ArticleNature communications2017
Thermostable exoshells fold and stabilize recombinant proteins.
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 13 papers.
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Who cites it
13 citing papers in PubMed.
- Review
- Bioorthogonal catalytic centres engineered for gastrointestinal stabilization provide oral delivery for the treatment of gastric cancer.Journal of nanobiotechnology · 2026Article
- Construction of primary chassis cells with efficient protein expression in Thermus thermophilus.Microbial cell factories · 2025Article
- High-Performance Molecular Dynamics Simulations for Native Mass Spectrometry of Large Protein Complexes with the Fast Multipole Method.Analytical chemistry · 2024Article
- Potential Application of Self-Assembled Peptides and Proteins in Breast Cancer and Cervical Cancer.International journal of molecular sciences · 2023Review
- Nanovaccines: Merits, and diverse roles in boosting antitumor immune responses.Human vaccines & immunotherapeutics · 2022Review
- Gastrointestinal Tract Stabilized Protein Delivery Using Disulfide Thermostable Exoshell System.International journal of molecular sciences · 2022Article
- Harnessing physicochemical properties of virus capsids for designing enzyme confined nanocompartments.Current opinion in virology · 2022Review
- Nanoencapsulation as a General Solution for Lyophilization of Labile Substrates.Pharmaceutics · 2021Article
- Genetically Encodable Scaffolds for Optimizing Enzyme Function.Molecules (Basel, Switzerland) · 2021Review
- Enzyme encapsulation by protein cages.RSC advances · 2020Review
- Improvement of the catalytic activity and thermostability of a hyperthermostable endoglucanase by optimizing N-glycosylation sites.Biotechnology for biofuels · 2020Article
- A protein-protein host-guest complex: Thermostable ferritin encapsulating positively supercharged green fluorescent protein.Protein science : a publication of the Protein Society · 2018Article
Corrections and comments
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The expression and stabilization of recombinant proteins is fundamental to basic and applied biology. Here we have engineered a thermostable protein nanoparticle (tES) to improve both expression and stabilization of recombinant proteins using this technology. tES provides steric accommodation and charge complementation to green fluorescent protein (GFPuv), horseradish peroxidase (HRPc), and Renilla luciferase (rLuc), improving the yields of functional in vitro folding by ~100-fold. Encapsulated enzymes retain the ability to metabolize small-molecule substrates, presumably via four 4.5-nm pores present in the tES shell. GFPuv exhibits no spectral shifts in fluorescence compared to a nonencapsulated control. Thermolabile proteins internalized by tES are resistant to thermal, organic, chaotropic, and proteolytic denaturation and can be released from the tES assembly with mild pH titration followed by proteolysis.
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