ArticleNature communications2023
A single-domain green fluorescent protein catenane.
Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Tangled Tail of Mechanically Interlocked Peptides.Journal of the American Chemical Society · 2026Review
- Boolean logic-gated protein presentation through autonomously compiled molecular topology.Nature chemical biology · 2025Article
- Folds from fold: Exploring topological isoforms of a single-domain protein.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Sequence-encoded bioactive protein-multiblock polymer conjugates via quantitative one-pot iterative living polymerization.Nature communications · 2024Article
- A single-domain protein catenane of dihydrofolate reductase.National science review · 2023Article
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Authors and funding
7 authors.
Funding
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Abstract
Natural proteins exhibit rich structural diversity based on the folds of an invariably linear chain. Macromolecular catenanes that cooperatively fold into a single domain do not belong to the current protein universe, and their design and synthesis open new territories in chemistry. Here, we report the design, synthesis, and properties of a single-domain green fluorescent protein catenane via rewiring the connectivity of GFP's secondary motifs. The synthesis could be achieved in two steps via a pseudorotaxane intermediate or directly via expression in cellulo. Various proteins-of-interest may be inserted at the loop regions to give fusion protein catenanes where the two subunits exhibit enhanced thermal resilience, thermal stability, and mechanical stability due to strong conformational coupling. The strategy can be applied to other proteins with similar fold, giving rise to a family of single-domain fluorescent proteins. The results imply that there may be multiple protein topological variants with desirable functional traits beyond their corresponding linear protein counterparts, which are now made accessible and fully open for exploration.
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