Molecular-Shape-Induced Efficiency Enhancement in PC₆₁BM and PC₇₁BM Based Ternary Blend Organic Solar Cells

Evolution of a self-organized molecular packing at the microscopic scale in a bulk heterojunction active layer is critical for improving the performance of organic solar cells. We demonstrate that the molecular-shape-induced effects improve the morphology of the ternary thin films as PC₆₁BM molecules were added to the host binary blend, PTB7-Th:PC₇₁BM. Compared to the binary PTB7-Th:PC₇₁BM devices, the ternary devices with 20% PC₆₁BM content (relative to PC₇₁BM) exhibited an enhanced efficiency, from 6.4% to 8.5%. In particular, we find that the spherical PC₆₁BM molecules with better precipitation kinetics than ellipsoidal PC₇₁BM alter the morphology of ternary thin film and modulate interfaces to expedite charge transport and collection by reducing various recombination losses

BITC inhibits angiogenesis in HUVECs.

<p><b>A</b>. BITC inhibits the secretion of proangiogenic factors from HUVECs. Cells were plated, stimulated with VEGF, and treated with BITC for 24 h. Media was collected and assayed for MMP-2 and VEGF by ELISA kit. *p<0.01 statistically significant when compared with controls. #p<0.01 statistically significant when compared with VEGF-stimulated controls. <b>B</b>. Regulation of VEGF mediated signaling by BITC. HUVECs were treated with various concentrations of BITC and whole cell lysates were analyzed by western blot. <b>C</b>. BITC down-regulates VEGFR2 and MMP-2 mRNA in HUVECs. Total RNA from BITC-treated HUVECs was isolated with Trizol and analyzed for the expression levels of VEGFR-2 and MMP-2 by RT-PCR. GAPDH was used as internal control. mRNA expression levels were quantified by Image J software and presented as bar diagram (lower panel). <b>D</b>. BITC inhibits STAT-3 DNA binding activity in HUVECs. HUVECs were treated with BITC and nuclear fraction was collected. Around 5 µg of nuclear protein subjected to STAT-3 DNA binding activity by Universal EZ-TFA transcription factor assay colorimetric kit according to the manufacturer's protocol. #p<0.01 statistically significant when compared with controls. <b>E</b>. BITC inhibits invasion of HUVECs. Invasion assay was performed using Boyden's chamber. *p<0.01 statistically significant when compared with controls. #p<0.01 statistically significant when compared with VEGF-stimulated controls</p

BITC inhibits <i>in vivo</i> tumor growth by inhibiting proangiogenic proteins.

<p><b>A</b>. BITC suppresses tumor growth <i>in vivo</i>. BxPC-3 xenografts bearing mice (n = 10) were orally fed with 12 µmol BITC daily for 40 days. Right side panel shows photographs of isolated tumors from control and BITC-treated mice. <b>B</b>. BITC inhibits tumor angiogenesis. BxPC-3 xenografts or matrigel plug-bearing mice were fed with 12 µmol BITC daily for 40 or 7 days, respectively. Tumors and plugs were collected and 50 mg of tumor or plugs were analyzed for hemoglobin content by Drabkin's reagent. <b>C</b>. BITC down-regulates pro-angiogenic proteins in tumor xenografts. Cell lysates were prepared from isolated tumor xenografts, subjected to western blot and analyzed for VEGFR-2, MMP-2, HIF-α, and Rho-GTPases <b>D</b>. Quantitative analysis of tumor western blots. *p<0.01 statistically significant when compared with controls.</p

Piperine suppresses the survival of melanoma cells.

<p>Effect of various concentrations of piperine at different time periods in (A) SK MEL 28, (B) B16 F0, (C) A375 and (D) Aspc-1 cells was determined by Sulforhodamine B cell survival assay. Values are the means ± S.D. of three independent experiments with eight replicates; *<i>p</i><0.05 when compared with control.</p

Piperine induces G1 phase cell cycle arrest in melanoma cells.

<p>(A) and (B) are representative cell cycle profiles of control and 150 µM piperine treated SK MEL 28 and B16 F0 cells for 48 h. FL2-A represents the intensity of propidium iodide, and the <i>y</i>-axis represents the cell counts. (C) And (D) represents concentration-dependent effects of piperine on number of cells in G1 phase in both SK MEL 28 and B16 F0 respectively. Values are means ± S.D. of three independent experiments, each conducted in triplicate. *p<0.05 when compared with control.</p

Piperine causes DNA damage and modulates G1 cell cycle regulatory proteins.

<p>SK MEL 28 (A) and B16 F0 (B) cells were treated with different concentrations of piperine for 48 h. Cells were lysed and total lysate was prepared as described under <i>Materials and Methods</i> and analyzed by western blotting. Representative immunoblots show the effect of piperine on the phosphorylation of H2A.X (Ser139), ATR (Ser428), Chk1 (Ser296) and p-Rb (Ser795), and the protein levels of DNA Polymerase β, p53, p21, Cyclin D1 and E2F1. Each blot was stripped and reprobed with anti-actin antibody to ensure equal protein loading. (C)Representative immunofluorescence images of p. Chk1 (Ser 296) in control and 150 µM piperine treated SK MEL 28 cells. Alexafluor 594 (Red) represents p.Chk1, Alexafluor 488(green) represents β-actin and DAPI (blue) represents nucleus. Each experiment was performed at least three times independently and the results were comparable.</p

BITC inhibits angiogenesis <i>ex vivo</i>.

