ArticleScientific reports2019
pH-depended protein shell dis- and reassembly of ferritin nanoparticles revealed by atomic force microscopy.
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
What it found
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The trial behind it
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Who cites it
20 citing papers in PubMed, 38 citations in OpenAlex.
- Direct measurement of protein dipoles reveals the mechanism for like-charge adsorption on silica.Nature communications · 2026Article
- Albumin-based nanocarriers: Singularities, synthesis methods, clinical relevance and targeting strategies in cancer.Acta pharmaceutica Sinica. B · 2026Review
- Direct evidence of acid-driven protein desolvation.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Bioorthogonal catalytic centres engineered for gastrointestinal stabilization provide oral delivery for the treatment of gastric cancer.Journal of nanobiotechnology · 2026Article
- Tracking single-molecule ferritin reassembly and disassembly using polymer-coated nanopores.Nanoscale · 2026Article
- Physicochemical Changes of Apoferritin Protein during Biodegradation of Magnetic Metal Oxide Nanoparticles.ACS applied materials & interfaces · 2024Article
- Review
- Self-assembling ferritin nanoplatform for the development of infectious hematopoietic necrosis virus vaccine.Frontiers in immunology · 2024Article
- Translational Challenges and Prospective Solutions in the Implementation of Biomimetic Delivery Systems.Pharmaceutics · 2023Review
- Self-Assembly of Polymer-Modified FePt Magnetic Nanoparticles and Block Copolymers.Materials (Basel, Switzerland) · 2023Article
- Digestibility of Protein and Iron Availability from Enriched Legume Sprouts.Plant foods for human nutrition (Dordrecht, Netherlands) · 2023Article
- In Vitro Immunoreactivity Evaluation of H-Ferritin-Based Nanodrugs.Bioconjugate chemistry · 2023Article
- Ferritin in cancer therapy: A pleiotropic tumoraffin nanocage-based transport.Cancer medicine · 2023Review
- Hybridization of papain molecules and DNA-wrapped single-walled carbon nanotubes evaluated by atomic force microscopy in fluids.Scientific reports · 2023Article
- Manufacturing of non-viral protein nanocages for biotechnological and biomedical applications.Frontiers in bioengineering and biotechnology · 2023Review
- Characterizing the Dynamic Disassembly/Reassembly Mechanisms of Encapsulin Protein Nanocages.ACS omega · 2022Article
- Modulating cell signalling in vivo with magnetic nanotransducers.Nature reviews. Methods primers · 2022Article
- Integrin αJournal of nanobiotechnology · 2021Article
- Passive Diffusion vs Active pH-Dependent Encapsulation of Tyrosine Kinase Inhibitors Vandetanib and Lenvatinib into Folate-Targeted Ferritin Delivery System.International journal of nanomedicine · 2021Article
- Crosstalk between noncoding RNAs and ferroptosis: new dawn for overcoming cancer progression.Cell death & disease · 2020Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ferritin, a protein that is present in the human body for a controlled iron storage and release, consists of a ferrihydrite core and a protein shell. Apoferritin, the empty shell of ferritin, can be modified to carry tailored properties exploitable for targeted and direct drug delivery. This protein shell has the ability to dis- and reassemble depending on the pH value of the liquid environment and can thus be filled with the desired substance. Here we observed the dis- and reassembly process of the protein shell of ferritin and apoferritin in situ and in real space using atomic force microscopy. Ferritin and apoferritin nanoparticles adsorbed on a mica substrate exhibited a change in their size by varying the pH value of the surrounding medium. Lowering the pH value of the solution led to a decrease in size of the nanoparticles whereas a successive increase of the pH value increased the particle size again. The pH dependent change in size could be related to the dis- and reassembling of the protein shell of ferritin and apoferritin. Supplementary imaging by bimodal magnetic force microscopy of ferritin molecules accomplished in air revealed a polygonal shape of the core and a three-fold symmetry of the protein shell providing valuable information about the substructure of the nanoparticles.
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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.