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A Lipid Bilayer Formed on a Hydrogel Bead for Single Ion Channel Recordings

Ion channel proteins play important roles in various cell functions, making them attractive drug targets. Artificial lipid bilayer recording is a technique used to measure the ion transport activities of channel proteins with high sensitivity and accuracy. However, the measurement efficiency is low....

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Autores principales: Hirano, Minako, Yamamoto, Daiki, Asakura, Mami, Hayakawa, Tohru, Mise, Shintaro, Matsumoto, Akinobu, Ide, Toru
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7759777/
https://www.ncbi.nlm.nih.gov/pubmed/33271761
http://dx.doi.org/10.3390/mi11121070
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author Hirano, Minako
Yamamoto, Daiki
Asakura, Mami
Hayakawa, Tohru
Mise, Shintaro
Matsumoto, Akinobu
Ide, Toru
author_facet Hirano, Minako
Yamamoto, Daiki
Asakura, Mami
Hayakawa, Tohru
Mise, Shintaro
Matsumoto, Akinobu
Ide, Toru
author_sort Hirano, Minako
collection PubMed
description Ion channel proteins play important roles in various cell functions, making them attractive drug targets. Artificial lipid bilayer recording is a technique used to measure the ion transport activities of channel proteins with high sensitivity and accuracy. However, the measurement efficiency is low. In order to improve the efficiency, we developed a method that allows us to form bilayers on a hydrogel bead and record channel currents promptly. We tested our system by measuring the activities of various types of channels, including gramicidin, alamethicin, α-hemolysin, a voltage-dependent anion channel 1 (VDAC1), a voltage- and calcium-activated large conductance potassium channel (BK channel), and a potassium channel from Streptomyces lividans (KcsA channel). We confirmed the ability for enhanced measurement efficiency and measurement system miniaturizion.
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spelling pubmed-77597772020-12-26 A Lipid Bilayer Formed on a Hydrogel Bead for Single Ion Channel Recordings Hirano, Minako Yamamoto, Daiki Asakura, Mami Hayakawa, Tohru Mise, Shintaro Matsumoto, Akinobu Ide, Toru Micromachines (Basel) Article Ion channel proteins play important roles in various cell functions, making them attractive drug targets. Artificial lipid bilayer recording is a technique used to measure the ion transport activities of channel proteins with high sensitivity and accuracy. However, the measurement efficiency is low. In order to improve the efficiency, we developed a method that allows us to form bilayers on a hydrogel bead and record channel currents promptly. We tested our system by measuring the activities of various types of channels, including gramicidin, alamethicin, α-hemolysin, a voltage-dependent anion channel 1 (VDAC1), a voltage- and calcium-activated large conductance potassium channel (BK channel), and a potassium channel from Streptomyces lividans (KcsA channel). We confirmed the ability for enhanced measurement efficiency and measurement system miniaturizion. MDPI 2020-12-01 /pmc/articles/PMC7759777/ /pubmed/33271761 http://dx.doi.org/10.3390/mi11121070 Text en © 2020 by the authors. 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 (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Hirano, Minako
Yamamoto, Daiki
Asakura, Mami
Hayakawa, Tohru
Mise, Shintaro
Matsumoto, Akinobu
Ide, Toru
A Lipid Bilayer Formed on a Hydrogel Bead for Single Ion Channel Recordings
title A Lipid Bilayer Formed on a Hydrogel Bead for Single Ion Channel Recordings
title_full A Lipid Bilayer Formed on a Hydrogel Bead for Single Ion Channel Recordings
title_fullStr A Lipid Bilayer Formed on a Hydrogel Bead for Single Ion Channel Recordings
title_full_unstemmed A Lipid Bilayer Formed on a Hydrogel Bead for Single Ion Channel Recordings
title_short A Lipid Bilayer Formed on a Hydrogel Bead for Single Ion Channel Recordings
title_sort lipid bilayer formed on a hydrogel bead for single ion channel recordings
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7759777/
https://www.ncbi.nlm.nih.gov/pubmed/33271761
http://dx.doi.org/10.3390/mi11121070
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