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Recent advances in membrane mimetics for membrane protein research

Membrane proteins are a highly relevant class of biological molecules and comprise ∼60% of current drug targets. Before being analyzed by structural, biochemical, and biophysical methods, membrane proteins must first be extracted from cellular membranes — often using detergents. Detergent-extracted...

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Detalles Bibliográficos
Autor principal: Young, John William
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Portland Press Ltd. 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10317169/
https://www.ncbi.nlm.nih.gov/pubmed/37345653
http://dx.doi.org/10.1042/BST20230164
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author Young, John William
author_facet Young, John William
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description Membrane proteins are a highly relevant class of biological molecules and comprise ∼60% of current drug targets. Before being analyzed by structural, biochemical, and biophysical methods, membrane proteins must first be extracted from cellular membranes — often using detergents. Detergent-extracted membrane proteins are amenable to analysis by structural, biochemical, and biophysical techniques. In certain cases, however, detergents can disturb native protein conformations and/or biological activity. This has led to the development of membrane mimetics, which stabilize membrane proteins in a native membrane-like environment that is water-soluble and detergent-free. This review provides an overview of recent developments in the membrane mimetic field, with a focus on nanodiscs, Saposin lipid nanoparticles (SapNPs), peptidiscs, and SMA lipid particles (SMALPs) — and highlights their utility for supporting biophysical, biochemical, and structural characterization of membrane proteins and complexes.
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spelling pubmed-103171692023-07-04 Recent advances in membrane mimetics for membrane protein research Young, John William Biochem Soc Trans Review Articles Membrane proteins are a highly relevant class of biological molecules and comprise ∼60% of current drug targets. Before being analyzed by structural, biochemical, and biophysical methods, membrane proteins must first be extracted from cellular membranes — often using detergents. Detergent-extracted membrane proteins are amenable to analysis by structural, biochemical, and biophysical techniques. In certain cases, however, detergents can disturb native protein conformations and/or biological activity. This has led to the development of membrane mimetics, which stabilize membrane proteins in a native membrane-like environment that is water-soluble and detergent-free. This review provides an overview of recent developments in the membrane mimetic field, with a focus on nanodiscs, Saposin lipid nanoparticles (SapNPs), peptidiscs, and SMA lipid particles (SMALPs) — and highlights their utility for supporting biophysical, biochemical, and structural characterization of membrane proteins and complexes. Portland Press Ltd. 2023-06-28 2023-06-22 /pmc/articles/PMC10317169/ /pubmed/37345653 http://dx.doi.org/10.1042/BST20230164 Text en © 2023 The Author(s) https://creativecommons.org/licenses/by/4.0/This is an open access article published by Portland Press Limited on behalf of the Biochemical Society and distributed under the Creative Commons Attribution License 4.0 (CC BY) (https://creativecommons.org/licenses/by/4.0/) . Open access for this article was enabled by the participation of University of Oxford in an all-inclusive Read & Publish agreement with Portland Press and the Biochemical Society under a transformative agreement with JISC.
spellingShingle Review Articles
Young, John William
Recent advances in membrane mimetics for membrane protein research
title Recent advances in membrane mimetics for membrane protein research
title_full Recent advances in membrane mimetics for membrane protein research
title_fullStr Recent advances in membrane mimetics for membrane protein research
title_full_unstemmed Recent advances in membrane mimetics for membrane protein research
title_short Recent advances in membrane mimetics for membrane protein research
title_sort recent advances in membrane mimetics for membrane protein research
topic Review Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10317169/
https://www.ncbi.nlm.nih.gov/pubmed/37345653
http://dx.doi.org/10.1042/BST20230164
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