Imaging and Characterization of Macromolecular Interface Structures for Whole Cell Biosensors

  • Vincent B. Pizziconi
  • Darren L. Page
Chapter

Abstract

Biosensor development continues to receive wide attention from researchers in the biomedical and biotechnology communities. The sustained level of interest in biosensors is due to the steady and marked evolution in biosensor technology which incorporates the latest advances in electrochemical, optoelectrical, piezoelectric, field effect transistors, and thermal transducer design. Even more promising approaches are now being explored resulting from advances made in the new frontiers of nanofabrication and molecular biology. One example of the latter is the exploitation of biological structures as the sensing elements of biosensors. This ‘hybrid’ approach represents a significant departure from ‘traditional’ chemical sensors which utilize strictly synthetic materials to detect biochemical events. The integration of advanced transducer design with complex, biologically active sensing elements holds great promise due to the superior detection capabilities offered by biological materials. Moreover, the newly emerging fields of molecular bioengineering and nanoengineering may ultimately provide the basis for the rational design of hybrid biosensors and other molecular-based devices as demonstrated by this feasibility study and other companion papers in this proceeding.

Keywords

Scan Tunneling Microscopy Biological Component Immobilization Method Critical Surface Tension Suspension Cell Line 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
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References

  1. 1.
    I. Karube and M. Suzuki, Microbial Biosensors, in: “Biosensors,” A. E. G. Cass, ed., Oxford University Press, New York (1990).Google Scholar
  2. 2.
    J. W. Parce, J. O. Owicki, K. M. Kersco, G. B. Sigal, H. G. Wada, V. C. Muir, L. J. Bousse, K. L. Ross, B. I. Sikic, H. M. McDonnel, Detection of cell-affecting agents with a silicon biosensor, Science 246:243 (1989).PubMedCrossRefGoogle Scholar
  3. 3.
    D. M. Rawson, A. J. Willmer, Whole-cell biosensors for environmental monitoring, Biosensors 4:299 (1989).PubMedCrossRefGoogle Scholar
  4. 4.
    I. Karube, Hybrid biosensors for clinical analysis and fermentation control, in: “Methods in Enzymology: Immobilized Enzymes and Cells,” Volume 137, Part D, K. Mosbach, ed., Academic Press Inc., San Diego (1988).Google Scholar
  5. 5.
    V. B. Pizziconi and D. L. Page, Whole cell biosensors in artificial organs, Trans. ASAIO (in preparation).Google Scholar
  6. 6.
    G. A. Rechnitz, Biosensors, Chemical Engineering News 66:24 (1988).CrossRefGoogle Scholar
  7. 7.
    D. G. Parce, Light-addressable Potentiometrie sensor for biochemical systems, Science 240:1182 (1988).PubMedCrossRefGoogle Scholar
  8. 8.
    E. J. Guilbeau, B. C Towe, and M. J. Muelbauer, Potentilly implantable thermoelectric sensor for measuremenmt of glucose, Trans. ASAIO 10(3):329 (1987).Google Scholar
  9. 9.
    V. B. Pizziconi and D. L. Page, The elucidation of macromolecular assemblies using scanning tunneling microscopy for the molecular bioengineering of cellular self-assemblies in molecular device design, in: “ACS Symposium Series No. 493, Macromolecular Assemblies in Polymeric Systems,” P. Stroeve and A. C. Balazs, eds., Chemical Society, Washington, DC (1992).Google Scholar
  10. 10.
    J. S. Sidwell and G. A. Rechnitz, Progress and challenges for biosensors using plant tissue materials, Biosensors 2:221 (1986).CrossRefGoogle Scholar
  11. 11.
    A. Navaratne and G. A. Rechnitz, Improved plant tissue-based biosensor using in-vitro cultured tobacco callus tissue, Analytica Chimica Acta 257:59 (1992).CrossRefGoogle Scholar
  12. 12.
