The gramicidin-based biosensor: a functioning nano-machine.

作者: B. A. Cornell , V. L. B. Braach-Maksvytis , L. G. King , P. D. J. Osman , B. Raguse

DOI: 10.1002/9780470515716.CH15

关键词: GramicidinBiosensorBiophysicsBilayerChemistryOrders of magnitude (temperature)Ion channelNanotechnologyGated Ion ChannelAnalyteMembrane

摘要: Biosensors combine a biological recognition mechanism with physical transduction technique. In nature, the for high sensitivity molecular detection is modulation of cell membrane ionic conductivity through specific ligand-receptor binding-induced switching ion channels. This effects an inherent signal amplification six to eight orders magnitude, corresponding total flow arising from single channel gating event. Here we describe first reduction this principle practical sensing device, which planar impedance element composed macroscopically supported synthetic bilayer incorporating gramicidin The and reservoir are covalently attached evaporated gold surface. channels have receptor groups (usually antibodies) that permit by analyte binding receptors. device may then be made wide range analytes, including proteins, drugs, hormones, antibodies, DNA, etc., currently in 10(-7)-10(-13) M range. It also lends itself readily microelectronic fabrication transduction. By adjusting surface density receptors/channel components during fabrication, optimum tuned over several magnitude.

参考文章(27)
See-Wing Chiu, Kamalakar Gulukota, Eric Jakobsson, Computational Approaches to Understanding the Ion Channel-Lipid System Springer, Dordrecht. pp. 315- 338 ,(1992) , 10.1007/978-94-011-2718-9_26
Valerie B. Myers, D.A. Haydon, Ion transfer across lipid membranes in the presence of gramicidin A Biochimica et Biophysica Acta (BBA) - Biomembranes. ,vol. 274, pp. 313- 322 ,(1972) , 10.1016/0005-2736(72)90179-4
D. Busath, G. Szabo, Permeation characteristics of gramicidin conformers. Biophysical Journal. ,vol. 53, pp. 697- 707 ,(1988) , 10.1016/S0006-3495(88)83151-5
J Bufler, S Kahlert, S Tzartos, K V Toyka, A Maelicke, C Franke, Activation and blockade of mouse muscle nicotinic channels by antibodies directed against the binding site of the acetylcholine receptor. The Journal of Physiology. ,vol. 492, pp. 107- 114 ,(1996) , 10.1113/JPHYSIOL.1996.SP021293
S. Cukierman, E.P. Quigley, D.S. Crumrine, Proton conduction in gramicidin A and in its dioxolane-linked dimer in different lipid bilayers Biophysical Journal. ,vol. 73, pp. 2489- 2502 ,(1997) , 10.1016/S0006-3495(97)78277-8
Steven R Reiken, Bernard J Van Wie, Himawan Sutisna, David F Moffett, Alan R Koch, Moris Silber, William C Davis, Bispecific antibody modification of nicotinic acetylcholine receptors for biosensing Biosensors and Bioelectronics. ,vol. 11, pp. 91- 102 ,(1996) , 10.1016/0956-5663(96)83716-X
Denise V. Greathouse, James F. Hinton, Kyung S. Kim, Roger E. Koeppe, Gramicidin A/short-chain phospholipid dispersions: chain length dependence of gramicidin conformation and lipid organization. Biochemistry. ,vol. 33, pp. 4291- 4299 ,(1994) , 10.1021/BI00180A025
Evyatar Av-Ron, Jean-Pierre Rospars, Modeling insect olfactory neuron signaling by a network utilizing disinhibition BioSystems. ,vol. 36, pp. 101- 108 ,(1995) , 10.1016/0303-2647(95)01531-O
A. Ring, J. Sandblom, Modulation of gramicidin A open channel lifetime by ion occupancy Biophysical Journal. ,vol. 53, pp. 549- 559 ,(1988) , 10.1016/S0006-3495(88)83135-7
S. Dante, M. De Rosa, E. Maccioni, A. Morana, C. Nicolini, F Rustichelli, V. I. Troitsky, B. Yang, Thermal, Stability of Bipolar Lipid Langmuir Blodgett Films by X-Ray Diffraction Molecular Crystals and Liquid Crystals. ,vol. 262, pp. 191- 207 ,(1995) , 10.1080/10587259508033525