MAASTY: A (dis)ordered copolymer for structural determination of human membrane proteins in native nanodiscs

Author:

Pugh Ciara FrancesORCID,Præstegaard Kaia Fiil,Feilen Lukas PeterORCID,Živković DušanORCID,Borthwick Neil JeanORCID,de Lichtenberg CasperORCID,Bolla Jani R.,Autzen Anton Allen AbbotsfordORCID,Autzen Henriette ElisabethORCID

Abstract

AbstractAmphiphilic copolymers capable of extracting membrane proteins directly from lipid bilayers into ”native nanodiscs” offer a simplified approach for preparing membrane proteins in lipid nanodiscs compared to approaches that rely on detergent. Amphiphilicity, length, and composition influence the performance of copolymers, in addition to the protein itself and the purification conditions used. Here, we report a copolymer composed of methacrylic acid and styrene, which we term MAASTY, leveraging the inherent monomer reactivity ratios to create an anionic copolymer with a statistical distribution of monomers. We show that MAASTY can be used for high-resolution structural determination of a human membrane protein with single particle cryo-electron microscopy, preserving endogenous lipids. Moreover, MAASTY copolymers effectively solubilize a broad range of lipid species and a wide range of different, eukaryotic membrane proteins from mammalian cells. We find that MAASTY copolymers are promising as effective solubilizers of membrane proteins and offer a new chemical platform for structural and functional characterization of membrane proteins in native nanodiscs.

Publisher

Cold Spring Harbor Laboratory

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