    D. G. Margineau and H. Vais, Bioelectrochemical sensors with living cells, in: “Bioinstrumentation: Research, Developments and Applications,” D. Wise ed., Butterworths, Boston (1990).Google Scholar
  13. 13.
    G. Xiuli, L. Yuqi, and Y. Guanghua, Study and application of a new adenosine electrode with thymus tissue, Biosensors & Bioelectronics 7:21 (1992).CrossRefGoogle Scholar
  14. 14.
    D. Wijesuriya and G. A. Rechnitz, Analytica Chimica Acta 256:39 (1992).CrossRefGoogle Scholar
  15. 15.
    R. M. Buch, T. Q. Barker, and G. A. Rechnitz, Intact chemoreceptor biosensors based on hawaiian aquatic species, Analytica Chimica Acta 243:157 (1991).CrossRefGoogle Scholar
  16. 16.
    E. A. H. Hall, “Biosensors,” London (1990).Google Scholar
  17. 17.
    J. Woodward, ed., “Immobilized Cells and Enzymes: A Practical Approach,” IRL Press, Oxford (1985).Google Scholar
  18. 18.
    K. Mosbach, ed., “Methods in Enzymology: Immobilized Enzymes and Cells,” Part B, Volume 135, Academic Press Inc., Orlando (1987).Google Scholar
  19. 19.
    K. Mosbach, ed., “Methods in Enzymology: Immobilized Enzymes and Cells,” Part C, Volume 136, Academic Press Inc., Orlando (1987).Google Scholar
  20. 20.
    K. Mosbach, ed., “Methods in Enzymology: Immobilized Enzymes and Cells,” Part D, Volume 137, Academic Press Inc., Orlando (1988).Google Scholar
  21. 21.
    R. F. Taylor, ed., “Protein Immobilization: Fundamentals and Applications,” Marcel Dekker Inc., New York (1991).Google Scholar
  22. 22.
    J. Tampion and M. D. Tampion, “Immobilized Cells: Principles and Applications,” Cambridge University Press, Cambridge (1987).Google Scholar
  23. 23.
    G. G. Guilbault, “Analytical Uses of Immobilized Enzymes,” Marcel Dekker Inc., New York (1984).Google Scholar
  24. 24.
    B. Mattiasson, ed., “Immobilized Cells and Organelles,” Volume I, CRC Press, Inc., Boca Raton (1983).Google Scholar
  25. 25.
    B. Mattiasson, ed., “Immobilized Cells and Organelles,” Volume II, CRC Press, Inc., Boca Raton (1983).Google Scholar
  26. 26.
    I. Chibata, ed., “Immobilized Enzymes,” Wiley, New York (1978).Google Scholar
  27. 27.
    J. W. Parce, G. B. Sigal, K. M. Kercso, J. C. Owicki, The silicon microphysiometer: Detection of biological effects of chemical and biochemical agents by alterations of celluar metabolic rate, in: “Biosensor Technology Fundamentals and Applications,” R. P. Buck, W. E. Hatfield, M. Umana, and E. F. Bowden, eds., Marcel Dekker, Inc., New York (1990).Google Scholar
  28. 28.
    B. S. Jacobson and D. Branton, Plasma membrane: rapid isolation and exposure of the cytoplasmic surface by use of positively charged beads, Science 195:302 (1976).CrossRefGoogle Scholar
  29. 29.
    B. C Arkles, A. S. Miller, and W. S. Brinigar, Whole cell and cell organelle immobilization on siliceous surfaces, in: “Syliated Surfaces” D. E. Leyden and W. T. Collins, eds., Gorden and Breach, Inc. (1980).Google Scholar
  30. 30.
    B. A. Pethica, Microbial and cell adhesion, in: “Microbial Adhesion to Surfaces,” R. C W. Berkeley, J. M. Lynch, J. Melling, P. R. Rutter and B. Rutter, eds., Soc. Chem. Ind., London (1980).Google Scholar
  31. 31.
    E. Evans, Mechanics of cell deformation and cell-surface adhesion, in: “Physical Basis for Cell-Cell Adhesion,” P. Bongrand, ed., CRC Press, Boca Raton (1988).Google Scholar
  32. 32.
    J. D. Andrade, L. M. Smith, and D. E. Gregonis, The contact angle and interface energetics, in: “Surface and Interfacial Aspects of Biomedical Polymers,” J. Andrade, ed., Plenum Press, New York (1985).CrossRefGoogle Scholar
  33. 33.
    J. M. Schakenraad, H. J. Busscher, C. R. H. Wildevuur, and J. Arends, The influence of substratum surface free energy on growth and spreading of human fibroblasts in the presence or absence of serum proteins, J. Biomed. Mater. Res. 20:773 (1986).PubMedCrossRefGoogle Scholar
  34. 34.
