Graphene-Based Steganographically Aptasensing System for Information Computing, Encryption and Hiding, Fluorescence Sensing and in Vivo Imaging of Fish Pathogens

Qiu Yan Zhu; Fu Rui Zhang; Yan Du; Xin Xing Zhang; Jiao Yang Lu; Qing Feng Yao; Wei Tao Huang; Xue Zhi Ding; Li Qiu Xia

doi:10.1021/acsami.8b22592

Graphene-Based Steganographically Aptasensing System for Information Computing, Encryption and Hiding, Fluorescence Sensing and in Vivo Imaging of Fish Pathogens

ACS Applied Materials & Interfaces ◽

10.1021/acsami.8b22592 ◽

2019 ◽

Vol 11 (9) ◽

pp. 8904-8914 ◽

Cited By ~ 5

Author(s):

Qiu Yan Zhu ◽

Fu Rui Zhang ◽

Yan Du ◽

Xin Xing Zhang ◽

Jiao Yang Lu ◽

...

Keyword(s):

In Vivo Imaging ◽

Fluorescence Sensing ◽

Fish Pathogens

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Iron(III)-Selective Chelation-Enhanced Fluorescence Sensing for In Vivo Imaging Applications

Chemistry - An Asian Journal ◽

10.1002/asia.201500415 ◽

2015 ◽

Vol 10 (9) ◽

pp. 1898-1902 ◽

Cited By ~ 12

Author(s):

Lin E. Guo ◽

Xin Yi Liu ◽

Huan Wang ◽

Qiu Ling Chen ◽

Guang Ke Wang ◽

...

Keyword(s):

In Vivo Imaging ◽

Fluorescence Sensing ◽

Enhanced Fluorescence ◽

Chelation Enhanced Fluorescence

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

Biochemical Society Transactions ◽

10.1042/bst20200444 ◽

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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