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Structural Analysis of a Genetically Encoded FRET Biosensor by SAXS and MD Simulations.

Ines Reinartz^1,2, Mona Sarter^3,4, Julia Otten⁵

¹Institute for Automation and Applied Informatics, Karlsruhe Institute of Technology, Hermann-von-Helmholtz-Platz 1, 76344 Eggenstein-Leopoldshafen, Germany.

Sensors (Basel, Switzerland)

|July 2, 2021

Summary

This summary is machine-generated.

Designing effective Förster resonance energy transfer (FRET)-based biosensors requires careful linker engineering. Attaching fluorescent proteins (FPs) to glucose binding proteins demonstrates that optimizing one FP

Keywords:

coarse-grained molecular dynamics (MD)glucose sensor green fluorescence protein (GFP)single-molecule FRET small angle X-ray scattering (SAXS)

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Area of Science:

Biochemistry
Biophysics
Molecular Biology

Background:

Ligand binding proteins can be engineered into Förster resonance energy transfer (FRET)-based biosensors by incorporating two fluorescent proteins (FPs).
These biosensors leverage conformational changes upon ligand binding to generate a measurable FRET signal.

Purpose of the Study:

To investigate the impact of linker sequences on the performance of FRET-based glucose biosensors.
To correlate structural changes measured by small angle X-ray scattering (SAXS) with FRET efficiency in glucose sensors.

Main Methods:

Construction and characterization of glucose sensors with varying linker sequences between glucose binding protein and FPs.
Measurement of glucose-induced conformational changes using small angle X-ray scattering (SAXS).
Comparison of SAXS data with existing single-molecule FRET results.
Coarse-grained molecular dynamics simulations of selected sensor constructs.

Main Results:

Different linker sequences resulted in varying degrees of glucose-induced conformational changes and FRET signal alterations.
One sensor construct showed significant changes in both energy transfer and radius of gyration upon glucose binding.
Molecular dynamics simulations highlighted the critical role of donor FP attachment in translating conformational changes to FRET signals.
The acceptor FP's attachment was found to be less critical for signal transduction.

Conclusions:

The precise attachment of the donor fluorescent protein is essential for efficient FRET signal transduction in response to glucose binding.
Optimizing the linker for one FP is sufficient for a functional FRET-based biosensor.
This study provides insights into rational design principles for engineering advanced FRET biosensors.