» Articles » PMID: 33304891

Polymer-Encased Nanodiscs and Polymer Nanodiscs: New Platforms for Membrane Protein Research and Applications

Overview
Date 2020 Dec 11
PMID 33304891
Citations 13
Authors
Affiliations
Soon will be listed here.
Abstract

Membrane proteins (MPs) are essential to many organisms' major functions. They are notorious for being difficult to isolate and study, and mimicking native conditions for studies has proved to be a challenge. Lipid nanodiscs are among the most promising platforms for MP reconstitution, but they contain a relatively labile lipid bilayer and their use requires previous protein solubilization in detergent. These limitations have led to the testing of copolymers in new types of nanodisc platforms. Polymer-encased nanodiscs and polymer nanodiscs support functional MPs and address some of the limitations present in other MP reconstitution platforms. In this review, we provide a summary of recent developments in the use of polymers in nanodiscs.

Citing Articles

Unsymmetric Triazine-Based Triglucoside Detergents for Membrane Protein Stability.

Ehsan M, Ghani L, Lan B, Katsube S, Poulsen I, Zhang X Chembiochem. 2025; 26(5):e202400958.

PMID: 39779472 PMC: 11875885. DOI: 10.1002/cbic.202400958.


On the Properties of Styrene-Maleic Acid Copolymer-Lipid Nanoparticles: A Solution NMR Perspective.

Motov V, Kot E, Kislova S, Bocharov E, Arseniev A, Boldyrev I Polymers (Basel). 2024; 16(21).

PMID: 39518219 PMC: 11548547. DOI: 10.3390/polym16213009.


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

Shah M, Rotich N, Okorafor E, Oestreicher Z, Demidovich G, Eapen J Biomacromolecules. 2024; 25(10):6611-6623.

PMID: 39283997 PMC: 11473226. DOI: 10.1021/acs.biomac.4c00772.


NINJ1 mediates plasma membrane rupture by cutting and releasing membrane disks.

David L, Borges J, Hollingsworth L, Volchuk A, Jansen I, Garlick E Cell. 2024; 187(9):2224-2235.e16.

PMID: 38614101 PMC: 11055670. DOI: 10.1016/j.cell.2024.03.008.


Exploring the World of Membrane Proteins: Techniques and Methods for Understanding Structure, Function, and Dynamics.

Boulos I, Jabbour J, Khoury S, Mikhael N, Tishkova V, Candoni N Molecules. 2023; 28(20).

PMID: 37894653 PMC: 10608922. DOI: 10.3390/molecules28207176.


References
1.
Routledge S, Jamshad M, Little H, Lin Y, Simms J, Thakker A . Ligand-induced conformational changes in a SMALP-encapsulated GPCR. Biochim Biophys Acta Biomembr. 2020; 1862(6):183235. PMC: 7156913. DOI: 10.1016/j.bbamem.2020.183235. View

2.
Hall S, Tognoloni C, Charlton J, Bragginton E, Rothnie A, Sridhar P . An acid-compatible co-polymer for the solubilization of membranes and proteins into lipid bilayer-containing nanoparticles. Nanoscale. 2018; 10(22):10609-10619. PMC: 5996351. DOI: 10.1039/c8nr01322e. View

3.
Hesketh S, Klebl D, Higgins A, Thomsen M, Pickles I, Sobott F . Styrene maleic-acid lipid particles (SMALPs) into detergent or amphipols: An exchange protocol for membrane protein characterisation. Biochim Biophys Acta Biomembr. 2020; 1862(5):183192. PMC: 7086155. DOI: 10.1016/j.bbamem.2020.183192. View

4.
Skrzypek R, Iqbal S, Callaghan R . Methods of reconstitution to investigate membrane protein function. Methods. 2018; 147:126-141. DOI: 10.1016/j.ymeth.2018.02.012. View

5.
Dorr J, Koorengevel M, Schafer M, Prokofyev A, Scheidelaar S, van der Cruijsen E . Detergent-free isolation, characterization, and functional reconstitution of a tetrameric K+ channel: the power of native nanodiscs. Proc Natl Acad Sci U S A. 2014; 111(52):18607-12. PMC: 4284610. DOI: 10.1073/pnas.1416205112. View