title: Detergent-Free Membrane Protein Purification.
abstract: Membrane proteins are localized within a lipid bilayer; in order to purify them for functional and structural studies the first step must involve solubilizing or extracting the protein from these lipids. To date this has been achieved using detergents which disrupt the bilayer and bind to the protein in the transmembrane region. However finding conditions for optimal extraction, without destabilizing protein structure, is time consuming and expensive. Here we present a recently-developed method using a styrene-maleic acid (SMA) co-polymer instead of detergents. The SMA co-polymer extracts membrane proteins in a small disc of lipid bilayer which can be used for affinity chromatography purification, thus enabling the purification of membrane proteins while maintaining their native lipid bilayer environment.
authors.affiliation: Life & Health Sciences, Aston University, Birmingham, B4 7ET, UK. A.ROTHNIE@aston.ac.uk.
authors.forename: Alice J
authors.initials: AJ
authors.lastname: Rothnie
mesh_terms: D002846:Chromatography, Affinity; D008051:Lipid Bilayers / Q000032:analysis; D008298:Maleates / Q000737:chemistry*; D008565:Membrane Proteins / Q000737:chemistry / Q000302:isolation & purification*; D011137:Polystyrenes / Q000737:chemistry*
chemical_list: D008051:Lipid Bilayers; D008298:Maleates; D008565:Membrane Proteins; D011137:Polystyrenes; C024074:styrene-maleic acid polymer
keywords: Detergent; Membrane proteins; Nanodisc; Polymer; Purification; SMALP; Solubilization