<p><b>A</b>. BITC inhibits VEGF-induced vessel sprouting <i>ex vivo</i>. Aortic rings (1 mm) were harvested from Sprague-Dawley rats, immerged in matrigel, and treated with VEGF (20 ng/mL) in the absence or presence of BITC (0, 2.5 and 5 and 10 µM) for 4 days and photographed under microscope (4X). Representative photographs are presented. <b>B</b>. Quantitative analysis of aortic ring assay. Aortic ring sprouting was quantified by Image J software and presented as mean ± SD of triplicates. <b>C</b>. Inhibition of CAM angiogenesis by BITC. Eggs were incubated at 37°C for 3 days. A Whatman filter disc containing the test compound (BITC 5 µmol) was placed on the CAM of eggs (n = 10) through pre-opened window and further incubated. On day 9–12 of incubation, photographs were made after removing the filter discs. A representative photograph is presented. <b>D</b>. Blood vessels density was quantified by Image J software and represented as a bar diagram.</p

Piperine generates ROS in melanoma cells.

<p>(A) Represents time dependent generation of ROS in SK MEL 28 cells and (B) represents ROS in B16 F0 cells in response to 150 µM piperine treatment and subsequently analysed using flow cytometer. (C) SK MEL 28 and (D) B16 F0 cells were treated piperine following which the cells were analyzed for ROS using flow cytometer. (E) SK MEL 28 cells were pre-treated with either 10 mM tiron or NAC for 1 h and then treated with 150 µM piperine for 48 h. The cells were processed for ROS analysis by flow cytometry. (F) SK MEL 28 cells were pre-treated with either 10 mM tiron or NAC for 1 h followed by 150 µM piperine for 48 h after which the cell survival was evaluated by sulphorhodamine B assay. (G) SK MEL 28 and (H) B16 F0 cells were pre-treated with 10 mM tiron for 1 h followed by 150 µM piperine for 48 h. The cells were then processed for cell cycle analysis by flow cytometry. In another experiment, SK MEL 28 cells were pre-treated with (I) tiron or (J) NAC as described above and analyzed by western blotting for p.H2A.X, p.Chk1 and cleavage of PARP. Each experiment was performed at least three times independently, and the results were comparable. The values are means ± S.D. *<i>p</i><0.05 when compared with control. **p<0.05 when compared to piperine treatment.</p

1-(3-Chlorophenyl)-4-(3-phenylseleno propyl) piperazine (L); synthesis, spectroscopic characterization, DFT studies, antimicrobial evaluation and its reactivity toward group 12 metal chlorides

<p>C₆H₅Se⁻Na⁺ (generated <i>in situ</i> by NaBH₄ reduction of (C₆H₅Se)₂) on reaction with ClC₃H₆C₄H₈N₂ClC₆H₅ under N₂ atmosphere results in C₆H₅SeC₃H₆C₄H₈N₂ClC₆H₅ (L) as a cream-colored solid. Its 1:1 metal complexes having the general formula [MLX₂], where M = Zn, Cd, Hg, and X = Cl, have been prepared. Ligand L and its complexes <b>1–3</b> are characterized on the basis of physico-chemical and spectral (FT-IR, ESI Mass, ¹H, ¹³C, DEPT 135° ¹³C {¹H}, and ⁷⁷Se{¹H} NMR) studies. IR spectroscopy revealed that L is coordinated solely through selenium and nitrogen to zinc, cadmium, and mercury ions forming a six-membered chelate ring around M(II) ions. Elemental analysis measurements along with ¹H, ¹³C, DEPT 135° ¹³C {¹H}, and ESI-mass data also confirm the bidentate coordination mode of the ligand. Moreover, the coordination from selenium atom is also supported by the downfield shift of signal in ⁷⁷Se{¹H} NMR spectroscopy. Using DFT-based optimization of structures, the HOMO-LUMO energy gaps and molecular electrostatic potential surface of ligand L and complexes <b>1–3</b> were theoretically calculated at the B3LYP/LANL2DZ level of theory. Ligand L and complexes <b>1–3</b> display significant antibacterial and antifungal activity.</p

Piperine induces apoptosis in melanoma cells. SK MEL-28 and B16 F0 cells were treated with different concentrations of piperine for 48 h.

<p>Cells were stained with Annexin V and PI and analysed using flow cytometer. (A) and (B) shows representative apoptosis profile of SK MEL 28 and B16 F0 respectively. It also shows the concentration-dependent increase in the percent of apoptotic cells in both the cell lines. Figure (C) and (D) shows western blot analysis of SK MEL 28 and B16 F0 cell lysates upon piperine treatment respectively. Representative immunoblots show the effect of piperine on the protein levels of XIAP, Bid (full length), Cleaved Caspase 3 and Cleaved PARP. Each blot was stripped and reprobed with anti-actin antibody to ensure equal protein loading. Each experiment was performed at least three times independently and the results were comparable.</p