Functional Near Infrared-Emitting Cr3+/Pr3+ Co-Doped Zinc Gallogermanate Persistent Luminescent Nanoparticles with Superlong Afterglow for in Vivo Targeted Bioimaging

2013 ◽  
Vol 135 (38) ◽  
pp. 14125-14133 ◽  
Author(s):  
Abdukader Abdukayum ◽  
Jia-Tong Chen ◽  
Qiang Zhao ◽  
Xiu-Ping Yan
Keyword(s):  
Near Infrared ◽  
Luminescent Nanoparticles ◽  
Co Doped

One-step synthesis of amino-functionalized ultrasmall near infrared-emitting persistent luminescent nanoparticles for in vitro and in vivo bioimaging

Nanoscale ◽  
2016 ◽  
Vol 8 (18) ◽  
pp. 9798-9804 ◽  
Author(s):  
Junpeng Shi ◽  
Xia Sun ◽  
Jianfei Zhu ◽  
Jinlei Li ◽  
Hongwu Zhang
Keyword(s):  
Near Infrared ◽  
One Step ◽  
Luminescent Nanoparticles

Improved Near-Infrared Up-Conversion Emission of Tm3+ Sensitized by Yb3+ and Ho3+ in LuF3 Nanocrystals

2016 ◽  
Vol 16 (4) ◽  
pp. 3664-3668 ◽  
Author(s):  
Xuhui Xu ◽  
Yumei Wu ◽  
Wenjuan Bian ◽  
Xue Yu ◽  
Buhao Zhang ◽  
...  
Keyword(s):  
Near Infrared ◽  
Laser Excitation ◽  
Green Emission ◽  
Color Displays ◽  
Bio Imaging ◽  
Nir Emission ◽  
Average Size ◽  
Co Doped

In the present work, mono-disperse and uniform orthorhombic lutetium fluoride (LuF3) nanocrystals with an average size of about 35 nm have been successfully synthesized by a simple ionothermal method without any template. The infrared (IR) to visible up-conversion (UC) photoluminescence of LuF3 doped with Yb3+, Tm3+, and Ho3+ under 980 nm excitation was systemically studied. The intensity of near infrared (NIR) to visible up-conversion emission of Tm3+ was improved efficiently by adding Yb3+ and Ho3+ in LuF3, especially for the broad NIR emission band located at 812 nm. Meanwhile, compared to the Yb3+ and Tm3+ co-doped LuF3, the ratio of red to green emission in the Yb3+, Tm3+, and Ho3+ co-doped LuF3 changed greatly, and a bright yellowish-green emission was observed under 980 nm laser excitation. It shows that Yb3+, Tm3+ and Ho3+ co-doped LuF3 nanocrystals provided a potential application in vitro and in vivo bio-imaging, color displays and optical storage.

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.

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