ArticleProceedings of the National Academy of Sciences of the United States of America2021
Generation of ordered protein assemblies using rigid three-body fusion.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed.
- Cryo-EM structures of higher order Gephyrin oligomers reveal principles of inhibitory postsynaptic scaffold organization.Nature communications · 2026Article
- Self-assembling protein cages: from coiled-coil module to machine learning-drivenMaterials advances · 2026Review
- De novo design of light-responsive protein-protein interactions enables reversible formation of protein assemblies.Nature chemistry · 2025Article
- Disulfide-constrained Fabs overcome target size limitation for high-resolution single particle cryoEM.Nature communications · 2025Article
- Article
- An immobilized antibody-based affinity grid strategy for on-grid purification of target proteins enables high-resolution cryo-EM.Communications biology · 2024Article
- Rapid and automated design of two-component protein nanomaterials using ProteinMPNN.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Crystal structure of human serum albumin in complex with megabody reveals unique human and murine cross-reactive binding site.Protein science : a publication of the Protein Society · 2024Article
- Antigen spacing on protein nanoparticles influences antibody responses to vaccination.Cell reports · 2023Article
- Cryo-EM structure determination of small therapeutic protein targets at 3 Å-resolution using a rigid imaging scaffold.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Antigen spacing on protein nanoparticles influences antibody responses to vaccination.bioRxiv : the preprint server for biology · 2023Article
- Engineering Self-Assembling Protein Nanoparticles for Therapeutic Delivery.Bioconjugate chemistry · 2022Review
- Hallucinating symmetric protein assemblies.Science (New York, N.Y.) · 2022Article
- Protein Design: From the Aspect of Water Solubility and Stability.Chemical reviews · 2022Review
- Review
- Reconfigurable asymmetric protein assemblies through implicit negative design.Science (New York, N.Y.) · 2022Article
- Putting on molecular weight: Enabling cryo-EM structure determination of sub-100-kDa proteins.Current research in structural biology · 2022Review
- Generation of ordered protein assemblies using rigid three-body fusion.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Design of multi-scale protein complexes by hierarchical building block fusion.Nature communications · 2021Article
- Designed proteins assemble antibodies into modular nanocages.Science (New York, N.Y.) · 2021Article
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Authors and funding
19 authors.
Funding
Abstract
Protein nanomaterial design is an emerging discipline with applications in medicine and beyond. A long-standing design approach uses genetic fusion to join protein homo-oligomer subunits via α-helical linkers to form more complex symmetric assemblies, but this method is hampered by linker flexibility and a dearth of geometric solutions. Here, we describe a general computational method for rigidly fusing homo-oligomer and spacer building blocks to generate user-defined architectures that generates far more geometric solutions than previous approaches. The fusion junctions are then optimized using Rosetta to minimize flexibility. We apply this method to design and test 92 dihedral symmetric protein assemblies using a set of designed homodimers and repeat protein building blocks. Experimental validation by native mass spectrometry, small-angle X-ray scattering, and negative-stain single-particle electron microscopy confirms the assembly states for 11 designs. Most of these assemblies are constructed from designed ankyrin repeat proteins (DARPins), held in place on one end by α-helical fusion and on the other by a designed homodimer interface, and we explored their use for cryogenic electron microscopy (cryo-EM) structure determination by incorporating DARPin variants selected to bind targets of interest. Although the target resolution was limited by preferred orientation effects and small scaffold size, we found that the dual anchoring strategy reduced the flexibility of the target-DARPIN complex with respect to the overall assembly, suggesting that multipoint anchoring of binding domains could contribute to cryo-EM structure determination of small proteins.
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