Researchers capture atomic-level view of mi3 virus-like particle self-assembly
Scientists purified and structurally analyzed SC003-mi3, an engineered virus-like particle derived from i3-01 with cysteine mutations and a SpyCatcher domain for attaching other proteins. Using E. coli expression, ammonium sulfate precipitation and dialysis, they produced pure particles suitable for detailed molecular observation of how the nanoparticle assembles itself.
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Understanding exactly how these engineered protein shells self-assemble at the molecular level helps researchers design more reliable vaccine platforms and drug-delivery nanoparticles, since VLPs like mi3 are already used as scaffolds for displaying antigens or therapeutic proteins. Better assembly knowledge could improve yield, stability and reproducibility of these particles in biotech and pharmaceutical applications.
- mi3-VLP is an engineered nanoparticle based on i3-01 with mutations for stability and a SpyCatcher tag for attaching cargo proteins
- The particles were produced in E. coli and purified via ammonium sulfate precipitation, filtration and dialysis
- This purification enabled molecular-level study of how the virus-like particle self-assembles, aiding future vaccine and delivery platform design
Source: nature.com — Asor, 2026-09-16
Published there as: “Molecular-level observation of the self-assembly of a virus-like particle”
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