ArticleProtein science : a publication of the Protein Society2023
De novo design of monomeric helical bundles for pH-controlled membrane lysis.
Article in Protein science : a publication of the Protein Society, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 10 citations in OpenAlex.
- Engineered internal architecture of core-shell lipid nanoparticles promotes efficient mRNA endosomal release.Nature communications · 2026Article
- Recent Advances in pH-Responsive Liposomes: Lessons Learnt and New Directions in Nanomedicine Development.Materials (Basel, Switzerland) · 2025Review
- A De Novo Designed Metalloprotein Displays Variable Thermal Stability and Binding Stoichiometry with Transition Metal Ions.Chembiochem : a European journal of chemical biology · 2025Article
- Protein-based nanoparticles for therapeutic nucleic acid delivery.Biomaterials · 2024Review
- ProteinMPNN Recovers Complex Sequence Properties of Transmembrane β-barrels.bioRxiv : the preprint server for biology · 2024Article
- Computational investigation of missense somatic mutations in cancer and potential links to pH-dependence and proteostasis.PloS one · 2024Article
- De novo design of monomeric helical bundles for pH-controlled membrane lysis.Protein science : a publication of the Protein Society · 2023Article
Corrections and comments
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Authors and funding
12 authors at 3 institutions in 2 countries.
Funding
Abstract
Targeted intracellular delivery via receptor-mediated endocytosis requires the delivered cargo to escape the endosome to prevent lysosomal degradation. This can in principle be achieved by membrane lysis tightly restricted to endosomal membranes upon internalization to avoid general membrane insertion and lysis. Here, we describe the design of small monomeric proteins with buried histidine containing pH-responsive hydrogen bond networks and membrane permeating amphipathic helices. Of the 30 designs that were experimentally tested, all expressed in Escherichia coli, 13 were monomeric with the expected secondary structure, and 4 designs disrupted artificial liposomes in a pH-dependent manner. Mutational analysis showed that the buried histidine hydrogen bond networks mediate pH-responsiveness and control lysis of model membranes within a very narrow range of pH (6.0-5.5) with almost no lysis occurring at neutral pH. These tightly controlled lytic monomers could help mediate endosomal escape in designed targeted delivery platforms.
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Registered trials
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