The lipid nanodisk morphology is an increasingly attractive platform for spectroscopic characterization of membrane proteins, and has seen use in obtaining pure protein for X-ray crystallography, as well as NMR characterization. Lipid disks can be formed using various copolymer formulations such as peptides, or here, a copolymer of styrene and maleic acid (SMA). Due to the cost of the commercially available material, there has been interest in synthesizing materials of equal quality. Our approach has been to use Reversible Addition Fragmentation chain Transfer (RAFT), a method of controlled radical polymerization that generates polymers with a narrow size distribution. Recently, we extensively characterized the structure of lipid nanodisks made from RAFT-synthesized polymers, as well as the structure and dynamics of membrane proteins suspended therein. DLS and TEM analysis reveal comparable quality to nanodisks formed using commercial material. Analysis of line shape in CW-EPR reveals that the spin label incorporated into the transmembrane domain of a model peptide becomes more rigid after the vesicle-to-disk transition.

Characterizing the structure and dynamics of styrene-maleic acid copolymer-lipid nanoparticles (SMALPS) as a membrane mimetic

2019 Spring National Meeting

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