<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Assadipapari M</submitter><funding>Wolfson Foundation</funding><funding>UK-India Education and Research Initiative</funding><funding>Scheme for Promotion of Academic and Research Collaboration</funding><funding>Royal Society</funding><funding>Biotechnology and Biological Sciences Research Council</funding><funding>Academy of Medical Sciences</funding><funding>HORIZON EUROPE Marie Sklodowska-Curie Actions</funding><pagination>1045-1054</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC12706752</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>18(2)</volume><pubmed_abstract>Ferritin is a multimeric protein that stores and releases iron, emerging as a promising candidate for nanomedicine, particularly in targeted drug delivery. Its ability to disassemble and reassemble under specific environments is crucial for encapsulating and releasing therapeutic payloads. In this work, we monitor ferritin reassembly and disassembly in real time at the single-molecule level using polymer-coated solid-state nanopores. The coating enabled continuous ion current recording of ferritin fragment translocations for up to 1 hour without clogging, overcoming a major challenge of uncoated nanopores. This long-term recording allowed us to track the full reassembly and disassembly processes. We show that while traditional population-based analysis can identify the presence of fragment</pubmed_abstract><journal>Nanoscale</journal><pubmed_title>Tracking single-molecule ferritin reassembly and disassembly using polymer-coated nanopores.</pubmed_title><pmcid>PMC12706752</pmcid><funding_grant_id>BB/T0083690/1</funding_grant_id><funding_grant_id>Springboard Award (SBF0010\1008)</funding_grant_id><funding_grant_id>I4WORLD</funding_grant_id><funding_grant_id>BB/T000627/1</funding_grant_id><pubmed_authors>Xu L</pubmed_authors><pubmed_authors>Li J</pubmed_authors><pubmed_authors>Adam M</pubmed_authors><pubmed_authors>Rahmani M</pubmed_authors><pubmed_authors>Assadipapari M</pubmed_authors><pubmed_authors>Clark AW</pubmed_authors><pubmed_authors>Kara H</pubmed_authors><pubmed_authors>Hudson AJ</pubmed_authors><pubmed_authors>Santana Vega M</pubmed_authors><pubmed_authors>Ying C</pubmed_authors><pubmed_authors>Yousefi A</pubmed_authors><pubmed_authors>Huang JA</pubmed_authors><pubmed_authors>Zargarbashi S</pubmed_authors><pubmed_authors>Soleimanian A</pubmed_authors><pubmed_authors>Wills MFK</pubmed_authors></additional><is_claimable>false</is_claimable><name>Tracking single-molecule ferritin reassembly and disassembly using polymer-coated nanopores.</name><description>Ferritin is a multimeric protein that stores and releases iron, emerging as a promising candidate for nanomedicine, particularly in targeted drug delivery. Its ability to disassemble and reassemble under specific environments is crucial for encapsulating and releasing therapeutic payloads. In this work, we monitor ferritin reassembly and disassembly in real time at the single-molecule level using polymer-coated solid-state nanopores. The coating enabled continuous ion current recording of ferritin fragment translocations for up to 1 hour without clogging, overcoming a major challenge of uncoated nanopores. This long-term recording allowed us to track the full reassembly and disassembly processes. We show that while traditional population-based analysis can identify the presence of fragment</description><dates><release>2026-01-01T00:00:00Z</release><publication>2026 Jan</publication><modification>2026-07-15T06:39:13.701Z</modification><creation>2026-06-30T03:20:17.272Z</creation></dates><accession>S-EPMC12706752</accession><cross_references><pubmed>41399872</pubmed><doi>10.1039/d5nr02885j</doi></cross_references></HashMap>