Synthesis and Properties of the p-Sulfonamide Analogue of the Green Fluorescent Protein (GFP) Chromophore: The Mimic of GFP Chromophore with Very Strong N–H Photoacid Strength

2018 ◽  
Vol 20 (7) ◽  
pp. 1768-1772 ◽  
Author(s):  
Yi-Hui Chen ◽  
Robert Sung ◽  
Kuangsen Sung
Keyword(s):  
Green Fluorescent Protein ◽  
Fluorescent Protein ◽  
Gfp Chromophore ◽  
Green Fluorescent

Fluorescent and “breathable” CO2 responsive vesicles inspired from green fluorescent protein

2017 ◽  
Vol 8 (40) ◽  
pp. 6283-6288 ◽  
Author(s):  
Lei Xu ◽  
Ning Ren ◽  
Ji Pang ◽  
Hongping Deng ◽  
Xinyuan Zhu ◽  
...  
Keyword(s):  
Green Fluorescent Protein ◽  
Block Copolymer ◽  
Fluorescent Protein ◽  
Gfp Chromophore ◽  
Green Fluorescent

CO2 responsive fluorescent vesicles from a GFP chromophore labeled block-copolymer could change their size and fluorescence to mimic jellyfish breathing.

scholarly journals Red-Shifted Aminated Derivatives of GFP Chromophore for Live-Cell Protein Labeling with Lipocalins

2018 ◽  
Vol 19 (12) ◽  
pp. 3778 ◽  
Author(s):  
Nina Bozhanova ◽  
Mikhail Baranov ◽  
Nadezhda Baleeva ◽  
Alexey Gavrikov ◽  
Alexander Mishin
Keyword(s):  
Green Fluorescent Protein ◽  
Live Cell Imaging ◽  
Cell Imaging ◽  
Fluorescent Protein ◽  
Live Cell ◽  
Protein Labeling ◽  
Cell Protein ◽  
Gfp Chromophore ◽  
Green Fluorescent ◽  
Derivatives Of

Fluorogens are an attractive type of dye for imaging applications, eliminating time-consuming washout steps from staining protocols. With just a handful of reported fluorogen-protein pairs, mostly in the green region of spectra, there is a need for the expansion of their spectral range. Still, the origins of solvatochromic and fluorogenic properties of the chromophores suitable for live-cell imaging are poorly understood. Here we report on the synthesis and labeling applications of novel red-shifted fluorogenic cell-permeable green fluorescent protein (GFP) chromophore analogs.

Synthesis and properties of geometrical 4-diarylmethylene analogs of the green fluorescent protein chromophore

2018 ◽  
Vol 16 (14) ◽  
pp. 2397-2401 ◽  
Author(s):  
Masahiro Ikejiri ◽  
Haruka Kojima ◽  
Yuumi Fugono ◽  
Aki Fujisaka ◽  
Yoshiko Chihara ◽  
...  
Keyword(s):  
Green Fluorescent Protein ◽  
Fluorescent Protein ◽  
Aggregation Induced Emission ◽  
Gfp Chromophore ◽  
Green Fluorescent

The E- and Z-isomers of E/Z-photoisomerizable diarylmethylene analogs of the GFP chromophore (geo-DAIN) produce different colors of aggregation-induced emission (AIE).

Against the NEER principle: The third type of photochromism for GFP chromophore derivatives

2021 ◽  
Author(s):  
Jun-Wei Liao ◽  
Robert Sung ◽  
Kuangsen Sung
Keyword(s):  
Excited State ◽  
Green Fluorescent Protein ◽  
Proton Transfer ◽  
Fluorescent Protein ◽  
Fluorescent Proteins ◽  
The Third ◽  
Excited State Proton Transfer ◽  
Gfp Chromophore ◽  
Green Fluorescent

Photochromism is the heart of photochromic fluorescent proteins. Excited-state proton transfer (ESPT) is the major photochromism for green fluorescent protein (GFP) and Z-E photoisomerization through τ-torsion is the major photochromism...

scholarly journals Snake Toxins Labeled by Green Fluorescent Protein or Its Synthetic Chromophore are New Probes for Nicotinic acetylcholine Receptors

