# Controlling the shape of membrane protein polyhedra

## TL;DR

This paper presents an analytic model explaining how membrane protein polyhedral nanoparticles (MPPNs) self-assemble, highlighting the role of bilayer-protein interactions in controlling their shape for potential applications in structural biology and drug delivery.

## Contribution

The authors develop a general analytic model linking bilayer-protein interactions to MPPN shape control, enabling targeted design of symmetric and uniform nanoparticles.

## Key findings

- Hydrophobic thickness mismatch is a key control parameter.
- Adjusting bilayer properties biases MPPN shape.
- Strategies for optimizing MPPN shape are proposed.

## Abstract

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.