38806193
Tuning exchange bias in core/shell FeO/Fe3O4 nanoparticles.
Monodisperse 35 nm FeO nanoparticles (NPs) were synthesized and oxidized in a dry air atmosphere into core/shell FeO/Fe(3)O(4) NPs with both FeO core and Fe(3)O(4) shell dimensions controlled by reaction temperature and time. Temperature-dependent magnetic properties were studied on FeO/Fe(3)O(4) NPs obtained from the FeO NPs oxidized at 60 and 100 °C for 30 min. A large exchange bias (shift in the hysteresis loop) was observed in these core/shell NPs. The relative dimensions of the core and shell determine not only the coercivity and exchange field but also the dominant reversal mechanism of the ferrimagnetic Fe(3)O(4) component. This is the first time demonstration of tuning exchange bias and of controlling asymmetric magnetization reversal in FeO/Fe(3)O(4) NPs with antiferromagnetic core and ferrimagnetic shell.
5495246
Dumbbell-like PtPd-Fe₃O₄ nanoparticles for enhanced electrochemical detection of H₂O₂.
Dumbbell-like Pt(x)Pd(100-x)-Fe(3)O(4) nanoparticles (NPs) were synthesized and studied for electrocatalytic reduction and sensing of H(2)O(2). In 0.1 M phosphate buffered saline (PBS) solution, the 4-10 nm Pt(x)Pd(100-x)-Fe(3)O(4) NPs showed the Pt/Pd composition-dependent catalysis with Pt(48)Pd(52)-Fe(3)O(4) NPs having the best activity. The Pt(48)Pd(52)-Fe(3)O(4) NPs were tested for H(2)O(2) detection, and their H(2)O(2) detection limit reached 5 nM, which was suitable for monitoring H(2)O(2) generated from Raw 264.7 cells. These dumbbell-like PtPd-Fe(3)O(4) NPs are the most sensitive probe ever reported and can be used to achieve real-time quantitative detection of H(2)O(2) in biological environment for biological and biomedical applications.
12321226
Monodisperse MFe2O4 (M = Fe, Co, Mn) nanoparticles.
High-temperature solution phase reaction of iron(III) acetylacetonate, Fe(acac)(3), with 1,2-hexadecanediol in the presence of oleic acid and oleylamine leads to monodisperse magnetite (Fe(3)O(4)) nanoparticles. Similarly, reaction of Fe(acac)(3) and Co(acac)(2) or Mn(acac)(2) with the same diol results in monodisperse CoFe(2)O(4) or MnFe(2)O(4) nanoparticles. Particle diameter can be tuned from 3 to 20 nm by varying reaction conditions or by seed-mediated growth. The as-synthesized iron oxide nanoparticles have a cubic spinel structure as characterized by HRTEM, SAED, and XRD. Further, Fe(3)O(4) can be oxidized to Fe(2)O(3), as evidenced by XRD, NEXAFS spectroscopy, and SQUID magnetometry. The hydrophobic nanoparticles can be transformed into hydrophilic ones by adding bipolar surfactants, and aqueous nanoparticle dispersion is readily made. These iron oxide nanoparticles and their dispersions in various media have great potential in magnetic nanodevice and biomagnetic applications.
46535580
Monodisperse FePt nanoparticles and ferromagnetic FePt nanocrystal superlattices
Synthesis of monodisperse iron-platinum (FePt) nanoparticles by reduction of platinum acetylacetonate and decomposition of iron pentacarbonyl in the presence of oleic acid and oleyl amine stabilizers is reported. The FePt particle composition is readily controlled, and the size is tunable from 3- to 10-nanometer diameter with a standard deviation of less than 5%. These nanoparticles self-assemble into three-dimensional superlattices. Thermal annealing converts the internal particle structure from a chemically disordered face-centered cubic phase to the chemically ordered face-centered tetragonal phase and transforms the nanoparticle superlattices into ferromagnetic nanocrystal assemblies. These assemblies are chemically and mechanically robust and can support high-density magnetization reversal transitions.
20835850
Size-controlled synthesis of magnetite nanoparticles.
Monodisperse magnetite nanoparticles have been synthesized by high-temperature solution-phase reaction of Fe(acac)3 in phenyl ether with alcohol, oleic acid, and oleylamine. Seed-mediated growth is used to control Fe3O4 nanoparticle size, and variously sized nanoparticles from 3 to 20 nm have been produced. The as-synthesized Fe3O4 nanoparticles have inverse spinel structure, and their assemblies can be transformed into gamma-Fe2O3 or alpha-Fe nanoparticle assemblies, depending on the annealing conditions. The reported procedure can be used as a general approach to various ferrite nanoparticles and nanoparticle superlattices.
