ArticleNature nanotechnology2024
De novo design of pH-responsive self-assembling helical protein filaments.
Article in Nature nanotechnology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
32 citing papers in PubMed, 60 citations in OpenAlex.
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- A histidine switch controls the pH-responsive self-assembly of a helical protein filament.bioRxiv : the preprint server for biology · 2026Article
- Protein design and RNA design: Perspectives.Quantitative biology (Beijing, China) · 2026Article
- Artificial intelligence driven protein design and sustainable nanomedicine for advanced theranostics.Bioactive materials · 2026Review
- Redesign of TALE proteins for DNA-templated assembly of protein fibers.Nature communications · 2026Article
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- Engineering complexity into protein-based biomaterials for biomedical applications.Nature reviews. Materials · 2026Article
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- Supramolecular Assemblies of Self-Immolative Janus Dendrimers With Rapid Photodegradation Response.Small (Weinheim an der Bergstrasse, Germany) · 2026Article
- Protein-inducible ribosomal frameshifting enables programmable translational control for genetic circuit design in Escherichia coli.Journal of biological engineering · 2026Article
- Nanorobots hold PD-L1 and break membrane of colorectal cancer cells for immunotherapy.Nature nanotechnology · 2026Article
- Sequence Prediction, Structural Modelling and the Challenges of Plasticity in Coiled Coils.Sub-cellular biochemistry · 2026Review
- Designability of α-Helical Protein Filaments.Sub-cellular biochemistry · 2026Review
- De novo design of light-responsive protein-protein interactions enables reversible formation of protein assemblies.Nature chemistry · 2025Article
- Monomer exchange dynamics in ureido-pyrimidinone supramolecular polymersJournal of materials chemistry. B · 2025Article
- Article
- Tumor Microenvironment-Responsive Nanomedicines for Potentiating Cancer Immunotherapy.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Review
- Mutation-induced filaments of folded proteins are inert and non-toxic in a cellular system.Molecular systems biology · 2025Article
- Article
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Authors and funding
14 authors at 4 institutions in 2 countries.
Funding
Abstract
Biological evolution has led to precise and dynamic nanostructures that reconfigure in response to pH and other environmental conditions. However, designing micrometre-scale protein nanostructures that are environmentally responsive remains a challenge. Here we describe the de novo design of pH-responsive protein filaments built from subunits containing six or nine buried histidine residues that assemble into micrometre-scale, well-ordered fibres at neutral pH. The cryogenic electron microscopy structure of an optimized design is nearly identical to the computational design model for both the subunit internal geometry and the subunit packing into the fibre. Electron, fluorescent and atomic force microscopy characterization reveal a sharp and reversible transition from assembled to disassembled fibres over 0.3 pH units, and rapid fibre disassembly in less than 1 s following a drop in pH. The midpoint of the transition can be tuned by modulating buried histidine-containing hydrogen bond networks. Computational protein design thus provides a route to creating unbound nanomaterials that rapidly respond to small pH changes.
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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.