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1.
Sensors (Basel) ; 15(2): 3513-39, 2015 Feb 03.
Article in English | MEDLINE | ID: mdl-25654724

ABSTRACT

Configurations capable of maximizing both the absorption component of system detection efficiency and the achievable polarization contrast were determined for 1550 nm polarized light illumination of different plasmonic structure integrated superconducting nanowire single-photon detectors (SNSPDs) consisting of p = 264 nm and P = 792 nm periodic niobium nitride (NbN) patterns on silica substrate. Global effective NbN absorptance maxima appear in case of p/s-polarized light illumination in S/P-orientation (γ = 90°/0° azimuthal angle) and the highest polarization contrast is attained in S-orientation of all devices. Common nanophotonical origin of absorptance enhancement is collective resonance on nanocavity gratings with different profiles, which is promoted by coupling between localized modes in quarter-wavelength metal-insulator-metal nanocavities and laterally synchronized Brewster-Zenneck-type surface waves in integrated SNSPDs possessing a three-quarter-wavelength-scaled periodicity. The spectral sensitivity and dispersion characteristics reveal that device design specific optimal configurations exist.


Subject(s)
Absorptiometry, Photon , Nanotechnology , Photometry , Electric Conductivity , Equipment Design , Nanowires/chemistry , Niobium
2.
Sci Rep ; 3: 2406, 2013.
Article in English | MEDLINE | ID: mdl-23934331

ABSTRACT

Plasmonic structures open novel avenues in photodetector development. Optimized illumination configurations are reported to improve p-polarized light absorptance in superconducting-nanowire single-photon detectors (SNSPDs) comprising short- and long-periodic niobium-nitride (NbN) stripe-patterns. In OC-SNSPDs consisting of ~quarter-wavelength dielectric layer closed by a gold reflector the highest absorptance is attainable at perpendicular incidence onto NbN patterns in P-orientation due to E-field concentration at the bottom of nano-cavities. In NCAI-SNSPDs integrated with nano-cavity-arrays consisting of vertical and horizontal gold segments off-axis illumination in S-orientation results in polar-angle-independent perfect absorptance via collective resonances in short-periodic design, while in long-periodic NCAI-SNSPDs grating-coupled surface waves promote EM-field transportation to the NbN stripes and result in local absorptance maxima. In NCDAI-SNSPDs integrated with nano-cavity-deflector-array consisting of longer vertical gold segments large absorptance maxima appear in 3p-periodic designs due to E-field enhancement via grating-coupled surface waves synchronized with the NbN stripes in S-orientation, which enable to compensate fill-factor-related retrogression.


Subject(s)
Nanotechnology/instrumentation , Photometry/instrumentation , Surface Plasmon Resonance/instrumentation , Absorption , Equipment Design , Equipment Failure Analysis , Infrared Rays , Photons , Systems Integration
3.
Colloids Surf B Biointerfaces ; 98: 43-9, 2012 Oct 01.
Article in English | MEDLINE | ID: mdl-22652358

ABSTRACT

Citrate-stabilized spherical silver nanoparticles (Ag NPs) with d=8.25±1.25 nm diameter were prepared and functionalized with L-cysteine (Cys) in aqueous dispersion. The nanosilver-cysteine interactions have been investigated by Raman and (1)H NMR spectroscopy. The effect of pH on stability of biofunctionalized Ag NPs was investigated. The cysteine-capped nanosilver dispersions remain stable at higher pH (pH>7), while the degree of aggregation increased as the pH decreased. Below pH ~7, the characteristic surface plasmon band of bare silver nanoparticles was back-shifted from λ(measured)(bareAgNP)=391 nm to λ(measured)(1)=387-391 nm, while the presence of a new band at λ(measured)(2)=550-600 nm was also observed depending on pH. Finite element method (FEM) was applied to numerically compute the absorption spectra of aqueous dispersions containing bare and cysteine-functionalized Ag NPs at different pH. Both the dynamic light scattering (DLS) measurements, Zeta potential values and the transmission electron microscopic (TEM) images confirmed our supposition. Namely, electrostatic interaction arose between the deprotonated carboxylate (COO(-)) and protonated amino groups (NH(3)(+)) of the amino acid resulting in cross-linking network of the Ag NPs between pH ~3 and 7. If the pH is measurable lower than ~3, parallel with the protonation of citrate and L-cysteine molecules the connection of the particles via l-cysteine is partly decomposed resulting in decrease of second plasmon band intensity.


