Cargando…
Mechanisms of Formation, Structure, and Dynamics of Lipoprotein Discs Stabilized by Amphiphilic Copolymers: A Comprehensive Review
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 p...
Autores principales: | , , , , , , , , , , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2022
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8838559/ https://www.ncbi.nlm.nih.gov/pubmed/35159706 http://dx.doi.org/10.3390/nano12030361 |
_version_ | 1784650157076250624 |
---|---|
author | Orekhov, Philipp S. Bozdaganyan, Marine E. Voskoboynikova, Natalia Mulkidjanian, Armen Y. Karlova, Maria G. Yudenko, Anna Remeeva, Alina Ryzhykau, Yury L. Gushchin, Ivan Gordeliy, Valentin I. Sokolova, Olga S. Steinhoff, Heinz-Jürgen Kirpichnikov, Mikhail P. Shaitan, Konstantin V. |
author_facet | Orekhov, Philipp S. Bozdaganyan, Marine E. Voskoboynikova, Natalia Mulkidjanian, Armen Y. Karlova, Maria G. Yudenko, Anna Remeeva, Alina Ryzhykau, Yury L. Gushchin, Ivan Gordeliy, Valentin I. Sokolova, Olga S. Steinhoff, Heinz-Jürgen Kirpichnikov, Mikhail P. Shaitan, Konstantin V. |
author_sort | Orekhov, Philipp S. |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-8838559 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-88385592022-02-13 Mechanisms of Formation, Structure, and Dynamics of Lipoprotein Discs Stabilized by Amphiphilic Copolymers: A Comprehensive Review Orekhov, Philipp S. Bozdaganyan, Marine E. Voskoboynikova, Natalia Mulkidjanian, Armen Y. Karlova, Maria G. Yudenko, Anna Remeeva, Alina Ryzhykau, Yury L. Gushchin, Ivan Gordeliy, Valentin I. Sokolova, Olga S. Steinhoff, Heinz-Jürgen Kirpichnikov, Mikhail P. Shaitan, Konstantin V. Nanomaterials (Basel) Review 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. MDPI 2022-01-23 /pmc/articles/PMC8838559/ /pubmed/35159706 http://dx.doi.org/10.3390/nano12030361 Text en © 2022 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Review Orekhov, Philipp S. Bozdaganyan, Marine E. Voskoboynikova, Natalia Mulkidjanian, Armen Y. Karlova, Maria G. Yudenko, Anna Remeeva, Alina Ryzhykau, Yury L. Gushchin, Ivan Gordeliy, Valentin I. Sokolova, Olga S. Steinhoff, Heinz-Jürgen Kirpichnikov, Mikhail P. Shaitan, Konstantin V. Mechanisms of Formation, Structure, and Dynamics of Lipoprotein Discs Stabilized by Amphiphilic Copolymers: A Comprehensive Review |
title | Mechanisms of Formation, Structure, and Dynamics of Lipoprotein Discs Stabilized by Amphiphilic Copolymers: A Comprehensive Review |
title_full | Mechanisms of Formation, Structure, and Dynamics of Lipoprotein Discs Stabilized by Amphiphilic Copolymers: A Comprehensive Review |
title_fullStr | Mechanisms of Formation, Structure, and Dynamics of Lipoprotein Discs Stabilized by Amphiphilic Copolymers: A Comprehensive Review |
title_full_unstemmed | Mechanisms of Formation, Structure, and Dynamics of Lipoprotein Discs Stabilized by Amphiphilic Copolymers: A Comprehensive Review |
title_short | Mechanisms of Formation, Structure, and Dynamics of Lipoprotein Discs Stabilized by Amphiphilic Copolymers: A Comprehensive Review |
title_sort | mechanisms of formation, structure, and dynamics of lipoprotein discs stabilized by amphiphilic copolymers: a comprehensive review |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8838559/ https://www.ncbi.nlm.nih.gov/pubmed/35159706 http://dx.doi.org/10.3390/nano12030361 |
work_keys_str_mv | AT orekhovphilipps mechanismsofformationstructureanddynamicsoflipoproteindiscsstabilizedbyamphiphiliccopolymersacomprehensivereview AT bozdaganyanmarinee mechanismsofformationstructureanddynamicsoflipoproteindiscsstabilizedbyamphiphiliccopolymersacomprehensivereview AT voskoboynikovanatalia mechanismsofformationstructureanddynamicsoflipoproteindiscsstabilizedbyamphiphiliccopolymersacomprehensivereview AT mulkidjanianarmeny mechanismsofformationstructureanddynamicsoflipoproteindiscsstabilizedbyamphiphiliccopolymersacomprehensivereview AT karlovamariag mechanismsofformationstructureanddynamicsoflipoproteindiscsstabilizedbyamphiphiliccopolymersacomprehensivereview AT yudenkoanna mechanismsofformationstructureanddynamicsoflipoproteindiscsstabilizedbyamphiphiliccopolymersacomprehensivereview AT remeevaalina mechanismsofformationstructureanddynamicsoflipoproteindiscsstabilizedbyamphiphiliccopolymersacomprehensivereview AT ryzhykauyuryl mechanismsofformationstructureanddynamicsoflipoproteindiscsstabilizedbyamphiphiliccopolymersacomprehensivereview AT gushchinivan mechanismsofformationstructureanddynamicsoflipoproteindiscsstabilizedbyamphiphiliccopolymersacomprehensivereview AT gordeliyvalentini mechanismsofformationstructureanddynamicsoflipoproteindiscsstabilizedbyamphiphiliccopolymersacomprehensivereview AT sokolovaolgas mechanismsofformationstructureanddynamicsoflipoproteindiscsstabilizedbyamphiphiliccopolymersacomprehensivereview AT steinhoffheinzjurgen mechanismsofformationstructureanddynamicsoflipoproteindiscsstabilizedbyamphiphiliccopolymersacomprehensivereview AT kirpichnikovmikhailp mechanismsofformationstructureanddynamicsoflipoproteindiscsstabilizedbyamphiphiliccopolymersacomprehensivereview AT shaitankonstantinv mechanismsofformationstructureanddynamicsoflipoproteindiscsstabilizedbyamphiphiliccopolymersacomprehensivereview |