Proximity Amino Acid Side Chains within the Transmembrane-Spanning Helixes of the P2X2 Receptor

<div><p>The transition from the closed to open state greatly alters the intra- and inter-subunit interactions of the P2X receptor (P2XR). The interactions that occur in the transmembrane domain of the P2X2R remain unclear. We used substituted cysteine mutagenesis disulfide mapping to identify pairs of residues that are in close proximity within the transmembrane domain of rP2X2R and compared our results to the predicted positions of these amino acids obtained from a rat P2X2R homology model of the available open and closed zebrafish P2X4R structures. Alternations in channel function were measured as a change in the ATP-gated current before and after exposure to dithiothreitol. Thirty-six pairs of double mutants of rP2X2R expressed in HEK293 cells produced normal functioning channels. Thirty-five pairs of these mutants did not exhibit a functionally detectable disulfide bond. The double mutant H33C/S345C formed redox-dependent cross-links in the absence of ATP. Dithiothreitol ruptured the disulfide bond of H33C/S345C and induced a 2 to 3-fold increase in current. The EC₅₀ for H33C/S345C before dithiothreitol treatment was ∼2-fold higher than that after dithiothreitol treatment. Dithiothreitol reduced the EC₅₀ to wild-type levels. Furthermore, expression of trimeric concatamer receptors with Cys mutations at some but not all six positions showed that the more disulfide bond formation sites within the concatamer, the greater current potentiation after dithiothreitol incubation. Immunoblot analysis of H33C/S345C revealed one monomer band under nonreducing conditions strongly suggesting that disulfide bonds are formed within single subunits (intra-subunit) and not between two subunits (inter-subunit). Taken together, these data indicate that His33 and Ser345 are proximal to each other across an intra-subunit interface. The relative movement between the first transmembrane and the second transmembrane in the intra-subunit is likely important for transmitting the action of ATP binding to the opening of the channel.</p></div

Laser scanning confocal microscopy examination.

<p>Representative confocal images of corneal Bowman’s membrane, stroma, and endothelium showed that CsA DDS alleviated inflammatory cell infiltration and maintained a normal endothelial cell density at all time-points (scale bar of 100 μm, n = 6 per group).</p

Disulfide bond formation between H33C and S345C alters channel opening.

<p>(A) Subcellular distribution of H33C/S345C (left panel), V48C/I328C (middle panel) and rP2X2-T (right panel) 24 h after transfection in the HEK293 cell line. Scale bar is 10 µm. (B) Effect of DTT and H₂O₂ on the H33C/S345C double mutant. After two stable responses were evoked by 30 μM ATP (black bar), the cells were incubated in 10 mM DTT for 5 min (first arrow) and were then evoked by 30 μM ATP plus 10 mM DTT (white bar). After stable currents were obtained, cells were incubated with 0.3% H₂O₂ (second arrow) for 3 min to reverse the effects of DTT, after which the cells were evoked by 30 μM ATP plus 0.3% H₂O₂ (grey bar). (C) The same protocol was applied to the rP2X2R-T, and had no effect on the responses evoked by 30 μM ATP plus 10 mM DTT. (D) Summary of relative current change in H33C/S345C and rP2X2R-T after DTT application. ** (<i>P</i>< 0.01), the values are significantly different from those obtained for H33C, S345C and rP2X2R-T. (E) Time course of the potentiation of ATP-evoked currents in V48C/I328C (△) and H33C/S345C (▪) double mutants by DTT. rP2X2R-T (•), H33C (○) and S345C (▾) single mutants were not affected by treatment with DTT. (F) Different concentrations of ATP (black bar) evoke currents in H33C/S345C. Each concentration of ATP (indicated below recordings) was applied twice for 2 s with similar results. 30 μM ATP was applied before each test concentration to evaluate rundown. The cell was superfused with 10 mM DTT (indicated by an arrow) for 5 min, and ATP plus DTT (white bar) were then co-applied for 2 s to evoke an inward current. DTT induced changes upon comparison with the control condition. (G) Concentration-response curves generated from the same experiment in (F) for rP2X2R-T (•), H33C (○), S345C (▾), H33C/S345C before (△) and after DTT application (▪). The EC₅₀ curves of single mutant and rP2X2-T after DTT treatment are not shown for the sake of clarity, because there were no significant changes. The dotted line indicates that the value of I/I_max is equal to 0.5. For (D) and (E), all currents were normalised to those measured prior to application of DTT (<i>n</i>  =  3-10 cells for each case). For (B), (C) and (F), the gaps indicate 3-min time intervals between each ATP application.</p