Controlling the shape of membrane protein polyhedra

• Published in: Europhysics letters Vol. 117; no. 5; pp. 58001 - 58007
• Main Authors: Li, Di, Kahraman, Osman, Haselwandter, Christoph A.
• Format: Journal Article
• Language: English
• Published: Les Ulis EDP Sciences, IOP Publishing and Società Italiana di Fisica 01-03-2017; IOP Publishing
• Subjects: 87.14.ep; 87.15.kt; 87.16.D; Lipids; Mechanical properties; Membranes; Molecular structure; Polyhedra; Proteins; Self-assembly; Shape optimization; Thickness
• ISSN: 0295-5075; 1286-4854
• DOI: 10.1209/0295-5075/117/58001

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.