1623657
Regression of solid tumors by engineered overexpression of von Hippel–Lindau tumor suppressor protein and antisense hypoxia-inducible factor-1α
The von Hippel–Lindau tumor suppressor protein (pVHL) suppresses tumor formation by binding the α subunits of hypoxia-inducible factors (HIFs) responsible for stimulating tumor angiogenesis and glycolysis, targeting them for ubiquitination and proteasomal destruction. Loss of pVHL leads to the development of sporadic renal cell carcinomas (RCCs). In the present study, we sought to determine whether engineered overexpression of pVHL in tumors other than RCC can inhibit tumor growth, either as a monotherapy, or in combination with antisense HIF-1α therapy. Intratumoral injection of subcutaneous EL-4 thymic lymphomas with an expression plasmid encoding pVHL resulted in the downregulation of HIF-1α and vascular endothelial growth factor (VEGF). There was a concomitant reduction in tumor angiogenesis and increased tumor cell apoptosis due in part to downregulation of Bcl-2 expression. VHL therapy resulted in the complete regression of small (0.1 cm diameter) tumors whereas, in contrast, large (0.4 cm diameter) EL-4 tumors were only slowed in their growth. Nevertheless, large tumors completely regressed in response to intratumoral injection of a combination of antisense HIF-1α and VHL plasmids. Combination therapy resulted in increased losses of HIF-1α, VEGF, and tumor blood vessels, and increased tumor cell apoptosis. These novel results suggest that synergistic therapies that simultaneously block the expression or function of HIF-1α, and enhance the expression or function of VHL may be beneficial in the treatment of cancer.
26818613
A facile and efficient strategy for one-step in situ preparation of hydrophobic organic monolithic stationary phases by click chemistry and its application on protein separation.
A simple one-step in situ "click" modification strategy was developed for the preparation of hydrophobic organic monolithic columns for the first time. The column morphology and surface chemistry of the fabricated monolithic columns were characterized by scanning electron microscopy, Fourier transform infrared spectroscopy and X-ray photoelectron spectroscopy, respectively. The chromatographic performances of the C8/C18 "click" monoliths were evaluated through the separation of a mixture of five proteins such as ribonuclease A, soybean trypsin inhibitor, cytochrome c, bovine haemoglobin and bovine serum albumin. Compared with the blank column, the higher hydrophobicity stationary phases obtained from the "clicked" modification have longer retention times and higher resolution for the five proteins. The separation of five proteins mixture on click C18 monolith with gradient elution at different flow rates was also investigated, the baseline separation of five proteins could be achieved at three different flow rates.
6943686
N-terminal domains of DELLA proteins are intrinsically unstructured in the absence of interaction with GID1/gibberellic acid receptors.
The plant growth-repressing DELLA proteins (DELLAs) are known to represent a convergence point in integration of multiple developmental and environmental signals in planta, one of which is hormone gibberellic acid (GA). Binding of the liganded GA receptor (GID1/GA) to the N-terminal domain of DELLAs is required for GA-induced degradation of DELLAs via the ubiquitin-proteasome pathway, thus derepressing plant growth. However, the conformational changes of DELLAs upon binding to GID1/GA, which are the key to understanding the precise mechanism of GID1/GA-mediated degradation of DELLAs, remain unclear. Using biophysical, biochemical, and bioinformatics approaches, we demonstrated for the first time that the unbound N-terminal domains of DELLAs are intrinsically unstructured proteins under physiological conditions. Within the intrinsically disordered N-terminal domain of DELLAs, we have identified several molecular recognition features, sequences known to undergo disorder-to-order transitions upon binding to interacting proteins in intrinsically unstructured proteins. In accordance with the molecular recognition feature analyses, we have observed the binding-induced folding of N-terminal domains of DELLAs upon interaction with AtGID1/GA. Our results also indicate that DELLA proteins can be divided into two subgroups in terms of their molecular compactness and their interactions with monoclonal antibodies.
8889473
Cannabinoid/Endocannabinoid signaling impact on early pregnancy events.
It has been known for decades that marijuana and its major psychoactive component Δ⁹-tetrahydrocannabinol (THC) alter both male and female reproductive functions in humans and laboratory animals. The discovery of cannabinoid-like molecules (endocannabinoids), anandamide (AEA) and 2-arachidonylglycerol (2AG), as well as G-protein-coupled cannabinoid/endocannabinoid receptors CB₁ and CB₂, created an opportunity to study the adverse and beneficial effects of cannabinoids/endocannabinoids on fertility using molecular, physiological and genetic approaches. In fact, studies to explore the significance of cannabinoid/endocannabinoid signaling in reproduction have revealed some intriguing physiological roles in early pregnant events. This review summarizes some aspects of these signaling molecules in preimplantation and implantation biology utilizing genetically engineered mouse models.
9796021
Methodological issues in cost-effectiveness studies: a brief overview.
This article discussed two methodological issues around cost-effectiveness studies, including validity and transferability of results. In an economic analysis study, methods to costing, health utility measurement, and economic modeling represent three important sources that may threaten the validity. Variations in health systems and clinical practice, and differential resource use and unit prices across regions and countries may have potentially large influence on transferability. The limitations of piggybacked design may also have implications for transferability. Caution is warranted in the design, conduct, and interpretation of cost-effectiveness studies regarding their validity and transferability.