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Allosteric Regulation

Allosteric Regulation

Allosteric regulation of enzymes occurs when the binding of an effector molecule to a site that is different from the active site causes a change in the enzymatic activity. This alternate site is called an allosteric site, and an enzyme can contain more than one of these sites. Allosteric regulation can either be positive or negative, resulting in an increase or decrease in enzyme activity. Most enzymes that display allosteric regulation are metabolic enzymes involved in the degradation or...

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Engineering of Tunable Allosteric-like Fluorogenic Protein Sensors.

Fanny Broch¹, Lina El Hajji¹, Nicolas Pietrancosta^1,2

¹Sorbonne Université, École Normale Supérieure, Université PSL, CNRS, Laboratoire des Biomolécules, LBM, 75005 Paris, France.

|October 13, 2023

Summary

Researchers developed novel optical protein sensors by integrating sensing units with the FAST (fluorescence-activating and absorption-shifting tag) system. This innovation enables tunable, analyte-responsive biosensors through allosteric modulation of fluorogen binding.

Keywords:

allosteric protein sensors analyte sensing chemogenetic fluorescent reporters optical sensors

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Area of Science:

Biochemistry
Molecular Biology
Biotechnology

Background:

Optical protein sensors are crucial for detecting biomolecules in biological research.
Existing biosensors utilize fluorescent reporters coupled with protein sensing units for selective analyte recognition.
Analyte binding typically induces conformational changes that alter the reporter's optical signal.

Purpose of the Study:

To design tunable, allosteric-like fluorogenic protein sensors.
To explore the incorporation of sensing protein units within the chemogenetic fluorescence-activating and absorption-shifting tag (FAST) system.
To achieve analyte-responsive modulation of fluorogen binding.

Main Methods:

Incorporation of protein sensing units into the FAST system.
Utilizing FAST's ability to bind and stabilize fluorescent states of 4-hydroxybenzylidene rhodanine (HBR) analogs.
Engineering conformational coupling between sensing units and the FAST-HBR complex.

Main Results:

Demonstrated the creation of tunable, allosteric-like fluorogenic protein sensors.
Showcased analyte-responsive modulation of fluorogen binding through conformational changes.
Successfully designed novel optical protein sensors with integrated sensing capabilities.

Conclusions:

The developed FAST-based system enables the design of versatile, analyte-responsive optical protein sensors.
Conformational coupling provides a powerful strategy for engineering biosensors with tunable optical outputs.
This approach advances the development of sophisticated tools for biological research and diagnostics.