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Bacteriophage PRD1 as a nanoscaffold for drug loading
Helen M E Duyvesteyn1,2, Isaac Santos-Pérez3, Francesca Peccati4
1Division of Structural Biology, University of Oxford, The Henry Wellcome Building for Genomic Medicine, Headington, Oxford, UK. dave.stuart@strubi.ox.ac.uk.
Nanoscale
|December 1, 2021
Summary
Researchers used cryo-electron microscopy to study the PRD1 virus. They discovered its protein shell can bind to the drug chlorpromazine (CPZ), showing potential for virus-based drug delivery.
Area of Science:
- Structural biology
- Virology
- Biomaterials science
Background:
- Viruses are attractive nanocarriers for genetic material.
- Viral protein capsids can be functionalized for selective payload uptake.
- PRD1 is a double-stranded DNA bacteriophage with an icosahedral capsid and lipid vesicle.
Purpose of the Study:
- To determine the 3D structure of PRD1 in complex with chlorpromazine (CPZ).
- To investigate the potential of viral capsomers for loading heterocyclic drugs.
Main Methods:
- Cryo-electron microscopy for structural determination.
- X-ray studies for binding analysis.
- Molecular dynamics simulations for molecular interactions.
Main Results:
- The 3D structure of PRD1 complexed with CPZ was elucidated.
- Viral major capsid protein P3 jellyrolls act as scaffolds for CPZ loading.
- CPZ molecules bind to P3 and the virion surface, with defined organization.
Conclusions:
- Virus capsomers can be utilized for loading heterocyclic drugs.
- The lattice-like organization and quasi-symmetric morphology of virus capsomers are key features.
- This study provides a proof of concept for virus-based drug delivery systems.
