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 | |
| Publication status | Published - Jul 21 2006 |
| Externally published | Yes |
Fingerprint
Keywords
- Lysenin
- Planar bilayer
- Single-channel
- Sphingomyelin
ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Molecular Biology
Cite this
Lysenin forms a voltage-dependent channel in artificial lipid bilayer membranes. / Ide, Toru; Aoki, Takaaki; Takeuchi, Yuko; Yanagida, Toshio.
In: Biochemical and Biophysical Research Communications, Vol. 346, No. 1, 21.07.2006, p. 288-292.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Lysenin forms a voltage-dependent channel in artificial lipid bilayer membranes
AU - Ide, Toru
AU - Aoki, Takaaki
AU - Takeuchi, Yuko
AU - Yanagida, Toshio
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
UR - http://www.scopus.com/inward/record.url?scp=33744976321&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=33744976321&partnerID=8YFLogxK
U2 - 10.1016/j.bbrc.2006.05.115
DO - 10.1016/j.bbrc.2006.05.115
M3 - Article
C2 - 16756950
AN - SCOPUS:33744976321
VL - 346
SP - 288
EP - 292
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 1
ER -