ArticleNature communications2019
Covalently-assembled single-chain protein nanostructures with ultra-high stability.
Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
22 citing papers in PubMed.
- 2D Assemblies Based on a Tetraphenylethylene D,L-Cyclic Peptide Scaffold.Angewandte Chemie (International ed. in English) · 2025Article
- EnhancingApplied and environmental microbiology · 2025Article
- Beyond Dimerization: Harnessing Tetrameric Coiled-Coils for Nanostructure Assembly.Angewandte Chemie (International ed. in English) · 2025Article
- Microbial Production of High-Performance Fibers from Muscle Protein Titin.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Biomolecular condensates form spatially inhomogeneous network fluids.Nature communications · 2024Article
- Preorganized cyclic modules facilitate the self-assembly of protein nanostructures.Chemical science · 2024Article
- Programming interchangeable and reversible heterooligomeric protein self-assembly using a bifunctional ligand.Chemical science · 2024Article
- Genetically Engineered Protein-Based Bioadhesives with Programmable Material Properties.ACS applied materials & interfaces · 2023Article
- Protein-Based Hydrogels and Their Biomedical Applications.Molecules (Basel, Switzerland) · 2023Review
- Bi-terminal fusion of intrinsically-disordered mussel foot protein fragments boosts mechanical strength for protein fibers.Nature communications · 2023Article
- Microbial Synthesis of High-Molecular-Weight, Highly Repetitive Protein Polymers.International journal of molecular sciences · 2023Review
- Voltage controlled shutter regulates channel size and motion direction of protein aperture as durable nano-electric rectifier-----An opinion in biomimetic nanoaperture.Biomaterials · 2022Article
- Transient Antibiotic Tolerance Triggered by Nutrient Shifts From Gluconeogenic Carbon Sources to Fatty Acid.Frontiers in microbiology · 2022Article
- A Biosynthetic Hybrid Spidroin-Amyloid-Mussel Foot Protein for Underwater Adhesion on Diverse Surfaces.ACS applied materials & interfaces · 2021Article
- Amyloids as Building Blocks for Macroscopic Functional Materials: Designs, Applications and Challenges.International journal of molecular sciences · 2021Review
- Symmetry-derived structure directing agents for two-dimensional crystals of arbitrary colloids.Soft matter · 2021Article
- Microbial production of megadalton titin yields fibers with advantageous mechanical properties.Nature communications · 2021Article
- A nanobody toolbox targeting dimeric coiled-coil modules for functionalization of designed protein origami structures.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- TriangularACS chemical biology · 2021Article
- Self-assembly and regulation of protein cages from pre-organised coiled-coil modules.Nature communications · 2021Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
Protein nanostructures with precisely defined geometries have many potential applications in catalysis, sensing, signal processing, and drug delivery. While many de novo protein nanostructures have been assembled via non-covalent intramolecular and intermolecular interactions, a largely unexplored strategy is to construct nanostructures by covalently linking multiple individually folded proteins through site-specific ligations. Here, we report the synthesis of single-chain protein nanostructures with triangular and square shapes made using multiple copies of a three-helix bundle protein and split intein chemistry. Coarse-grained simulations confirm the experimentally observed flexibility of these nanostructures, which is optimized to produce triangular structures with high regularity. These single-chain nanostructures also display ultra-high thermostability, resist denaturation by chaotropes and organic solvents, and have applicability as scaffolds for assembling materials with nanometer resolution. Our results show that site-specific covalent ligation can be used to assemble individually folded proteins into single-chain nanostructures with bespoke architectures and high stabilities.
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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.