Abstract
Amphiphilic copolymers consisting of alternating hydrophilic and hydrophobic units account for a major recent methodical breakthrough in the investigations of membrane proteins. Styrene–maleic acid (SMA), diisobutylene–maleic acid (DIBMA), and related copolymers have been shown to extract membrane proteins directly from lipid membranes without the need for classical detergents. Within the particular experimental setup, they form disc-shaped nanoparticles with a narrow size distribution, which serve as a suitable platform for diverse kinds of spectroscopy and other biophysical techniques that require relatively small, homogeneous, water-soluble particles of separate membrane proteins in their native lipid environment. In recent years, copolymer-encased nanolipoparticles have been proven as suitable protein carriers for various structural biology applications, including cryo-electron microscopy (cryo-EM), small-angle scattering, and conventional and single-molecule X-ray diffraction experiments. Here, we review the current understanding of how such nanolipoparticles are formed and organized at the molecular level with an emphasis on their chemical diversity and factors affecting their size and solubilization efficiency.
Highlights
The study of three-dimensional structures of integral membrane proteins (MPs) is one of the main tasks of molecular biology
While styrene–maleic acid (SMA) copolymers are most popular as lipodisc-forming agents, several alternative amphiphilic polymers have been introduced over the recent years
electron paramagnetic resonance (EPR) spectroscopy of spin-label doxyl moieties incorporated into the lipid bilayer in the 5th or 16th position combined with differential scanning calorimetry (DSC) allowed characterizing the temperature-dependent lipid properties in a DMPC model membrane surrounded by Styrene–maleic acid (SMA), diisobutylene–maleic acid (DIBMA), or poly(styrene-co-maleic amide sulfobetaine) (SMA-SB), as compared to liposomes [105]
Summary
Bozdaganyan 1,2,4 , Natalia Voskoboynikova 5 , Armen Y. Karlova 1 , Anna Yudenko 7 , Alina Remeeva 7 , Yury L. Ryzhykau 7 , Ivan Gushchin 7 , Valentin I. Sokolova 1,2 , Heinz-Jürgen Steinhoff 5 , Mikhail P. N.N. Semenov Federal Research Center for Chemical Physics, Russian Academy of Sciences, 119991 Moscow, Russia. Faculty of Bioengineering and Bioinformatics and Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, 119234 Moscow, Russia. JuStruct: Jülich Center for Structural Biology, Forschungszentrum Jülich, 52428 Jülich, Germany. Publisher’s Note: MDPI stays neutral with regard to jurisdictional claims in published maps and institutional affiliations
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