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. 2024 Oct 14;25(10):6611-6623.
doi: 10.1021/acs.biomac.4c00772. Epub 2024 Sep 16.

Vinyl Ether Maleic Acid Polymers: Tunable Polymers for Self-Assembled Lipid Nanodiscs and Environments for Membrane Proteins

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Vinyl Ether Maleic Acid Polymers: Tunable Polymers for Self-Assembled Lipid Nanodiscs and Environments for Membrane Proteins

Muhammad Zeeshan Shah et al. Biomacromolecules. .

Abstract

Native lipid bilayer mimetics, including those that use amphiphilic polymers, are important for the effective study of membrane-bound peptides and proteins. Copolymers of vinyl ether monomers and maleic anhydride were developed with controlled molecular weights and hydrophobicity through reversible addition-fragmentation chain-transfer polymerization. After polymerization, the maleic anhydride units can be hydrolyzed, giving dicarboxylates. The vinyl ether and maleic anhydride copolymerized in a close to alternating manner, giving essentially alternating hydrophilic maleic acid units and hydrophobic vinyl ether units along the backbone after hydrolysis. The vinyl ether monomers and maleic acid polymers self-assembled with lipids, giving vinyl ether maleic acid lipid particles (VEMALPs) with tunable sizes controlled by either the vinyl ether hydrophobicity or the polymer molecular weight. These VEMALPs were able to support membrane-bound proteins and peptides, creating a new class of lipid bilayer mimetics.

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References

    1. Chen A; Majdinasab EJ; Fiori MC; Liang H; Altenberg GA Polymer-Encased Nanodiscs and Polymer Nanodiscs: New Platforms for Membrane Protein Research and Applications. Front. Bioeng. Biotechnol 2020, 8, 598450. 10.3389/fbioe.2020.598450. - DOI - PMC - PubMed
    1. Dürr UHN; Gildenberg M; Ramamoorthy A The Magic of Bicelles Lights Up Membrane Protein Structure. Chem. Rev 2012, 112 (11), 6054–6074. 10.1021/cr300061w. - DOI - PMC - PubMed
    1. Ravula T; Hardin NZ; Ramamoorthy A Polymer Nanodiscs: Advantages and Limitations. Chem. Phys. Lipids 2019, 219, 45–49. 10.1016/j.chemphyslip.2019.01.010. - DOI - PMC - PubMed
    1. Cournia Z; Allen TW; Andricioaei I; Antonny B; Baum D; Brannigan G; Buchete N-V; Deckman JT; Delemotte L; del Val C; Friedman R; Gkeka P; Hege H-C; Hénin J; Kasimova MA; Kolocouris A; Klein ML; Khalid S; Lemieux MJ; Lindow N; Roy M; Selent J; Tarek M; Tofoleanu F; Vanni S; Urban S; Wales DJ; Smith JC; Bondar A-N Membrane Protein Structure, Function, and Dynamics: A Perspective from Experiments and Theory. J. Membr. Biol 2015, 248 (4), 611–640. 10.1007/s00232-015-9802-0. - DOI - PMC - PubMed
    1. Gordon EA; Richardson YB; Shah MZ; Burridge KM; Konkolewicz D; Lorigan GA Formation of Styrene Maleic Acid Lipid Nanoparticles (SMALPs) Using SMA Thin Film on a Substrate. Anal. Biochem 2022, 647, 114692. 10.1016/j.ab.2022.114692. - DOI - PubMed

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