Conclusion
The rich properties of engineered carbon nanotubes will find themselves in wide range of biological and medicinal applications. Combining the natural biological molecular recognition process by natural proteins (ion channels, for example) with the properties of carbon nanotubes, an integrated new class of hybrid devices of carbon nanotubes and biological proteins will have versatile unprecedented selectivity, sensitivity, efficiency, and controllability.
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References
Bertil Hille. Ionic Channels of Excitable Membranes. Sinauer Associates Inc., Sunderland, Massachusetts, second edition, 1992.
Lawrence H. Pinto, L. J. Holsinger, and R. A. Lamb, Influenza virus protein has ion channel activity, Cell, 69, 517–528 (1992).
D. Dawson, editor. Ion Channels and Genetic Diseases. Society of General Physiologists. Rockefeller University Press, New York, 1995.
S. W. Cowan, T. Schirmer, G. Rummel, M. Steiert, R. Ghosh, R. A. Pauptit, J. N. Jansonius, and J. Rosenbusch, Crystal structures explain two functional properties of two E. coli porins, Nature, 358, 727–733 (1992).
Denis Jeanteur, Tilman Schirmer, Didier Fourel, Valerie Simonet, Gabriele Rummel, Christine Widmer, Jurg P. Rosenbusch, Franc Pattus, and Jean-Marie Pagès, Structural and functional alterations of a colicin-resistant mutant of OmpF porin from Escherichia coli, Proc. Natl. Acad. Sci. USA, 91, 10675–10679 (1994).
Roger Sayle. RasMol: Molecular Graphics Visualisation tool. Biomolecular Structures Group, Glaxo Wellcome Research & Development, Stevenage, Hertfordshire, UK, 1995.
R. Misra and S. A. Benson, Genetic identification of the pore domain of the OmpC porin of Escherichia coli K-12, J. Bacteriol., 170, 3611–3617 (1988).
G. Meissner, Ryanodine activation and inhibition of the Ca2+ release channel of sarcoplasmic reticulum, J. Biol. Chem., 261, 6300–6306 (1986).
J. Smith, T. Imagawa, J. Ma, M. Fill, K. Campbell, and R. Coronado, Purified ryanodine receptor from rabbit skeletal muscle is the calcium-release channel of sarcoplasmic reticulum, J. Gen. Physiol, 92, 1–26 (1988).
B. Jap and P. Walian, Biophysics of structure and function of porin, Quart. Rev. Biophys., 23, 367–403 (1990).
H. Nikaido, Transport across the bacterial outer membrane, J. Bioenerg. Biomembr., 25, 581–589 (1993).
Jurg Rosenbusch. Porins In Phosphate in Microorganisms. Celluar and Molecular Biology, A. Torriani-Gorini, E. Yagil, and S. Silver, editors, pages 329–334. ASM Press, Washington, DC, 1994.
Xuanqing Jiang, Marvin A. Payne, Zhenghua Cao, Samuel B. Foster, Jimmy B. Feix, Salete M. C. Newton, and Phillip E. Klebba, Ligand-specific opening of a gated-porin channel in the outer membrane of living bacteria, Secience, 276, 1261–1264 (1997).
D. A. Doyle, J. M. Cabral, Richard A. Pfuetzner, A. Kuo, J. M. Gulbis, S. L. Cohen, B. T. Chait, and R. MacKinnon, The structure of the potassium channel: Molecular basis of K + conduction and selectivity, Science, 280, 69–77 (1998).
Bert Sakmann and Erwin Neher, editors. Single Channel Recording. Plenum Press, New York, 2nd edition, 1995.
Duan P. Chen, Le Xu, Ashutosh Tripathy, Gerhard Meissner, and Bob Eisenberg, Permeation through the calcium release channel of cardiac muscle, Biophys. J., 73, 1337–1354 (1997).
V. Barcilon, D. P. Chen, R. S. Eisenberg, and M. A. Ratner, Barrier crossing with concentration boundary conditions in biological channels and chemical reactions, J. Chem. Phys., 98, 1193–1212 (1993).
Masakatsu Watanabe, J. Rosenbusch, T. Schirmer, and Martin Karplus, Computer simulations of the OmpF porin from the outer memebrane of Escherichia coli, Biophys. J., 72, 2094–2102 (1997).
S.-W. Chiu, S. Subramaniam, E. Jakobsson, and J. A. McCammon, Water and polypeptide conformations in the gramicidin channel: a molecular dynamics study, Biophys. J., 56, 253–261 (1989).
Johan Åqvist and Arieh Warshel, Energetics of ion permeation through membrane channels, solvation of Na+ by gramicidin A, Biophys. J., 56, 171–182 (1989).
Benoit Roux and Martin Karplus, Ion transport in a model gramicidin channel: structure and thermodynamics, Biophys. J., 59, 961–981 (1991).
Wonpil Im and Benoit Roux, Ion and counterions in a biological channel: A molecular dynamics simulation of ompf porin from escherichia coli in an explicit membrane with 1m kcl aqueous salt solution, J. Mol. Biol., 319, 1177–1197 (2002).
Wonpil Im and Benoit Roux, Ion permeation and selectivity of ompf porin: A theoretical study based on molecular dynamics, brownian dynamics and continuum electrodiffusion theory, J. Mol. Biol., 322, 851–869 (2002).
Duan P. Chen, Le Xu, Ashutosh Tripathy, Gerhard Meissner, and Bob Eisenberg, Selectivity and permeation through the calcium release channel of cardiac muscle: Monovalent alkaline metal ions, Biophys. J., 76, 1346–1366 (1999).
Duan P. Chen, Le Xu, Bob Eisenberg, and Gerhard Meissner, Calcium ion permeation through the calcium release channel (ryanodine receptor) of cardiac muscle, J. Phys. Chem., 107, 9139–9145 (2003).
Z. Schuss, B. Nadler, and R. S. Eisenberg, Derivation of poisson and nernstplanck equations in a bath and channel from a molecular model, Phys. Rev. E, 64, 036116-1–036116-14 (2001).
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Chen, D.P. (2004). Bridging Natural Nano-Tubes with Designed Nanotubes. In: Stroscio, M.A., Dutta, M. (eds) Biological Nanostructures and Applications of Nanostructures in Biology. Bioelectric Engineering. Springer, Boston, MA. https://doi.org/10.1007/0-306-48628-8_7
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DOI: https://doi.org/10.1007/0-306-48628-8_7
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