Controlling the shape of membrane protein polyhedra. (24th April 2017)

• Record Type: Journal Article
• Authors: Li, Di; Kahraman, Osman; Haselwandter, Christoph A.
• Is Part Of: Europhysics letters. Volume 117:Number 5(2017:Mar.)
• Publication Date: 2017-04-24
• Subjects: 87.16.D- -- 87.14.ep -- 87.15.kt; Physics -- Periodicals; Electronic journals; 530.05
• DOI: 10.1209/0295-5075/117/58001
• Languages: English
• ISSNs: 0295-5075

Abstract

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.