Locking the GFP Fluorophore to Enhance Its Emission Intensity

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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 beta-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.

keywords

GREEN FLUORESCENT PROTEIN; CONFORMATIONALLY LOCKED CHROMOPHORES; INTRAMOLECULAR PROTON-TRANSFER; CONFINED CHROMOPHORES; STATE; ANALOGS; ACTIVATION; BENZOXAZOLE; MECHANISM

subject category

Biochemistry & Molecular Biology; Chemistry

authors

Ferreira, JRM; Esteves, CIC; Marques, MMB; Guieu, S

our authors

foto Samuel Jacques André Guieu

Samuel Jacques André Guieu

Junior Researcher

Groups

G1 - Porous Materials and Nanosystems

Projects

CICECO - Aveiro Institute of Materials (UID/CTM/50011/2019)

CICECO - Aveiro Institute of Materials (UIDB/50011/2020)

CICECO - Aveiro Institute of Materials (UIDP/50011/2020)

acknowledgements

Thanks are due to the University of Aveiro, FCT/MEC, Centro 2020 and Portugal2020, the COMPETE program, and the European Union (FEDER program) via the financial support to the LAQV-REQUIMTE (UIDB/50006/2020 and UIDP/50006/2020), to the CICECO-Aveiro Institute of Materials (UID/CTM/50011/2019, UIDB/50011/2020 and UIDP/50011/2020), financed by national funds through the FCT/MCTES, to the Portuguese NMR Network. SG is supported by national funds (OE), through FCT, I.P., in the scope of the framework contract foreseen in the numbers 4, 5, and 6 of the article 23, of the Decree-Law 57/2016, of August 29, changed by Law 57/2017, of July 19. JRMF. Thanks FCT and ESF (European Social Fund) through POCH (Programa Operacional Capital Humano) for her PhD grant (UI/BD/151272/2021).

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Publication Details

type
Journal Article
year
2023
journal
MOLECULES
volume
28
article number
234
publisher
MDPI
issue
1
digital object identifier
10.3390/molecules28010234
web of science article identifier
WOS:000909565300001

Journal Metrics (JCR 2019)

Journal Impact Factor
3.267
Journal Impact Factor (5 yrs)
3.589
category normalized journal percentile
56.714

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