Journal
CHEMOSENSORS
Volume 9, Issue 8, Pages -Publisher
MDPI
DOI: 10.3390/chemosensors9080234
Keywords
polarity sensor; green fluorescent protein chromophore; fluorogenicity; twisted intramolecular charge transfer; ultrafast spectroscopy; multivariable analysis
Funding
- U.S. NSF [CHE-2003550]
- Russian Science Foundation [18-73-10105]
- Russian Science Foundation [18-73-10105] Funding Source: Russian Science Foundation
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Researchers discovered a novel fluorophore by incorporating a -NMe2 group into a conformationally locked GFP scaffold, showing marked solvent-polarity-dependent behavior. They revealed the formation of a TICT state through fs-TA spectroscopy and quantum calculations, which effectively quenches fluorescence. The polarity dependence of the FS -> TICT reaction barrier was mainly modulated by H-bonding capability instead of solvent viscosity.
We discovered a novel fluorophore by incorporating a dimethylamino group (-NMe2) into the conformationally locked green fluorescent protein (GFP) scaffold. It exhibited a marked solvent-polarity-dependent fluorogenic behavior and can potentially find broad applications as an environment-polarity sensor in vitro and in vivo. The ultrafast femtosecond transient absorption (fs-TA) spectroscopy in combination with quantum calculations revealed the presence of a twisted intramolecular charge transfer (TICT) state, which is formed by rotation of the -NMe2 group in the electronic excited state. In contrast to the bright fluorescent state (FS), the TICT state is dark and effectively quenches fluorescence upon formation. We employed a newly developed multivariable analysis approach to the FS lifetime in various solvents and showed that the FS -> TICT reaction barrier is mainly modulated by H-bonding capability instead of viscosity of the solvent, accounting for the observed polarity dependence. These deep mechanistic insights are further corroborated by the dramatic loss of fluorogenicity for two similar GFP-derived chromophores in which the rotation of the -NMe2 group is inhibited by structural locking.
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