ArticleProceedings of the National Academy of Sciences of the United States of America2016
Flexible, symmetry-directed approach to assembling protein cages.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed, 101 citations in OpenAlex.
- Engineering complexity into protein-based biomaterials for biomedical applications.Nature reviews. Materials · 2026Article
- Self-assembling protein cages: from coiled-coil module to machine learning-drivenMaterials advances · 2026Review
- Pleomorphism in Wild-Type and Engineered PP7 Virus-Like Particles.Small (Weinheim an der Bergstrasse, Germany) · 2025Article
- Inverse Design of DNA-Programmable Protein Colloidal Crystals.Journal of the American Chemical Society · 2025Article
- Dynamic Assembly of Pentamer-Based Protein Nanotubes.ACS nano · 2025Article
- Article
- Design of a symmetry-broken tetrahedral protein cage by a method of internal steric occlusion.Protein science : a publication of the Protein Society · 2024Article
- Design of a symmetry-broken tetrahedral protein cage by a method of internal steric occlusion.bioRxiv : the preprint server for biology · 2023Article
- Protein Design: From the Aspect of Water Solubility and Stability.Chemical reviews · 2022Review
- Protein Assembly by Design.Chemical reviews · 2021Review
- Experimental and theoretical study on converting myoglobin into a stable domain-swapped dimer by utilizing a tight hydrogen bond network at the hinge region.RSC advances · 2021Article
- Artificial Organelles: Towards Adding or Restoring Intracellular Activity.Chembiochem : a European journal of chemical biology · 2021Review
- Generation of ordered protein assemblies using rigid three-body fusion.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Structure-based design of novel polyhedral protein nanomaterials.Current opinion in microbiology · 2021Review
- Protein-based antigen presentation platforms for nanoparticle vaccines.NPJ vaccines · 2021Review
- De Novo Designed Peptide and Protein Hairpins Self-Assemble into Sheets and Nanoparticles.Small (Weinheim an der Bergstrasse, Germany) · 2021Review
- Self-assembly and regulation of protein cages from pre-organised coiled-coil modules.Nature communications · 2021Article
- Article
- A complete rule set for designing symmetry combination materials from protein molecules.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Analyzing microglial-associated Aβ in Alzheimer's disease transgenic mice with a novel mid-domain Aβ-antibody.Scientific reports · 2020Article
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Authors and funding
10 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The assembly of individual protein subunits into large-scale symmetrical structures is widespread in nature and confers new biological properties. Engineered protein assemblies have potential applications in nanotechnology and medicine; however, a major challenge in engineering assemblies de novo has been to design interactions between the protein subunits so that they specifically assemble into the desired structure. Here we demonstrate a simple, generalizable approach to assemble proteins into cage-like structures that uses short de novo designed coiled-coil domains to mediate assembly. We assembled eight copies of a C3-symmetric trimeric esterase into a well-defined octahedral protein cage by appending a C4-symmetric coiled-coil domain to the protein through a short, flexible linker sequence, with the approximate length of the linker sequence determined by computational modeling. The structure of the cage was verified using a combination of analytical ultracentrifugation, native electrospray mass spectrometry, and negative stain and cryoelectron microscopy. For the protein cage to assemble correctly, it was necessary to optimize the length of the linker sequence. This observation suggests that flexibility between the two protein domains is important to allow the protein subunits sufficient freedom to assemble into the geometry specified by the combination of C4 and C3 symmetry elements. Because this approach is inherently modular and places minimal requirements on the structural features of the protein building blocks, it could be extended to assemble a wide variety of proteins into structures with different symmetries.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.