scholarly journals Biodegradable and Excretable 2D W 1.33 C i ‐MXene with Vacancy Ordering for Theory‐Oriented Cancer Nanotheranostics in Near‐Infrared Biowindow

2021 ◽  
pp. 2101043
Author(s):  
Bangguo Zhou ◽  
Haohao Yin ◽  
Caihong Dong ◽  
Liping Sun ◽  
Wei Feng ◽  
...  
Keyword(s):  
Near Infrared ◽  
Vacancy Ordering

Transmission Electron Microscopy studies of the vacancy ordering in YSI2-X thin films

1991 ◽  
Vol 49 ◽  
pp. 562-563
Author(s):  
F.-R. Chen ◽  
T. L. Lee ◽  
L. J. Chen
Keyword(s):  
Crystal Structure ◽  
Electron Microscopy ◽  
Thin Films ◽  
Diffraction Pattern ◽  
Annealing Temperature ◽  
Lattice Mismatch ◽  
Si Substrate ◽  
Metal Thin Films ◽  
Transmission Electron ◽  
Vacancy Ordering

YSi2-x thin films were grown by depositing the yttrium metal thin films on (111)Si substrate followed by a rapid thermal annealing (RTA) at 450 to 1100°C. The x value of the YSi2-x films ranges from 0 to 0.3. The (0001) plane of the YSi2-x films have an ideal zero lattice mismatch relative to (111)Si surface lattice. The YSi2 has the hexagonal AlB2 crystal structure. The orientation relationship with Si was determined from the diffraction pattern shown in figure 1(a) to be and . The diffraction pattern in figure 1(a) was taken from a specimen annealed at 500°C for 15 second. As the annealing temperature was increased to 600°C, superlattice diffraction spots appear at position as seen in figure 1(b) which may be due to vacancy ordering in the YSi2-x films. The ordered vacancies in YSi2-x form a mesh in Si plane suggested by a LEED experiment.

Point and planar defects in the iron sulfide compounds Fe1-xS

1984 ◽  
Vol 42 ◽  
pp. 434-435
Author(s):  
Thao A. Nguyen
Keyword(s):  
Low Temperatures ◽  
Direct Evidence ◽  
Iron Sulfide ◽  
Planar Defects ◽  
Selective Area ◽  
Vacancy Ordering ◽  
Different Types ◽  
Lattice Images ◽  
The Subject ◽  
Beam Lattice

It is well known that the large deviations from stoichiometry in iron sulfide compounds, Fe1-xS (0≤x≤0.125), are accommodated by iron vacancies which order and form superstructures at low temperatures. Although the ordering of the iron vacancies has been well established, the modes of vacancy ordering, hence superstructures, as a function of composition and temperature are still the subject of much controversy. This investigation gives direct evidence from many-beam lattice images of Fe1-xS that the 4C superstructure transforms into the 3C superstructure (Fig. 1) rather than the MC phase as previously suggested. Also observed are an intrinsic stacking fault in the sulfur sublattice and two different types of vacancy-ordering antiphase boundaries. Evidence from selective area optical diffractograms suggests that these planar defects complicate the diffraction pattern greatly.

A study of oxygen and vacancy ordering in YBa2Cu3O7−x

1989 ◽  
Vol 47 ◽  
pp. 164-165
Author(s):  
Y. P. Lin ◽  
A. H. O’Reilly ◽  
J. E. Greedan ◽  
M. Post
Keyword(s):  
Electron Microscopy ◽  
Neutron Diffraction ◽  
Oxygen Content ◽  
Carbon Film ◽  
Nitrogen Atmosphere ◽  
Vacancy Ordering ◽  
Powder Samples ◽  
Vacancy Chains ◽  
Chain Ordering

In the basal planes of the orthorhombic YBa2Cu3O7-X compound with x=0.07, which has a Tc of around 90K, chains of copper-oxygen are formed along the [010] direction. Previous investigations on the variation of Tc with oxygen content have shown the existence of a plateau at Tc = 60K for x=0.3 to 0.4, suggesting the presence of a separate phase. This phase has also been identified to be orthorhombic, but with a 2x superlattice along [100] of the parent structure, and the superlattice has been attributed to the formation of alternating copper-oxygen and copper-vacancy chains. In our work, we have studied the chain ordering phenomenon by electron microscopy and neutron diffraction on samples with different oxygen contents. We report here some of our electron microscopy findings for samples with x=0.4.Powder samples of YBa2Cu3O7-X were prepared by controlled re-oxidation of previously reduced material. For electron microscopy, the sample was dry ground using a mortar and pestle in a dry nitrogen atmosphere without the use of any solvent and transferred dry onto holey carbon film for examination in a Philips CM12 microscope.

