Issue 48, 2018

The equilibrium structure of self-assembled protein nano-cages

Abstract

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.

Graphical abstract: The equilibrium structure of self-assembled protein nano-cages

Supplementary files

Article information

Article type
Paper
Submitted
04 sen 2018
Accepted
05 noy 2018
First published
05 dek 2018

Nanoscale, 2018,10, 22802-22809

Author version available

The equilibrium structure of self-assembled protein nano-cages

S. Panahandeh, S. Li and R. Zandi, Nanoscale, 2018, 10, 22802 DOI: 10.1039/C8NR07202G

To request permission to reproduce material from this article, please go to the Copyright Clearance Center request page.

If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.

If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.

Read more about how to correctly acknowledge RSC content.

Social activity

Spotlight

Advertisements