Lysenin forms a voltage-dependent channel in artificial lipid bilayer membranes

Toru Ide; Takaaki Aoki; Yuko Takeuchi; Toshio Yanagida

doi:10.1016/j.bbrc.2006.05.115

Lysenin forms a voltage-dependent channel in artificial lipid bilayer membranes

Toru Ide, Takaaki Aoki, Yuko Takeuchi, Toshio Yanagida

Research output: Contribution to journal › Article › peer-review

26 Citations (Scopus)

Abstract

Lysenin, a hemolytic protein derived from the body fluid of earthworm, was incorporated into artificial bilayer membranes. Upon insertion, it formed a voltage-dependent large conductance channel in asolectin bilayers in a sphingomyelin-dependent manner. The channel had low ion-selectivity. Single-channel conductance was calculated as approximately 550 pS in 100 mM KCl. The channel in asolectin bilayers closed when the membrane was held at a positive potential. In contrast, the channel showed no voltage dependency in membranes made of pure phosphatidylcholine and sphingomyelin, suggesting some lipid contents included in the asolectin membranes affected channel gating.

Original language	English
Pages (from-to)	288-292
Number of pages	5
Journal	Biochemical and Biophysical Research Communications
Volume	346
Issue number	1
DOIs	https://doi.org/10.1016/j.bbrc.2006.05.115
Publication status	Published - Jul 21 2006
Externally published	Yes

Keywords

Lysenin
Planar bilayer
Single-channel
Sphingomyelin

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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10.1016/j.bbrc.2006.05.115

Cite this

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title = "Lysenin forms a voltage-dependent channel in artificial lipid bilayer membranes",

abstract = "Lysenin, a hemolytic protein derived from the body fluid of earthworm, was incorporated into artificial bilayer membranes. Upon insertion, it formed a voltage-dependent large conductance channel in asolectin bilayers in a sphingomyelin-dependent manner. The channel had low ion-selectivity. Single-channel conductance was calculated as approximately 550 pS in 100 mM KCl. The channel in asolectin bilayers closed when the membrane was held at a positive potential. In contrast, the channel showed no voltage dependency in membranes made of pure phosphatidylcholine and sphingomyelin, suggesting some lipid contents included in the asolectin membranes affected channel gating.",

keywords = "Lysenin, Planar bilayer, Single-channel, Sphingomyelin",

author = "Toru Ide and Takaaki Aoki and Yuko Takeuchi and Toshio Yanagida",

note = "Funding Information: The authors thank our colleagues at Osaka University for valuable discussions and Dr. Peter Karagiannis for carefully revising the manuscript. This work was supported by grant from the Ministry of Education, Culture, Sports, Science and Technology of Japan (Promotion of Novel Interdisciplinary Fields Based on Nanotechnology and Materials).",

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T1 - Lysenin forms a voltage-dependent channel in artificial lipid bilayer membranes

AU - Ide, Toru

AU - Aoki, Takaaki

AU - Takeuchi, Yuko

AU - Yanagida, Toshio

N1 - Funding Information: The authors thank our colleagues at Osaka University for valuable discussions and Dr. Peter Karagiannis for carefully revising the manuscript. This work was supported by grant from the Ministry of Education, Culture, Sports, Science and Technology of Japan (Promotion of Novel Interdisciplinary Fields Based on Nanotechnology and Materials).

PY - 2006/7/21

Y1 - 2006/7/21

N2 - Lysenin, a hemolytic protein derived from the body fluid of earthworm, was incorporated into artificial bilayer membranes. Upon insertion, it formed a voltage-dependent large conductance channel in asolectin bilayers in a sphingomyelin-dependent manner. The channel had low ion-selectivity. Single-channel conductance was calculated as approximately 550 pS in 100 mM KCl. The channel in asolectin bilayers closed when the membrane was held at a positive potential. In contrast, the channel showed no voltage dependency in membranes made of pure phosphatidylcholine and sphingomyelin, suggesting some lipid contents included in the asolectin membranes affected channel gating.

AB - Lysenin, a hemolytic protein derived from the body fluid of earthworm, was incorporated into artificial bilayer membranes. Upon insertion, it formed a voltage-dependent large conductance channel in asolectin bilayers in a sphingomyelin-dependent manner. The channel had low ion-selectivity. Single-channel conductance was calculated as approximately 550 pS in 100 mM KCl. The channel in asolectin bilayers closed when the membrane was held at a positive potential. In contrast, the channel showed no voltage dependency in membranes made of pure phosphatidylcholine and sphingomyelin, suggesting some lipid contents included in the asolectin membranes affected channel gating.

KW - Lysenin

KW - Planar bilayer

KW - Single-channel

KW - Sphingomyelin

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JO - Biochemical and Biophysical Research Communications

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Lysenin forms a voltage-dependent channel in artificial lipid bilayer membranes

Abstract

Keywords

ASJC Scopus subject areas

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