scholarly journals Polychromatic in vivo imaging of multiple targets using visible and near infrared light

2013 ◽  
Vol 65 (8) ◽  
pp. 1112-1119 ◽  
Author(s):  
Hisataka Kobayashi ◽  
Michelle R. Longmire ◽  
Peter L. Choyke
Talanta ◽  
2021 ◽  
Vol 227 ◽  
pp. 122156
Author(s):  
Linna Huang ◽  
Feng Chen ◽  
Xia Zong ◽  
Qiujun Lu ◽  
Cuiyan Wu ◽  
...  

2020 ◽  
Vol 48 (6) ◽  
pp. 2657-2667
Author(s):  
Felipe Montecinos-Franjola ◽  
John Y. Lin ◽  
Erik A. Rodriguez

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.


Small ◽  
2008 ◽  
Vol 4 (7) ◽  
pp. 1001-1007 ◽  
Author(s):  
Takuro Niidome ◽  
Yasuyuki Akiyama ◽  
Kohei Shimoda ◽  
Takahito Kawano ◽  
Takeshi Mori ◽  
...  

2020 ◽  
Vol 32 (4) ◽  
pp. 187-193
Author(s):  
Ayşe Dündar ◽  
Mehmet Ertuğrul Çiftçi ◽  
Özlem İşman ◽  
Ali Murat Aktan

2020 ◽  
Vol 6 (44) ◽  
pp. eabb6165
Author(s):  
Lukas Pfeifer ◽  
Nong V. Hoang ◽  
Maximilian Scherübl ◽  
Maxim S. Pshenichnikov ◽  
Ben L. Feringa

Light-controlled artificial molecular machines hold tremendous potential to revolutionize molecular sciences as autonomous motion allows the design of smart materials and systems whose properties can respond, adapt, and be modified on command. One long-standing challenge toward future applicability has been the need to develop methods using low-energy, low-intensity, near-infrared light to power these nanomachines. Here, we describe a rotary molecular motor sensitized by a two-photon absorber, which efficiently operates under near-infrared light at intensities and wavelengths compatible with in vivo studies. Time-resolved spectroscopy was used to gain insight into the mechanism of energy transfer to the motor following initial two-photon excitation. Our results offer prospects toward in vitro and in vivo applications of artificial molecular motors.


ACS Nano ◽  
2020 ◽  
Vol 14 (4) ◽  
pp. 4178-4187 ◽  
Author(s):  
Yawen You ◽  
Fangfang Cao ◽  
Yajie Zhao ◽  
Qingqing Deng ◽  
Yanjuan Sang ◽  
...  

Nanoscale ◽  
2020 ◽  
Vol 12 (18) ◽  
pp. 10361-10368
Author(s):  
Yunxia Wu ◽  
Judun Zheng ◽  
Da Xing ◽  
Tao Zhang

Spatiotemporally controllable platform enables in situ fluorogenic labeling of alkene sialic acids based upconverting photoclick nanoprobe.


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