Engineering of Tunable Allosteric-like Fluorogenic Protein Sensors

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Broch, Fanny | El Hajji, Lina | Pietrancosta, Nicolas | Gautier, Arnaud

Edité par CCSD ; American Chemical Society -

International audience. Optical protein sensors that enable to detect relevant biomolecules of interest play central roles in biological research. Coupling fluorescent reporters to protein sensing units has enabled the development of a wide range of biosensors that recognize analytes with high selectivity. In these sensors, analyte recognition induces a conformational change of the protein sensing unit that can modulate the optical signal of the fluorescent reporter. Here, we explore various designs for the creation of tunable allosteric-like fluorogenic protein sensors through incorporation of sensing protein units within the chemogenetic fluorescence-activating and absorption-shifting tag (FAST) that selectively binds and stabilizes the fluorescent state of 4-hydroxybenzylidene rhodanine (HBR) analogs. Conformational coupling allowed us to design analyte-responsive optical protein sensors through allosteric-like modulation of fluorogen binding.

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