Journal
NANOSCALE
Volume 10, Issue 48, Pages 22802-22809Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/c8nr07202g
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Funding
- National Science Foundation [DMR-1719550]
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Understanding how highly symmetric, robust, monodisperse protein nano-cages self-assemble can have major applications in various areas of bio-nanotechnology, such as drug delivery, biomedical imaging and gene therapy. We develop a model to investigate the assembly of protein subunits into the structures with different sizes and symmetries. Using Monte Carlo simulation, we obtain global minimum energy structures. Our results suggest that the physical properties including the spontaneous curvature, flexibility and bending rigidity of coat proteins are sufficient to predict the size, symmetry and shape selectivity of the assembly products. Further, on a thermodynamic basis, we discuss the polymorphism of nano-cages observed in assembly experiments.
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