ArticleCommunications biology2021
Design of functionalised circular tandem repeat proteins with longer repeat topologies and enhanced subunit contact surfaces.
Article in Communications biology, 2021. 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.
- Molecular and Structural Characterization of an Immunopurified Telomerase fromMicroorganisms · 2025Article
- Rationally seeded computational protein design of ɑ-helical barrels.Nature chemical biology · 2024Article
- De novo design of knotted tandem repeat proteins.Nature communications · 2023Article
- Design of stimulus-responsive two-state hinge proteins.Science (New York, N.Y.) · 2023Article
- Profiling human pathogenic repeat expansion regions by synergistic and multi-level impacts on molecular connections.Human genetics · 2023Article
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Authors and funding
10 authors.
Funding
Abstract
Circular tandem repeat proteins ('cTRPs') are de novo designed protein scaffolds (in this and prior studies, based on antiparallel two-helix bundles) that contain repeated protein sequences and structural motifs and form closed circular structures. They can display significant stability and solubility, a wide range of sizes, and are useful as protein display particles for biotechnology applications. However, cTRPs also demonstrate inefficient self-assembly from smaller subunits. In this study, we describe a new generation of cTRPs, with longer repeats and increased interaction surfaces, which enhanced the self-assembly of two significantly different sizes of homotrimeric constructs. Finally, we demonstrated functionalization of these constructs with (1) a hexameric array of peptide-binding SH2 domains, and (2) a trimeric array of anti-SARS CoV-2 VHH domains. The latter proved capable of sub-nanomolar binding affinities towards the viral receptor binding domain and potent viral neutralization function.
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