ArticleBiochemistry2017
Thermophilic Ferritin 24mer Assembly and Nanoparticle Encapsulation Modulated by Interdimer Electrostatic Repulsion.
Article in Biochemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 37 citations in OpenAlex.
- Peptide-Ligand Cooperative Interplay Drives Gold Nanoparticle Encapsulation by Protein Cages.Small (Weinheim an der Bergstrasse, Germany) · 2026Article
- Cavity acidification limits ferritin iron biomineralization.Journal of inorganic biochemistry · 2026Article
- Molecular Mechanisms and Biomedical Applications of Ferritin Nanocages: A Comprehensive Review of Self-Assembly, Engineering, and Multifunctional Delivery Platforms.International journal of nanomedicine · 2026Review
- Charge engineering controls cooperative assembly and loading in protein host-guest complexes.Journal of materials chemistry. B · 2025Article
- Unveiling the stochastic nature of human heteropolymer ferritin self-assembly mechanism.Protein science : a publication of the Protein Society · 2024Article
- Functional Characterization of Salmonella Typhimurium Encoded YciF, a Domain of Unknown Function (DUF892) Family Protein, and Its Role in Protection during Bile and Oxidative Stress.Journal of bacteriology · 2023Article
- Hyperthermostable recombinant human heteropolymer ferritin derived from a novel plasmid design.Protein science : a publication of the Protein Society · 2023Article
- Structural and Functional Insights into the Roles of Potential Metal-Binding Sites inPolymers · 2022Article
- Article
- Computational Design of Single-Peptide Nanocages with Nanoparticle Templating.Molecules (Basel, Switzerland) · 2022Article
- A Ferritin-Albumin-Cu Nanoparticle that Efficaciously Delivers Copper(II) Ions to a Tumor and Improves the Therapeutic Efficacy of Disulfiram.ACS omega · 2020Article
- Review
- Infinite Assembly of Folded Proteins in Evolution, Disease, and Engineering.Angewandte Chemie (International ed. in English) · 2019Review
- Disulfide-mediated conversion of 8-mer bowl-like protein architecture into three different nanocages.Nature communications · 2019Article
- Spatially controlled assembly of affinity ligand and enzyme cargo enables targeting ferritin nanocarriers to caveolae.Biomaterials · 2018Article
- A protein-protein host-guest complex: Thermostable ferritin encapsulating positively supercharged green fluorescent protein.Protein science : a publication of the Protein Society · 2018Article
- Ferritin-based drug delivery systems: Hybrid nanocarriers for vascular immunotargeting.Journal of controlled release : official journal of the Controlled Release Society · 2018Review
- Ferritin Nanocages with Biologically Orthogonal Conjugation for Vascular Targeting and Imaging.Bioconjugate chemistry · 2018Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
Protein cage self-assembly enables encapsulation and sequestration of small molecules, macromolecules, and nanomaterials for many applications in bionanotechnology. Notably, wild-type thermophilic ferritin from Archaeoglobus fulgidus (AfFtn) exists as a stable dimer of four-helix bundle proteins at a low ionic strength, and the protein forms a hollow assembly of 24 protomers at a high ionic strength (∼800 mM NaCl). This assembly process can also be initiated by highly charged gold nanoparticles (AuNPs) in solution, leading to encapsulation. These data suggest that salt solutions or charged AuNPs can shield unfavorable electrostatic interactions at AfFtn dimer-dimer interfaces, but specific "hot-spot" residues controlling assembly have not been identified. To investigate this further, we computationally designed three AfFtn mutants (E65R, D138K, and A127R) that introduce a single positive charge at sites along the dimer-dimer interface. These proteins exhibited different assembly kinetics and thermodynamics, which were ranked in order of increasing 24mer propensity: A127R < wild type < D138K ≪ E65R. E65R assembled into the 24mer across a wide range of ionic strengths (0-800 mM NaCl), and the dissociation temperature for the 24mer was 98 °C. X-ray crystal structure analysis of the E65R mutant identified a more compact, closed-pore cage geometry. A127R and D138K mutants exhibited wild-type ability to encapsulate and stabilize 5 nm AuNPs, whereas E65R did not encapsulate AuNPs at the same high yields. This work illustrates designed protein cages with distinct assembly and encapsulation properties.
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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.