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Protein Dynamics in Living Cells

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Using Protein Design and Directed Evolution to Monomerize a Bright Near-Infrared Fluorescent Protein.

Xiuhong Hu^1,2, Yang Xu^1,2, Junxi Yi^1,3

¹Department of Rheumatology and Immunology, The First Affiliated Hospital of USTC, Center for Advanced Interdisciplinary Science and Biomedicine of IHM, Hefei National Center for Interdisciplinary Sciences at the Microscale, Division of Life Sciences and Medicine, University of Science and Technology of China, Hefei, Anhui 230027, China.

ACS Synthetic Biology

|March 29, 2024

Summary

This summary is machine-generated.

Researchers engineered a bright, monomeric near-infrared fluorescent protein (DMsmURFP) from a dimeric precursor. This novel protein is stable, suitable for in vivo bioimaging, and developed using a versatile protein design strategy.

Keywords:

biliverdin bioimaging near-infrared fluorescent protein protein design protein monomerization

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Area of Science:

Biochemistry
Molecular Biology
Biotechnology

Background:

Small ultrared fluorescent protein (smURFP) is a dimeric near-infrared (NIR) fluorescent protein.
Its dimeric nature and biliverdin chromophore binding at the dimer interface limit its application in certain bioimaging techniques.

Purpose of the Study:

To engineer a monomeric NIR fluorescent protein based on smURFP for improved bioimaging suitability.
To develop a novel protein design strategy applicable to other multimeric proteins.

Main Methods:

Protein engineering using backbone design to create a monomeric variant of smURFP.
Directed evolution to enhance fluorescence properties.
X-ray crystallography to determine the structure of the designed protein.
In vivo imaging in mammalian systems to demonstrate utility.

Main Results:

A monomeric protein with weak fluorescence was initially designed.
Directed evolution yielded designed monomeric smURFP (DMsmURFP), a bright, stable, and monomeric NIR FP.
Crystal structures confirmed the designed monomeric architecture.
DMsmURFP demonstrated successful application in in vivo mammalian imaging.

Conclusions:

A novel strategy for monomerizing multimeric proteins via backbone design was successfully implemented.
DMsmURFP is a bright, stable, and monomeric NIR FP suitable for advanced bioimaging applications.
The protein design approach offers a versatile method for developing new fluorescent proteins and engineering other multimeric proteins.