ArticleNature communications2017
Efficient protein production inspired by how spiders make silk.
Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers.
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Who cites it
61 citing papers in PubMed, 130 citations in OpenAlex.
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- Cis-Acting Chaperoning by Macromolecular Tethering: A Built-In Layer of Cellular Chaperoning.International journal of molecular sciences · 2026Review
- Ganglioside GM1 slows down Aβ(1-42) aggregation by a primary nucleation inhibitory mechanism that is modulated by sphingomyelin and cholesterol.Communications chemistry · 2025Article
- Chaperone-Mediated Regulation of Tau Phase Separation, Fibrillation, and Toxicity.Journal of the American Chemical Society · 2025Article
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- Native Mass Spectrometry Captures the Conformational Plasticity of Proteins with Low-Complexity Domains.JACS Au · 2025Article
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- Beyond Misfolding: A New Paradigm for the Relationship Between Protein Folding and Aggregation.International journal of molecular sciences · 2024Review
- What is new in synthetic lung surfactant protein technology?Expert review of respiratory medicine · 2024Article
- Liquid-liquid crystalline phase separation of spider silk proteins.Communications chemistry · 2024Review
- Design of amyloidogenic peptide traps.Nature chemical biology · 2024Article
- Controlling Drug Partitioning in Individual Protein Condensates through Laser-Induced Microscale Phase Transitions.Journal of the American Chemical Society · 2024Article
- Molecular basis for different substrate-binding sites and chaperone functions of the BRICHOS domain.Protein science : a publication of the Protein Society · 2024Article
- Efficient Biosynthetic Fabrication of Spidroins with High Spinning Performance.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Identification of potential aggregation hotspots on Aβ42 fibrils blocked by the anti-amyloid chaperone-like BRICHOS domain.Nature communications · 2024Article
- Murine Norovirus: Additional Protocols for Basic and Antiviral Studies.Current protocols · 2023Article
- Mass Spectrometry of RNA-Binding Proteins during Liquid-Liquid Phase Separation Reveals Distinct Assembly Mechanisms and Droplet Architectures.Journal of the American Chemical Society · 2023Article
1 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
20 authors at 7 institutions in 5 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Membrane proteins are targets of most available pharmaceuticals, but they are difficult to produce recombinantly, like many other aggregation-prone proteins. Spiders can produce silk proteins at huge concentrations by sequestering their aggregation-prone regions in micellar structures, where the very soluble N-terminal domain (NT) forms the shell. We hypothesize that fusion to NT could similarly solubilize non-spidroin proteins, and design a charge-reversed mutant (NT*) that is pH insensitive, stabilized and hypersoluble compared to wild-type NT. NT*-transmembrane protein fusions yield up to eight times more of soluble protein in Escherichia coli than fusions with several conventional tags. NT* enables transmembrane peptide purification to homogeneity without chromatography and manufacture of low-cost synthetic lung surfactant that works in an animal model of respiratory disease. NT* also allows efficient expression and purification of non-transmembrane proteins, which are otherwise refractory to recombinant production, and offers a new tool for reluctant proteins in general.
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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.