ArticleNature chemistry2019
Stimulus-responsive self-assembly of protein-based fractals by computational design.
Article in Nature chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Identifying nature's smallest fractals.Nature structural & molecular biology · 2024Article
- Non-destructive real-time monitoring and investigation of the self-assembly process using fluorescent probes.Chemical science · 2024Review
- A closed-loop catalytic nanoreactor system on a transistor.Science advances · 2023Article
- N-terminal region of Drosophila melanogaster Argonaute2 forms amyloid-like aggregates.BMC biology · 2023Article
- Asymmetric block copolymer membrane fabrication mechanism through self-assembly and non-solvent induced phase separation (SNIPS) process.Scientific reports · 2022Article
- Silica Nanoparticles with Virus-Mimetic Spikes Enable Efficient siRNA Delivery In Vitro and In Vivo.Research (Washington, D.C.) · 2022Article
- Lighting up solid states using a rubber.Nature communications · 2021Article
- Manifold of self-assembly of aRSC advances · 2020Article
- Fabrication of Pascal-triangle Lattice of Proteins by Inducing Ligand Strategy.Angewandte Chemie (International ed. in English) · 2020Article
- Diverse protein assembly driven by metal and chelating amino acids with selectivity and tunability.Nature communications · 2019Article
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Authors and funding
19 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Fractal topologies, which are statistically self-similar over multiple length scales, are pervasive in nature. The recurrence of patterns in fractal-shaped branched objects, such as trees, lungs and sponges, results in a high surface area to volume ratio, which provides key functional advantages including molecular trapping and exchange. Mimicking these topologies in designed protein-based assemblies could provide access to functional biomaterials. Here we describe a computational design approach for the reversible self-assembly of proteins into tunable supramolecular fractal-like topologies in response to phosphorylation. Guided by atomic-resolution models, we develop fusions of Src homology 2 (SH2) domain or a phosphorylatable SH2-binding peptide, respectively, to two symmetric, homo-oligomeric proteins. Mixing the two designed components resulted in a variety of dendritic, hyperbranched and sponge-like topologies that are phosphorylation-dependent and self-similar over three decades (~10 nm-10 μm) of length scale, in agreement with models from multiscale computational simulations. Designed assemblies perform efficient phosphorylation-dependent capture and release of cargo proteins.
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31209296What OpenQuestion holds
Registered trials
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.