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A single-domain green fluorescent protein catenane
Zhiyu Qu1,2,3,4, Jing Fang1,2,3,4, Yu-Xiang Wang1,2,3,4
1Beijing National Laboratory for Molecular Sciences, Beijing, P. R. China.
Nature Communications
|June 13, 2023
Summary
Researchers designed and synthesized a novel single-domain green fluorescent protein catenane, a unique macromolecular structure. This breakthrough opens new avenues for creating topologically diverse proteins with enhanced stability and functionality.
Area of Science:
- Biochemistry
- Chemical Biology
- Protein Engineering
Background:
- Proteins typically exist as linear chains with diverse folds.
- Macromolecular catenanes, topologically interlocked rings, are not found in nature and represent a new frontier in chemistry.
Purpose of the Study:
- To design and synthesize a single-domain green fluorescent protein (GFP) catenane.
- To explore the properties and potential applications of this novel protein topology.
Main Methods:
- Rewiring the connectivity of GFP's secondary motifs.
- Synthesis via a pseudorotaxane intermediate or direct in cellulo expression.
- Insertion of proteins-of-interest into loop regions to create fusion protein catenanes.
Main Results:
- Successful design and synthesis of a single-domain GFP catenane.
- Demonstrated enhanced thermal, mechanical, and conformational stability in fusion protein catenanes.
- Established a versatile strategy applicable to other proteins with similar folds.
Conclusions:
- Single-domain protein catenanes represent a novel class of macromolecules beyond the natural protein universe.
- This work provides a method for creating topologically diverse proteins with potentially superior functional traits.
- The developed strategy enables the exploration of new protein variants with enhanced stability and customizable functionalities.