Construction of a near-infrared responsive upconversion nanoplatform against hypoxic tumors via NO-enhanced photodynamic therapy

Nanoscale ◽  
2020 ◽  
Vol 12 (14) ◽  
pp. 7875-7887 ◽  
Author(s):  
Ying Lan ◽  
Xiaohui Zhu ◽  
Ming Tang ◽  
Yihan Wu ◽  
Jing Zhang ◽  
...  
Keyword(s):  
Photodynamic Therapy ◽  
Near Infrared ◽  
Upconversion Nanoparticles

A near-infrared (NIR) activated theranostic nanoplatform based on upconversion nanoparticles (UCNPs) is developed in order to overcome the hypoxia-associated resistance in photodynamic therapy by photo-release of NO upon NIR illumination.

A nitroreductase-activatable near-infrared theranostic photosensitizer for photodynamic therapy under mild hypoxia

2020 ◽  
Vol 56 (43) ◽  
pp. 5819-5822
Author(s):  
Jing Zheng ◽  
Yongzhuo Liu ◽  
Fengling Song ◽  
Long Jiao ◽  
Yingnan Wu ◽  
...  
Keyword(s):  
Photodynamic Therapy ◽  
Triplet State ◽  
Near Infrared ◽  
Mild Hypoxia

In this study, a near-infrared (NIR) theranostic photosensitizer was developed based on a heptamethine aminocyanine dye with a long-lived triplet state.

Fluorescent proteins for in vivo imaging, where's the biliverdin?

2020 ◽  
Vol 48 (6) ◽  
pp. 2657-2667
Author(s):  
Felipe Montecinos-Franjola ◽  
John Y. Lin ◽  
Erik A. Rodriguez
Keyword(s):  
Hydrogen Peroxide ◽  
In Vivo Imaging ◽  
Near Infrared ◽  
Fluorescent Protein ◽  
Fluorescent Proteins ◽  
Fluorescent Imaging ◽  
Infrared Light ◽  
Red Fluorescent Protein ◽  
Color Palette

Noninvasive fluorescent imaging requires far-red and near-infrared fluorescent proteins for deeper imaging. Near-infrared light penetrates biological tissue with blood vessels due to low absorbance, scattering, and reflection of light and has a greater signal-to-noise due to less autofluorescence. Far-red and near-infrared fluorescent proteins absorb light >600 nm to expand the color palette for imaging multiple biosensors and noninvasive in vivo imaging. The ideal fluorescent proteins are bright, photobleach minimally, express well in the desired cells, do not oligomerize, and generate or incorporate exogenous fluorophores efficiently. Coral-derived red fluorescent proteins require oxygen for fluorophore formation and release two hydrogen peroxide molecules. New fluorescent proteins based on phytochrome and phycobiliproteins use biliverdin IXα as fluorophores, do not require oxygen for maturation to image anaerobic organisms and tumor core, and do not generate hydrogen peroxide. The small Ultra-Red Fluorescent Protein (smURFP) was evolved from a cyanobacterial phycobiliprotein to covalently attach biliverdin as an exogenous fluorophore. The small Ultra-Red Fluorescent Protein is biophysically as bright as the enhanced green fluorescent protein, is exceptionally photostable, used for biosensor development, and visible in living mice. Novel applications of smURFP include in vitro protein diagnostics with attomolar (10−18 M) sensitivity, encapsulation in viral particles, and fluorescent protein nanoparticles. However, the availability of biliverdin limits the fluorescence of biliverdin-attaching fluorescent proteins; hence, extra biliverdin is needed to enhance brightness. New methods for improved biliverdin bioavailability are necessary to develop improved bright far-red and near-infrared fluorescent proteins for noninvasive imaging in vivo.

Sign in / Sign up

Export Citation Format

Share Document