Ferritin serves as the main iron-storage protein in the body. It forms a well-defined cage-like 24mer structure under physiological pH and can self-assemble and disassemble based on pH. Thermophilic ferritin from the archaeon <i>Archaeoglobus Fulgidus</i> (AfFtn) has a unique feature of salt-dependent self-assembly, which provides even greater flexibility for cargo encapsulation compared to other ferritins. Due to its unique architecture, thermal stability and self-assembly properties, we and other labs have modified the protein surface and re-engineered ferritin for the purpose of targeted delivery of therapeutic cargo. In the process of purifying AfFtn from overexpression in <i>E. coli</i>, we found that native oligonucleotides co-purify with AfFtn and are encapsulated under high-salt buffer conditions. This discovery has led to efforts to load exogenous oligos into AfFtn. These studies build on our ongoing research in ferritin-mediated cellular delivery of protein and nanoparticle cargo, for example, in targeting ferritin to in vivo sites of inflammation.

Ferritin nanocage based oligo encapsulation and delivery

Macromolecular Chemistry: The Second Century

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ACS Spring 2020 National Meeting & Expo

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.