| Issue |
EPL
Volume 117, Number 5, March 2017
|
|
|---|---|---|
| Article Number | 58001 | |
| Number of page(s) | 7 | |
| Section | Interdisciplinary Physics and Related Areas of Science and Technology | |
| DOI | https://doi.org/10.1209/0295-5075/117/58001 | |
| Published online | 24 April 2017 | |
Controlling the shape of membrane protein polyhedra
Department of Physics & Astronomy and Molecular and Computational Biology Program, Department of Biological Sciences, University of Southern California - Los Angeles, CA 90089, USA
Received: 6 February 2017
Accepted: 6 April 2017
Membrane proteins and lipids can self-assemble into membrane protein polyhedral nanoparticles (MPPNs). MPPNs have a closed spherical surface and a polyhedral protein arrangement, and may offer a new route for structure determination of membrane proteins and targeted drug delivery. We develop here a general analytic model of how MPPN self-assembly depends on bilayer-protein interactions and lipid bilayer mechanical properties. We find that the bilayer-protein hydrophobic thickness mismatch is a key molecular control parameter for MPPN shape that can be used to bias MPPN self-assembly towards highly symmetric and uniform MPPN shapes. Our results suggest strategies for optimizing MPPN shape for structural studies of membrane proteins and targeted drug delivery.
PACS: 87.16.D- – Membranes, bilayers, and vesicles / 87.14.ep – Membrane proteins / 87.15.kt – Protein-membrane interactions
© EPLA, 2017
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