10 research outputs found
Industrial-Quality Graphene Oxide Switched Highly Efficient Metal- and Solvent-Free Synthesis of β‑Ketoenamines under Feasible Conditions
Metal-
and solvent-free industrial-quality graphene oxide (IQGO)-based
highly efficient carbocatalytic system has been developed for the
synthesis of β-ketoenamines. Initially, physicochemical properties
of IQGO are briefly discussed by means of various microscopic and
spectroscopic techniques. The present system accessed a wide range
of substrates to yield β-ketoenamines in an excellent yield
(86–100%) with 100% selectivity. Catalytic activity of IQGO
is compared with other carbon materials such as carbon nanotubes,
carbon nanofibers, and graphene nanoplatelets. Cost effective recovery,
high level reusability, chemoselective nature, possible scale reaction,
and sustainability of IQGO are demonstrated. Based upon experimental
results and earlier reports, possible reaction mechanism has been
proposed for the synthesis of β-ketoenamines
Human Hair: A Suitable Platform for Catalytic Nanoparticles
Human
hair (HH) has been utilized as a support for Au and Ag nanoparticles
(NPs) for the very first time. Initially, a very fine human hair powder
(HHP) was obtained from HH by a simple ball milling method. The HHP
after chemical treatment (e-HHP) was used to prepare two different
nanocatalysts, Ag NPs immobilized e-HHP (Ag/HHP) and Au NPs decorated
e-HHP (Au/HHP). Influence of e-HHP on the morphology of nanocatalyts
and metal–support interactions were studied. Merit of Ag/HHP
and Au/HHP was realized from its excellent yields in cyclo addition
and <i>aza</i>-Michael reactions, respectively. Reusability
and heterogeneity tests of the nanocatalysts were also performed
Utilization of Human Hair as a Synergistic Support for Ag, Au, Cu, Ni, and Ru Nanoparticles: Application in Catalysis
Human hair powder (HHP) after chemical
treatment (e-HHP) has been
successfully utilized as a unique catalyst support for immobilization
of metal nanoparticles (MNPs). Ag, Au, Cu, Ni, and Ru NPs were used
to prepare five different nanocatalysts (MNPs/e-HHP). High-resolution
transmission electron microscopy results confirmed the excellent attachment
of ultrafine MNPs on the surface of e-HHP. Actual loading of metal
in MNPs/e-HHP was determined by energy-dispersive spectroscopy and
X-ray photoelectron spectroscopy analyses. The zero-valent state of
MNPs in MNPs/e-HHP and a very strong interaction between MNPs and
e-HHP were also proven. The obtained AgNPs/e-HHP, AuNPs/e-HHP, CuNPs/e-HHP,
NiNPs/e-HHP, and RuNPs/e-HHP catalysts were employed for the self-coupling
of amines, <i>N</i>-oxidation of tertiary amines, <i>aza</i>-Michael reaction, imines synthesis, and oxidation of
alcohols, respectively. Reaction conditions were optimized, and the
scope of the catalytic systems was extended. The merit of the MNPs/e-HHP
materials is shown to be the superior catalytic activity. Advantages,
shortcomings, and future scope of the MNPs/e-HHP system are also highlighted
New transition metal(II) complexes with naphthoate and aminoguanidine-based ligands: a combined spectroscopic and theoretical study with its applications
A new series of transition metal complexes of Mn(ΙΙ), Fe(ΙΙ), Co(ΙΙ) and Ni(ΙΙ) is synthesized from aminoguanidine and 3-hydroxy-2-naphthoic acid ligands with the formula (N4H7C)2[M{(C10H6(O)(COO)}2]·2H2O. The synthesized complexes were characterized by analytical, spectral and thermal studies. The elemental analysis confirms the composition of the complexes. The XRD studies show that all the complexes are isostructural in nature. The complexes were screened for antimicrobial activity against a Gram-positive, Bacillus subtilis (B. subtilis), and a Gram-negative, Escherichia coli (E. coli), bacterial species. The antibacterial results were concurrent with the output of the DFT investigation of metal complex, showing that the aminoguanidine moiety plays a key role in biological activity. Molecular docking studies have been carried out to identify the binding affinity and the mode of interaction of metal complexes with E. coli protein (2FUM). Further the synthesized complex is used as a single source precursor for preparation of nano metal oxides. The photocatalytic activity was carried out using the metal oxide as catalyst for degradation of dye materials. The metal oxide is found to be an efficient catalyst for degradation of methyl orange dye.</p
<i>Hwanggeumchal sorghum</i> Induces Cell Cycle Arrest, and Suppresses Tumor Growth and Metastasis through Jak2/STAT Pathways in Breast Cancer Xenografts
<div><p>Background</p><p>Cancer is one of the highly virulent diseases known to humankind with a high mortality rate. Breast cancer is the most common cancer in women worldwide. Sorghum is a principal cereal food in many parts of the world, and is critical in folk medicine of Asia and Africa. In the present study, we analyzed the effects of HSE in metastatic breast cancer.</p><p>Methodology/Principal Findings</p><p>Preliminary studies conducted on MDA-MB 231 and MCF-7 xenograft models showed tumor growth suppression by HSE. Western blotting studies conducted both <i>in vivo</i> and <i>in vitro</i> to check the effect of HSE in Jak/STAT pathways. Anti-metastatic effects of HSE were confirmed using both MDA-MB 231 and MCF-7 metastatic animal models. These studies showed that HSE can modulate Jak/STAT pathways, and it hindered the STAT5b/IGF-1R and STAT3/VEGF pathways not only by down-regulating the expression of these signal molecules and but also by preventing their phosphorylation. The expression of angiogenic factors like VEGF, VEGF-R2 and cell cycle regulators like cyclin D, cyclin E, and pRb were found down-regulated by HSE. In addition, it also targets Brk, p53, and HIF-1α for anti-cancer effects. HSE induced G1 phase arrest and migration inhibition in MDA-MB 231 cells. The metastasis of breast cancer to the lungs also found blocked by HSE in the metastatic animal model.</p><p>Conclusions/Significance</p><p>Usage of HS as a dietary supplement is an inexpensive natural cancer therapy, without any side effects. We strongly recommend the use of HS as an edible therapeutic agent as it possesses tumor suppression, migration inhibition, and anti-metastatic effects on breast cancer.</p></div
Suppression of STAT3/DNA binding activity leads to the crackdown of target gene products.
