The equilibrium structure of self-assembled protein nano-cages

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 struct...

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Bibliographic Details
Published in:Nanoscale 2018-12, Vol.1 (48), p.2282-2289
Main Authors: Panahandeh, Sanaz, Li, Siyu, Zandi, Roya
Format: Article
Language:English
Subjects:
Cages
Computer simulation
Curvature
Drug delivery systems
Gene therapy
Medical imaging
Monte Carlo simulation
Nanotechnology
Physical properties
Polymorphism
Proteins
Selectivity
Self-assembly
Symmetry
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Summary: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. Global minimum energy structures of protein nano-cages are investigated as a function of the mechanical properties of coat proteins.
ISSN:2040-3364
2040-3372
DOI:10.1039/c8nr07202g