A Study on Absorption and Reflection of Infrared Light by the Uncoated and Al Coated Surfaces of Polymer Films Techniques

2014 ◽  
pp. 23-38
Keyword(s):  
Polymer Films ◽  
Infrared Light ◽  
Coated Surfaces

Anisotropic optical properties of oriented silver nanorice and nanocarrots in stretched polymer films

Nanoscale ◽  
2015 ◽  
Vol 7 (19) ◽  
pp. 8858-8863 ◽  
Author(s):  
Xia Tong ◽  
Hongyan Liang ◽  
Yanlong Liu ◽  
Long Tan ◽  
Dongling Ma ◽  
...  
Keyword(s):  
Optical Properties ◽  
Polymer Films ◽  
Spectral Region ◽  
Near Infrared ◽  
Infrared Light ◽  
Near Infrared Light

Oriented arrays of silver nanorice or nanocarrots in stretched polymer films show polarization-dependent transmission of near-infrared light over a wide spectral region.

scholarly journals Brushing up from “anywhere” under sunlight: a universal surface-initiated polymerization from polydopamine-coated surfaces

2015 ◽  
Vol 6 (3) ◽  
pp. 2068-2073 ◽  
Author(s):  
Wenbo Sheng ◽  
Bin Li ◽  
Xiaolong Wang ◽  
Bin Dai ◽  
Bo Yu ◽  
...  
Keyword(s):  
Polymer Films ◽  
Thin Polymer Films ◽  
Surface Initiated Polymerization ◽  
Thin Polymer ◽  
Coated Surfaces

A generalized surface-initiated photografting procedure, which utilizes polydopamine as a photosensitive initiating layer, allows functionalization of almost any substrate with thin polymer films under sunlight.

Gum arabic helps prepare better lacey polymer films for specimen support in electron microscopy

1993 ◽  
Vol 51 ◽  
pp. 240-241
Author(s):  
Shailesh R. Sheth ◽  
Jayesh R. Bellare
Keyword(s):  
Electron Microscopy ◽  
Polymer Films ◽  
Gum Arabic ◽  
Complete Removal ◽  
Ammonium Bromide ◽  
Release Agent ◽  
Astigmatism Correction ◽  
Long Time ◽  
Micro Holes ◽  
Cetyl Trimethyl Ammonium

Specimen support and astigmatism correction in Electron Microscopy are at least two areas in which lacey polymer films find extensive applications. Although their preparation has been studied for a very long time, present techniques still suffer from incomplete release of the film from its substrate and presence of a large number of pseudo holes in the film. Our method ensures complete removal of the entire lacey film from the substrate and fewer pseudo holes by pre-treating the substrate with Gum Arabic, which acts as a film release agent.The method is based on the classical condensation technique for preparing lacey films which is essentially deposition of minute water or ice droplets on the substrate and laying the polymer film over it, so that micro holes are formed corresponding to the droplets. A microscope glass slide (the substrate) is immersed in 2.0% (w/v) aq. CTAB (cetyl trimethyl ammonium bromide)-0.22% (w/v) aq.

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