ArticleACS nano2024
Structural Flexibility and Disassembly Kinetics of Single Ferritin Molecules Using Optical Nanotweezers.
Article in ACS nano, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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11 citing papers in PubMed.
- Plasmonic Optical Tweezers and Surface-Enhanced Raman Spectroscopy: Fundamentals, Single-Entity Applications, and the Evolving Role of Artificial Intelligence.Bioengineering (Basel, Switzerland) · 2026Review
- Structural flexibility of the human vault particle revealed by high-resolution cryo-EM and molecular dynamics simulations.Nature communications · 2026Article
- Geometric Confinement in Solid-State Nanopores Enables Single-Molecule Discrimination of Ferritin Subunits and Translocation Bias.Nano letters · 2026Article
- Tracking single-molecule ferritin reassembly and disassembly using polymer-coated nanopores.Nanoscale · 2026Article
- Label-Free Single-Molecule Conalbumin Analysis.Micromachines · 2026Article
- Label-free optical observation of disordered-to-ordered transitions in single intrinsically disordered proteins.Npj biosensing · 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
- Native globular ferritin nanopore sensor.Nature communications · 2025Article
- Unveiling the stochastic nature of human heteropolymer ferritin self-assembly mechanism.Protein science : a publication of the Protein Society · 2024Article
- Energy landscape of conformational changes for a single unmodified protein.Npj biosensing · 2024Article
- Challenges in Exploiting Human H Ferritin Nanoparticles for Drug Delivery: Navigating Physiological Constraints.Wiley interdisciplinary reviews. Nanomedicine and nanobiotechnologyReview
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Authors and funding
13 authors.
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Abstract
Ferritin, a spherical protein shell assembled from 24 subunits, functions as an efficient iron storage and release system through its channels. Understanding how various chemicals affect the structural behavior of ferritin is crucial for unravelling the origins of iron-related diseases in living organisms including humans. In particular, the influence of chemicals on ferritin's dynamics and iron release is barely explored at the single-protein level. Here, by employing optical nanotweezers using double-nanohole (DNH) structures, we examined the effect of ascorbic acid (reducing reagent) and pH on individual ferritin's conformational dynamics. The dynamics of ferritin increased as the concentration of ascorbic acid approached saturation. At pH 2.0, ferritin exhibited significant structural fluctuations and eventually underwent a stepwise disassembly into fragments. This work demonstrated the disassembly pathway and kinetics of a single ferritin molecule in solution. We identified four critical fragments during its disassembly pathway, which are 22-mer, 12-mer, tetramer, and dimer subunits. Moreover, we present single-molecule evidence of the cooperative disassembly of ferritin. Interrogating ferritin's structural change in response to different chemicals holds importance for understanding their roles in iron metabolism, hence facilitating further development of medical treatments for its associated diseases.
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