<p>A, western blotting analysis of whole cell lysates from MDA MB-231, MCF-7 and SKBR-3 cells treated with increasing concentration of HSE. B, RT-PCR analysis of MDA-MB 231, MCF-7, and SKBR-3 cells treated with different concentration of HSE showed transcriptional regulation of IGF-1R, Cyclin D1 and VEGF mRNA levels. 18S RNA was used as a control.</p
HSE suppressed the binding activities of STAT5b to the IGF-1R and STAT3 to the VEGF promoter sites.
<p>A, electrophoretic mobility shift assay (EMSA) showed, HSE suppressed the DNA-binding activity of STAT5b to the IGF-1R (i) and STAT3 to the VEGF (ii) binding sites in MDA-MB 231 cells treated with HSE for 24 h. B, nuclear protein extracts (NE) were separated and blotted onto nitrocellulose membrane showing decrease in the level of p-STAT5, p-STAT3, VEGF and IGF-1R. C and D, shows the activation of STAT5b/IGF-1R promoter and STAT3/VEGF promoter in COS-7 cells by HSE. COS-7 cells were transiently co-transfected with STAT5b and IGF-1R (C) and STAT3 and VEGF genes (D). Data represent means of at least three separate experiments. Asterisks indicate a statistically significant decrease by t-test (***p<0.001) in the crosstalks of STAT5b/IGF-1R and STAT3/VEGF respectively.</p
HSE inhibited breast cancer cell growth, induce G1 cell cycle arrest, maintained the expression of tumor suppressor proteins and suppressed the expression of oncogenic proteins over other whole grain extracts.
<p>A, breast cancer cells MDA-MB 231, MCF-7, and SKBR-3 were treated with HSE. After 24 h, cell viability was evaluated by the MTT assay. B, the expression of Bcl-2, Cyclin D1, Cyclin E, ppRb, pRb, p53, p21 and BRCA1 in MDA-MB 231 cells. C, the cell cycle arrest is confirmed through flow cytometry. Flow cytometry MDA-MB 231 cells using propidium iodide flow cytometry. D, the oncogenic protein expression of in MDA-MB 231 cells treated with whole grain extracts (10 µg/ml). The protein extracts were separated by 10% SDS-PAGE, and western blots were performed as described in experimental procedures. β-actin was used as a control for protein loading. Data represent the mean of at least three separate experiments, mean ± SEM. Asterisks indicate a IC<sub>50</sub> value.</p
HSE down-regulated the STAT5b/IGF-1R and STAT3/VEGF pathways in time and dose dependent manner.
<p>A, human breast cancer cells MDA-MB 231, MCF-7, and SKBR-3 were exposed to different incubation time with HSE (10 µg/ml). B, MDA-MB 231, MCF-7, and SKBR-3 cells were exposed to various concentrations of HSE. The protein extracts (10 µg) were separated by 10% SDS-PAGE, and western blots were performed as described in experimental procedures. β-actin was used as a control for protein loading.</p
HSE might block the metastasis of breast cancer to lungs in animal model.
<p>A, analysis of the effect of HSE on the experimental lung metastases established by MDA-MB 231 and MCF-7 cells. Mice were injected with MDA-MB 231 cells (1×10<sup>7</sup> in 200 µL PBS per mouse) and MCF-7 cells (1×10<sup>7</sup> in 200 µL PBS per mouse). They are randomized into two groups for each cell model. One group of mice (n = 6) was injected with HSE for 30 days, and the other group of mice (n = 6) was injected with water using the same schedule. Lungs were collected on day 30 after the start of treatment and formalin-fixed paraffin-embedded lung tissues were stained with hematoxylin and eosin. Representative images are shown (A, magnification: ×200, scale bar = 200 µm). Arrow points the area of metastasis. B, quantitative analysis of tumor areas shown in A. The area of metastatic nodules in each section was quantified from six fields (magnification: ×200). The values are means ± S.E (n = 6) after normalization to vehicle (internal control). Asterisks indicate a statistically significant decrease by t-test (***p<0.001). C, HSE inhibited the migration of MDA-MB 231 cells treated with HSE (10 µg/ml for 24 h). MDA-MB 231 cells were plated into DMEM medium separately. After 24 hours, medium was replaced with and without HSE (10 µg/ml). Live cell images were acquired 24 hours after media changes (i and ii; pre-confluent), (iii and iv; confluent). <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0040531#pone.0040531.s001" target="_blank">Movie S1</a>, MDA-MB 231 cells without HSE (control) and <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0040531#pone.0040531.s002" target="_blank">Movie S2</a>, MDA-MB 231 cells treated by HSE.</p