ReviewMolecules (Basel, Switzerland)2022
Locking the GFP Fluorophore to Enhance Its Emission Intensity.
Review in Molecules (Basel, Switzerland), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Photoinduced chromophore dissociation resulting in aggregation-induced red fluorescence.Communications biology · 2025Article
- Tailoring Peptide Coacervates for Advanced Biotechnological Applications: Enhancing Control, Encapsulation, and Antioxidant Properties.ACS applied materials & interfaces · 2025Article
- Introducing Rigidity into the GFP Chromophore via a Boron Bridge: Insights and Application in Two-Photon Imaging.Organic letters · 2025Article
- Pseudo-Ring Methodology to Control the Conformations of Macrocyclic Peptides.Chemistry (Weinheim an der Bergstrasse, Germany) · 2025Article
- A Molecular Hybrid of the GFP Chromophore and 2,2'-Bipyridine: An Accessible Sensor for ZnInternational journal of molecular sciences · 2024Article
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Authors and funding
4 authors.
Funding
Abstract
The Green Fluorescent Protein (GFP) and its analogues have been widely used as fluorescent biomarkers in cell biology. Yet, the chromophore responsible for the fluorescence of the GFP is not emissive when isolated in solution, outside the protein environment. The most accepted explanation is that the quenching of the fluorescence results from the rotation of the aryl-alkene bond and from the Z/E isomerization. Over the years, many efforts have been performed to block these torsional rotations, mimicking the environment inside the protein β-barrel, to restore the emission intensity. Molecule rigidification through chemical modifications or complexation, or through crystallization, is one of the strategies used. This review presents an overview of the strategies developed to achieve highly emissive GFP chromophore by hindering the torsional rotations.
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Registered trials
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