Self-Assembly in the Ferritin Nano-Cage Protein Superfamily
2011
Self-Assembly in the Ferritin Nano-Cage Protein Superfamily
publication
10 minutes
Evidence: moderate
Author Information
Author(s): Zhang Yu, Brendan P. Orner
Primary Institution: Nanyang Technological University
Hypothesis
Understanding the principles of protein self-assembly can enhance their applications in nanomaterials.
Conclusion
Ferritin proteins self-assemble into multi-subunit, hollow, nano-scale cages, which have potential applications in drug delivery and nanostructured materials.
Supporting Evidence
- Ferritins are found in both prokaryotes and eukaryotes.
- Maxi-ferritins form hollow spheres with octahedral symmetry composed of twenty-four monomers.
- Mini-ferritins are tetrahedrally symmetric, hollow assemblies composed of twelve monomers.
- Understanding ferritin self-assembly can lead to novel applications in nanotechnology.
Takeaway
Ferritin proteins can stick together to form tiny cages that can hold iron, which is important for many biological processes.
Methodology
This review summarizes structural studies and mechanisms of self-assembly of ferritin proteins.
Limitations
The review does not provide experimental data but rather discusses existing literature.
Digital Object Identifier (DOI)
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