TY - JOUR
T1 - In situ modification of lipid-loaded MCM-41 channels with bovine serum albumin at a planar lipid bilayer for biosensing
AU - Nozawa, Keiichiro
AU - Oshima, Azusa
AU - Nasu, Tomohiro
AU - Shoji, Atsushi
AU - Hirano-Iwata, Ayumi
AU - Niwano, Michio
AU - Sugawara, Masao
N1 - Funding Information:
The authors thank to Miss T. Tanaka and Mr. K. Sekine for their help in experiments. This work was financially supported by Grant-in-Aid for Scientific and Research (B) (no. 21350045 ) from the Ministry of Education, Culture, Sports, Science, and Technology of Japan . Financial support from a research grant from the College of Humanities and Sciences at Nihon University is also acknowledged. One (A. H.-I.) of the authors thanks PRESTO, Japan Science and Technology Agency (JST) for the financial support.
PY - 2011/12/15
Y1 - 2011/12/15
N2 - An in situ method for modifying a receptor site on mesoporous silica MCM-41 channels in planar lipid bilayers is described, in which bovine serum albumin (BSA) is covalently linked to the MCM-41 channels via head groups of lipids loaded in the nanopores. Prior to receptor modification, lipid-loaded MCM-41 channels were incorporated with lipid bilayers formed at an aperture of a Teflon film. The in situ coupling of BSA to lipid-loaded MCM-41 channels at the lipid bilayer interface was achieved by the sulfhydryl coupling method. The lipid bilayers containing BSA-modified MCM-41 exhibited channel-like currents, which were augmented in a concentration-dependent manner by the addition of anti-BSA at fM level. The in situ modification of lipid-loaded MCM-41 channels with BSA by the amine coupling technique was also investigated. The potential of the present approach for the development of channel-type biosensors is discussed in terms of modifying bilayer interfaces with bioreceptors.
AB - An in situ method for modifying a receptor site on mesoporous silica MCM-41 channels in planar lipid bilayers is described, in which bovine serum albumin (BSA) is covalently linked to the MCM-41 channels via head groups of lipids loaded in the nanopores. Prior to receptor modification, lipid-loaded MCM-41 channels were incorporated with lipid bilayers formed at an aperture of a Teflon film. The in situ coupling of BSA to lipid-loaded MCM-41 channels at the lipid bilayer interface was achieved by the sulfhydryl coupling method. The lipid bilayers containing BSA-modified MCM-41 exhibited channel-like currents, which were augmented in a concentration-dependent manner by the addition of anti-BSA at fM level. The in situ modification of lipid-loaded MCM-41 channels with BSA by the amine coupling technique was also investigated. The potential of the present approach for the development of channel-type biosensors is discussed in terms of modifying bilayer interfaces with bioreceptors.
KW - Anti-BSA antibody
KW - Bovine serum albumin
KW - In situ modification of bioreceptor
KW - Lipid bilayer
KW - MCM-41 channel
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U2 - 10.1016/j.snb.2011.07.024
DO - 10.1016/j.snb.2011.07.024
M3 - Article
AN - SCOPUS:81155152489
VL - 160
SP - 139
EP - 144
JO - Sensors and Actuators, B: Chemical
JF - Sensors and Actuators, B: Chemical
SN - 0925-4005
IS - 1
ER -