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Fluorescence Approaches for Characterizing Ion Channels in Synthetic Bilayers

Ion channels are membrane proteins that play important roles in a wide range of fundamental cellular processes. Studying membrane proteins at a molecular level becomes challenging in complex cellular environments. Instead, many studies focus on the isolation and reconstitution of the membrane protei...

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Detalles Bibliográficos
Autores principales: Islam, Md. Sirajul, Gaston, James P., Baker, Matthew A. B.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8619978/
https://www.ncbi.nlm.nih.gov/pubmed/34832086
http://dx.doi.org/10.3390/membranes11110857
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author Islam, Md. Sirajul
Gaston, James P.
Baker, Matthew A. B.
author_facet Islam, Md. Sirajul
Gaston, James P.
Baker, Matthew A. B.
author_sort Islam, Md. Sirajul
collection PubMed
description Ion channels are membrane proteins that play important roles in a wide range of fundamental cellular processes. Studying membrane proteins at a molecular level becomes challenging in complex cellular environments. Instead, many studies focus on the isolation and reconstitution of the membrane proteins into model lipid membranes. Such simpler, in vitro, systems offer the advantage of control over the membrane and protein composition and the lipid environment. Rhodopsin and rhodopsin-like ion channels are widely studied due to their light-interacting properties and are a natural candidate for investigation with fluorescence methods. Here we review techniques for synthesizing liposomes and for reconstituting membrane proteins into lipid bilayers. We then summarize fluorescence assays which can be used to verify the functionality of reconstituted membrane proteins in synthetic liposomes.
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spelling pubmed-86199782021-11-27 Fluorescence Approaches for Characterizing Ion Channels in Synthetic Bilayers Islam, Md. Sirajul Gaston, James P. Baker, Matthew A. B. Membranes (Basel) Review Ion channels are membrane proteins that play important roles in a wide range of fundamental cellular processes. Studying membrane proteins at a molecular level becomes challenging in complex cellular environments. Instead, many studies focus on the isolation and reconstitution of the membrane proteins into model lipid membranes. Such simpler, in vitro, systems offer the advantage of control over the membrane and protein composition and the lipid environment. Rhodopsin and rhodopsin-like ion channels are widely studied due to their light-interacting properties and are a natural candidate for investigation with fluorescence methods. Here we review techniques for synthesizing liposomes and for reconstituting membrane proteins into lipid bilayers. We then summarize fluorescence assays which can be used to verify the functionality of reconstituted membrane proteins in synthetic liposomes. MDPI 2021-11-04 /pmc/articles/PMC8619978/ /pubmed/34832086 http://dx.doi.org/10.3390/membranes11110857 Text en © 2021 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
Islam, Md. Sirajul
Gaston, James P.
Baker, Matthew A. B.
Fluorescence Approaches for Characterizing Ion Channels in Synthetic Bilayers
title Fluorescence Approaches for Characterizing Ion Channels in Synthetic Bilayers
title_full Fluorescence Approaches for Characterizing Ion Channels in Synthetic Bilayers
title_fullStr Fluorescence Approaches for Characterizing Ion Channels in Synthetic Bilayers
title_full_unstemmed Fluorescence Approaches for Characterizing Ion Channels in Synthetic Bilayers
title_short Fluorescence Approaches for Characterizing Ion Channels in Synthetic Bilayers
title_sort fluorescence approaches for characterizing ion channels in synthetic bilayers
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8619978/
https://www.ncbi.nlm.nih.gov/pubmed/34832086
http://dx.doi.org/10.3390/membranes11110857
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