scholarly journals Unique interactions between the chromophore and glutamate 16 lead to far-red emission in a red fluorescent protein

2009 ◽  
Vol 18 (2) ◽  
pp. 460-466 ◽  
Author(s):  
Xiaokun Shu ◽  
Lei Wang ◽  
Leslie Colip ◽  
Karen Kallio ◽  
S. James Remington
Keyword(s):  
Fluorescent Protein ◽  
Red Fluorescent Protein ◽  
Red Emission

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.

scholarly journals Novel Regeneration Approach for Creating Reusable FO-SPR Probes with NTA Surface Chemistry

Nanomaterials ◽  
2021 ◽  
Vol 11 (1) ◽  
pp. 186
Author(s):  
Jia-Huan Qu ◽  
Karen Leirs ◽  
Remei Escudero ◽  
Žiga Strmšek ◽  
Roman Jerala ◽  
...  
Keyword(s):  
Surface Chemistry ◽  
Fluorescent Protein ◽  
Cost Effective ◽  
Nitrilotriacetic Acid ◽  
Antibody Fragments ◽  
Rapid Screening ◽  
Red Fluorescent Protein ◽  
Effective Manner ◽  
Surface Regeneration ◽  
Sensitivity Specificity

To date, surface plasmon resonance (SPR) biosensors have been exploited in numerous different contexts while continuously pushing boundaries in terms of improved sensitivity, specificity, portability and reusability. The latter has attracted attention as a viable alternative to disposable biosensors, also offering prospects for rapid screening of biomolecules or biomolecular interactions. In this context here, we developed an approach to successfully regenerate a fiber-optic (FO)-SPR surface when utilizing cobalt (II)-nitrilotriacetic acid (NTA) surface chemistry. To achieve this, we tested multiple regeneration conditions that can disrupt the NTA chelate on a surface fully saturated with His6-tagged antibody fragments (scFv-33H1F7) over ten regeneration cycles. The best surface regeneration was obtained when combining 100 mM EDTA, 500 mM imidazole and 0.5% SDS at pH 8.0 for 1 min with shaking at 150 rpm followed by washing with 0.5 M NaOH for 3 min. The true versatility of the established approach was proven by regenerating the NTA surface for ten cycles with three other model system bioreceptors, different in their size and structure: His6-tagged SARS-CoV-2 spike fragment (receptor binding domain, RBD), a red fluorescent protein (RFP) and protein origami carrying 4 RFPs (Tet12SN-RRRR). Enabling the removal of His6-tagged bioreceptors from NTA surfaces in a fast and cost-effective manner can have broad applications, spanning from the development of biosensors and various biopharmaceutical analyses to the synthesis of novel biomaterials.

A brilliant monomeric red fluorescent protein to visualize cytoskeleton dynamics inDictyostelium

FEBS Letters ◽  
2004 ◽  
Vol 577 (1-2) ◽  
pp. 227-232 ◽  
Author(s):  
Markus Fischer ◽  
Ilka Haase ◽  
Evelyn Simmeth ◽  
Günther Gerisch ◽  
Annette Müller-Taubenberger
Keyword(s):  
Fluorescent Protein ◽  
Red Fluorescent Protein ◽  
Cytoskeleton Dynamics

Crystallization and preliminary X-ray diffraction analysis of the red fluorescent protein eqFP611

2003 ◽  
Vol 59 (7) ◽  
pp. 1253-1255 ◽  
Author(s):  
Karin Nienhaus ◽  
Beatrice Vallone ◽  
Fabiana Renzi ◽  
Jörg Wiedenmann ◽  
G. Ulrich Nienhaus
Keyword(s):  
Diffraction Analysis ◽  
Fluorescent Protein ◽  
Red Fluorescent Protein ◽  
X Ray Diffraction ◽  
X Ray

A pH-sensitive red fluorescent protein compatible with hydrophobic resin embedding

2017 ◽  
Author(s):  
Wenyan Guo ◽  
Yadong Gang ◽  
Xiuli Liu ◽  
Hongfu Zhou ◽  
Shaoqun Zeng
Keyword(s):  
Fluorescent Protein ◽  
Ph Sensitive ◽  
Red Fluorescent Protein
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