Subject(s)
Cysteine/chemistry , Metal Nanoparticles/chemistry , Silver/chemistry , Hydrogen-Ion Concentration , Magnetic Resonance Spectroscopy , Particle Size
4.
Blood ; 117(4): e39-48, 2011 Jan 27.
Article in English | MEDLINE | ID: mdl-21041717

ABSTRACT

Numerous diseases, recently reported to associate with elevated microvesicle/microparticle (MP) counts, have also long been known to be characterized by accelerated immune complex (IC) formation. The goal of this study was to investigate the potential overlap between parameters of protein complexes (eg, ICs or avidin-biotin complexes) and MPs, which might perturb detection and/or isolation of MPs. In this work, after comprehensive characterization of MPs by electron microscopy, atomic force microscopy, dynamic light-scattering analysis, and flow cytometry, for the first time, we drive attention to the fact that protein complexes, especially insoluble ICs, overlap in biophysical properties (size, light scattering, and sedimentation) with MPs. This, in turn, affects MP quantification by flow cytometry and purification by differential centrifugation, especially in diseases in which IC formation is common, including not only autoimmune diseases, but also hematologic disorders, infections, and cancer. These data may necessitate reevaluation of certain published data on patient-derived MPs and contribute to correct the clinical laboratory assessment of the presence and biologic functions of MPs in health and disease.


Subject(s)
Biophysical Phenomena/physiology , Cell Fractionation/methods , Cell-Derived Microparticles/chemistry , Multiprotein Complexes/pharmacology , Adult , Aged , Case-Control Studies , Cell Fractionation/standards , Cell-Derived Microparticles/physiology , Female , Flow Cytometry , Humans , Male , Microscopy, Atomic Force , Microscopy, Electron , Middle Aged , Multiprotein Complexes/chemistry , Particle Size
5.
J Alzheimers Dis ; 22(3): 777-94, 2010.
Article in English | MEDLINE | ID: mdl-20847411

ABSTRACT

Endothelial cells of brain capillaries forming the blood-brain barrier play an important role in the pathogenesis and therapy of Alzheimer's disease. Amyloid-ß (Aß) peptides are key pathological elements in the development of the disease. A blood-brain barrier model, based on primary rat brain endothelial cells was used in which the barrier properties were induced by glial cells. The effects of amyloid peptides have been tested on cell viability and barrier functions. Aß showed toxic effects on primary rat brain endothelial cells measured by MTT dye conversion and the lactate dehydrogenase release. Morphologically cytoplasmic vacuolization, disruption of the structure of cytoplasmic organelles and tight junctions could be observed in brain endothelial cells. Treatment with Aß1-42 decreased the electrical resistance, and increased the permeability of brain endothelial cell monolayers for both fluorescein and albumin. Serum amyloid P component which stabilizes Aß fibrils in cortical amyloid plaques and cerebrovascular amyloid deposits significantly potentiated the barrier-weakening effect of Aß1-42. Sulfated polysaccharide pentosan could decrease the toxic effects of Aß peptides in brain endothelial cells. It could also significantly protect the barrier integrity of monolayers from damaging actions of peptides. Pentosan modified the size, and significantly decreased the number of amyloid aggregates demonstrated by atomic force microscopy. The present data further support the toxic effects of amyloid peptides on brain endothelial cells, and can contribute to the development of molecules protecting the blood-brain barrier in Alzheimer's disease.


Subject(s)
Amyloid beta-Peptides/antagonists & inhibitors , Amyloid beta-Peptides/toxicity , Blood-Brain Barrier/drug effects , Blood-Brain Barrier/ultrastructure , Neuroprotective Agents/pharmacology , Pentosan Sulfuric Polyester/pharmacology , Peptide Fragments/antagonists & inhibitors , Peptide Fragments/toxicity , Animals , Blood-Brain Barrier/physiology , Cells, Cultured , Rats
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