ArticleProtein science : a publication of the Protein Society2023
Hyperthermostable recombinant human heteropolymer ferritin derived from a novel plasmid design.
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 9 papers.
What it found
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Who cites it
9 citing papers in PubMed, 10 citations in OpenAlex.
- Review
- Application and Research Progress of Self-Assembling Protein Nanoparticles in Vaccine Development.International journal of molecular sciences · 2026Review
- Molecular Mechanisms and Biomedical Applications of Ferritin Nanocages: A Comprehensive Review of Self-Assembly, Engineering, and Multifunctional Delivery Platforms.International journal of nanomedicine · 2026Review
- The Role of Confinement in Biomineralization.Chemical reviews · 2025Review
- Ultrasound-Assisted Ferritin Extraction from Northern Pike Liver: An Innovative Approach for Chlorogenic Acid Encapsulation with Enhanced Thermal Stability.Molecules (Basel, Switzerland) · 2025Article
- Unveiling the stochastic nature of human heteropolymer ferritin self-assembly mechanism.Protein science : a publication of the Protein Society · 2024Article
- Ferritin microheterogeneity, subunit composition, functional, and physiological implications.Scientific reports · 2023Article
- Ferritin nanocages as efficient nanocarriers and promising platforms for COVID-19 and other vaccines development.Biochimica et biophysica acta. General subjects · 2023Review
- Hyperthermostable recombinant human heteropolymer ferritin derived from a novel plasmid design.Protein science : a publication of the Protein Society · 2023Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
Mammalian ferritins are predominantly heteropolymeric species consisting of 2 structurally similar, but functionally and genetically distinct subunit types, called H (Heavy) and L (Light). The two subunits co-assemble in different H and L ratios to form 24-mer shell-like protein nanocages where thousands of iron atoms can be mineralized inside a hollow cavity. Here, we use differential scanning calorimetry (DSC) to study ferritin stability and understand how various combinations of H and L subunits confer aspects of protein structure-function relationships. Using a recently engineered plasmid design that enables the synthesis of complex ferritin nanostructures with specific H to L subunit ratios, we show that homopolymer L and heteropolymer L-rich ferritins have a remarkable hyperthermostability (Tm = 115 ± 1°C) compared to their H-ferritin homologues (Tm = 93 ± 1°C). Our data reveal a significant linear correlation between protein thermal stability and the number of L subunits present on the ferritin shell. A strong and unexpected iron-induced protein thermal destabilization effect (ΔT
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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.