2021 ◽  
Vol 8 ◽  
Author(s):  
Igor E. Kasheverov ◽  
Alexey I. Kuzmenkov ◽  
Denis S. Kudryavtsev ◽  
Ivan S. Chudetskiy ◽  
Irina V. Shelukhina ◽  
...  
Keyword(s):  
Green Fluorescent Protein ◽  
Nicotinic Acetylcholine Receptors ◽  
Acetylcholine Receptors ◽  
Fluorescent Protein ◽  
Full Length ◽  
Fluorescent Label ◽  
Muscle Type ◽  
Nicotinic Acetylcholine ◽  
Gfp Chromophore ◽  
Green Fluorescent

Fluorescence can be exploited to monitor intermolecular interactions in real time and at a resolution up to a single molecule. It is a method of choice to study ligand-receptor interactions. However, at least one of the interacting molecules should possess good fluorescence characteristics, which can be achieved by the introduction of a fluorescent label. Gene constructs with green fluorescent protein (GFP) are widely used to follow the expression of the respective fusion proteins and monitor their function. Recently, a small synthetic analogue of GFP chromophore (p-HOBDI-BF2) was successfully used for tagging DNA molecules, so we decided to test its applicability as a potential fluorescent label for proteins and peptides. This was done on α-cobratoxin (α-CbTx), a three-finger protein used as a molecular marker of muscle-type, neuronal α7 and α9/α10 nicotinic acetylcholine receptors (nAChRs), as well as on azemiopsin, a linear peptide neurotoxin selectively inhibiting muscle-type nAChRs. An activated N-hydroxysuccinimide ester of p-HOBDI-BF2 was prepared and utilized for toxin labeling. For comparison we used a recombinant α-CbTx fused with a full-length GFP prepared by expression of a chimeric gene. The structure of modified toxins was confirmed by mass spectrometry and their activity was characterized by competition with iodinated α-bungarotoxin in radioligand assay with respective receptor preparations, as well as by thermophoresis. With the tested protein and peptide neurotoxins, introduction of the synthetic GFP chromophore induced considerably lower decrease in their affinity for the receptors as compared with full-length GFP attachment. The obtained fluorescent derivatives were used for nAChR visualization in tissue slices and cell cultures.

How far can a single hydrogen bond tune the spectral properties of the GFP chromophore?

2015 ◽  
Vol 17 (31) ◽  
pp. 20056-20060 ◽  
Author(s):  
Hjalte V. Kiefer ◽  
Elie Lattouf ◽  
Natascha W. Persen ◽  
Anastasia V. Bochenkova ◽  
Lars H. Andersen
Keyword(s):  
Hydrogen Bond ◽  
Green Fluorescent Protein ◽  
Spectral Properties ◽  
Fluorescent Protein ◽  
Gfp Chromophore ◽  
Green Fluorescent ◽  
Hydrogen Bonded

Photoabsorption of the hydrogen-bonded HBDI·HBDI− dimer, simultaneously resembling the two states of the Green Fluorescent Protein chromophore, is measured in vacuum.

scholarly journals Mechanism of Color and Photoacidity Tuning for the Protonated Green Fluorescent Protein Chromophore

2020 ◽  
Author(s):  
Chi-Yun Lin ◽  
Steven Boxer
Keyword(s):  
Green Fluorescent Protein ◽  
Fluorescent Protein ◽  
Stokes Shift ◽  
Site Directed Mutagenesis ◽  
Color Tuning ◽  
Tuning Mechanism ◽  
Donor Acceptor ◽  
Form Model ◽  
Gfp Chromophore ◽  
Green Fluorescent

The neutral or A state of the green fluorescent protein (GFP) chromophore is a remarkable example of a photoacid naturally embedded in the protein environment and accounts for the large Stokes shift of GFP in response to near UV excitation. Its color tuning mechanism has been largely overlooked, as it is less preferable for imaging applications than the redder anionic or B state. Past studies, based on site-directed mutagenesis or solvatochromism of the isolated chromophore, have concluded that its color tuning range is much narrower than its anionic counterpart. However, as we performed extensive investigation on more GFP mutants, we found the color of the neutral chromophore to be much more sensitive to protein electrostatics. Electronic Stark spectroscopy reveals a fundamentally different electrostatic color tuning mechanism for the neutral state of the chromophore that demands a three-form model compared with that of the anionic state, which requires only two forms. Specifically, an underlying zwitterionic charge transfer state is required to explain its sensitivity to electrostatics. As the Stokes shift is tightly linked to the protonated chromophore’s photoacidity and excited-state proton transfer (ESPT), we infer design principles of the GFP chromophore as a photoacid through the color tuning mechanisms of both protonation states. The three-form model could also be applied to similar biological and nonbiological dyes and complements the failure of two-form model for donor–acceptor systems with localized electronic distributions.

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