ArticleDose-response : a publication of International Hormesis Society
Salt-Dependent Aggregation and Assembly of E coli-Expressed Ferritin.
Article in Dose-response : a publication of International Hormesis Society. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Ferritin Vaccine Platform for Animal and Zoonotic Viruses.Vaccines · 2024Review
- Protein-based antigen presentation platforms for nanoparticle vaccines.NPJ vaccines · 2021Review
- Soluble expression, purification, and secondary structure determination of human MESP1 transcription factor.Applied microbiology and biotechnology · 2021Article
- Chaperna-Mediated Assembly of Ferritin-Based Middle East Respiratory Syndrome-Coronavirus Nanoparticles.Frontiers in immunology · 2018Article
- Thermostable exoshells fold and stabilize recombinant proteins.Nature communications · 2017Article
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Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ferritin, with the primary function of iron storage, is a nearly ubiquitous protein found in most living organisms. Our recent investigations suggest that ferritin can assemble nanoparticles. So we use ferritin as a novel type of delivery vehicle for recombinant epitope vaccines. And, we found that ferritin form nonnative aggregates depended sensitively on NaCl concentrations. Here, we report that ferritin is an ion-sensitive protein and has the attribute of salt-dependent aggregation. Our results indicate that recombinant ferritin can be released as a soluble form from Escherichia coli at low NaCl concentrations (≤50 mmol/L). Moreover, this result affords us to confirm a proper self-assembling solution for soluble ferritin or other ferritin-based fusion proteins to assemble nanoparticles.
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Registered trials
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