TY - JOUR
T1 - A single-channel sensor based on gramicidin controlled by molecular recognition at bilayer lipid membranes containing receptor
AU - Hirano, Ayumi
AU - Wakabayashi, Masaki
AU - Matsuno, Yuka
AU - Sugawara, Masao
N1 - Funding Information:
This work was financially supported by grants from the Ministry of Education, Science and Culture. Financial support from research grant by College of Humanities and Sciences, Nihon University is also acknowledged.
PY - 2003/8/1
Y1 - 2003/8/1
N2 - A novel ion-channel sensor based on a membrane bound receptor and a single gramicidin channel is described, in which the binding of an analyte to the membrane bound receptor modulates the single-channel activity of gramicidin. The sensor is composed of a planar bilayer lipid membrane (BLM) containing biotin-labeled phosphatidylethanolamine as receptor for avidin and gramicidin as signal transducer. When the receptor catches an analyte (avidin or ferritin-labeled avidin (FA)) at the membrane surface, the bilayer structure is locally distorted and the gramicidin monomer/dimer kinetics is modulated in a manner that the fraction of channel opening with a short lifetime (≦100 ms) to the total opening events increases. The fraction was found to increase with the concentration of avidin from 1.0×10-9 to 1.0×10-6 M and of FA from 1.0×10-9 to 1.0×10-8 M. With dinitrophenyl-labeled PE embedded as receptor in the BLM for monoclonal anti-dinitrophenyl antibody (anti-DNP), the fraction of channel openings (≦100 ms) increased with the concentration of anti-DNP from 2.0×10-9 to 2.0×10-7 g/ml. Bovine serum albumin (BSA) and anti-BSA antibody caused no changes in the channel opening. The possible mechanism of analyte-induced modulation of single-channel activity of gramicidin is also discussed.
AB - A novel ion-channel sensor based on a membrane bound receptor and a single gramicidin channel is described, in which the binding of an analyte to the membrane bound receptor modulates the single-channel activity of gramicidin. The sensor is composed of a planar bilayer lipid membrane (BLM) containing biotin-labeled phosphatidylethanolamine as receptor for avidin and gramicidin as signal transducer. When the receptor catches an analyte (avidin or ferritin-labeled avidin (FA)) at the membrane surface, the bilayer structure is locally distorted and the gramicidin monomer/dimer kinetics is modulated in a manner that the fraction of channel opening with a short lifetime (≦100 ms) to the total opening events increases. The fraction was found to increase with the concentration of avidin from 1.0×10-9 to 1.0×10-6 M and of FA from 1.0×10-9 to 1.0×10-8 M. With dinitrophenyl-labeled PE embedded as receptor in the BLM for monoclonal anti-dinitrophenyl antibody (anti-DNP), the fraction of channel openings (≦100 ms) increased with the concentration of anti-DNP from 2.0×10-9 to 2.0×10-7 g/ml. Bovine serum albumin (BSA) and anti-BSA antibody caused no changes in the channel opening. The possible mechanism of analyte-induced modulation of single-channel activity of gramicidin is also discussed.
KW - Avidin
KW - Bilayer lipid membrane
KW - Biotinylated phosphatidylethanolamine
KW - Ferritin-labeled avidin
KW - Gramicidin
KW - Ion-channel sensor
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U2 - 10.1016/S0956-5663(02)00219-1
DO - 10.1016/S0956-5663(02)00219-1
M3 - Article
C2 - 12782460
AN - SCOPUS:0037681615
VL - 18
SP - 973
EP - 983
JO - Biosensors and Bioelectronics
JF - Biosensors and Bioelectronics
SN - 0956-5663
IS - 8
ER -