    D. R. Absolom, L. A. Hawthorn, and G. Chang, Endothelialization of polymer surfaces, J. Biomed. Mater. Res. 22:271 (1988).PubMedCrossRefGoogle Scholar
  35. 35.
    S. A. Klotz, Role of hydrophobic interactions in microbial adhesion to plastics used in medical devices, in: “Microbial Cell Surface Hydrophobicity,” R. J. Doyle and M. Rosenberg, eds., American Society for Microbiology, Washington, DC (1990).Google Scholar
  36. 36.
    Y. Ito, Cell adhesion factor immobilized materials, in: “Synthesis of Biocomposite Materials,” Y. Imanishi, ed., CRC Press, Boca Raton, (1992).Google Scholar
  37. 37.
    T. A. Horbett and B. Schway, Correlations between mouse 3T3 cell spreading and serum fibronectin adsorption on glass and hydroxyethylmethacrylate-ethylmethacrylate copolymers,J. Biomed. Mater. Res. 22:763 (1988).PubMedCrossRefGoogle Scholar
  38. 38.
    E. Ruoslahti and M. D. Pierschbacher, New perspectives in cell adhesion: RGD and integrins, Science 238:491 (1987).PubMedCrossRefGoogle Scholar
  39. 39.
    F. Grinnell, Cellular adhesivienes and extracellular substrates, International Review of Cytology 53:65 (1978).PubMedCrossRefGoogle Scholar
  40. 40.
    K. M. Yamada, Cell surface interactions with extracellular materials, Ann. Rev. Biochem. 52:761 (1983).PubMedCrossRefGoogle Scholar
  41. 41.
    E. Ruoslahti and M. D. Pierschbacher, ARG-GLY-ASP a versatile cell recognition signal, Cell 44:517 (1986).PubMedCrossRefGoogle Scholar
  42. 42.
    R. Bar-Shavit, V. Sabbah, M. G. Lampugnani, P. C. Marchisio, J. W. Fenton II, I. Vlodavsky, and E. Dejena, ARG-GLY-ASPP sequence within thrombin promotes endothelial-cell adhesion, J. Cell Biol. 112(2):335 (1991).PubMedCrossRefGoogle Scholar
  43. 43.
    E. C. Tsilibary, L. A. Reger, A. M. Vogel, G. G. Koliaakos, S. S. Anderson, A. S. Charonis, J. N. Alegre, and L. T. Furcht, Identification of a multifunctional, cell-binding peptide sequence from the al(NCl) of type IV Collagen, J. Cell Biol. 111:1583 (1990).PubMedCrossRefGoogle Scholar
  44. 44.
    D. W. Barnes and J. Silnutzer, Isolation of human serum spreading factor, J. Biol. Chem. 258(20):12548 (1983).PubMedGoogle Scholar
  45. 45.
    R. M. Senior, G. L. Griffin, R. M. Mecham, D. S. Wrenn, K. U. Prasad, and D. W. Urry, Val-Gly-Val-Ala-Pro-Gly, a repeating peptide in elastin, is chemotactic for fibroblasts and monocytes, J. Cell Biol. 99:870 (1984).PubMedCrossRefGoogle Scholar
  46. 46.
    M. Hook, L. M. Switalski, T. Wadstrom, and M. Lindberg, Interactions of the pathogenic microorganisms with fibronectin, in: “Fibronectin,” D. Mosher, ed., Biology of Extracellular Matrix: A Series, Academic Press, New York (1989).Google Scholar
  47. 47.
    H. L. Thompson, P. D. Burbelo, B. Segui-Real, Y. Yamada, and D. D. Metcalfe, Laminin promotes mast cell attatchment, Immunology 143(7):2323 (1989).Google Scholar
  48. 48.
    H. L. Thompson, P. D. Burbelo, Y. Yamada, H. K. Kleinman, and D. D. Metcalfe, Identification of an amino acid sequence in the laminin A chaim mediating mast cell attatchment and spreading, Immunology 72:144 (1991).PubMedGoogle Scholar
  49. 49.
    J. Dastych, J. J. Costa, H. L. Thompson, and D. D. Metcalfe, Mast cell adhesion to fibronectin, Immunology 73:478 (1991).PubMedGoogle Scholar
  50. 50.
    H. K. Kleinman, F. B. Cannon, G. W. Laurie, J. R. Hassell, M. Aumailley, V. P. Terranova, and M. DuBois-Dalcq, Biological activities of laminin, J. Cell. Biochem. 27:317 (1985).PubMedCrossRefGoogle Scholar
  51. 51.
    J. Enenestein and L. T. Furcht, Epithelial and neural localization and heparin binding of the cell-substratum adhesion molecule, epinectin, J. Invest. Dermatol 91(1):34 (1988).CrossRefGoogle Scholar
  52. 52.
    K. S. Stenn, Epibolin: a protein of human plasma that supports epithelial cell movement, Proc. Natl. Acad. Sci. USA 78(11):6907 (1981).PubMedCrossRefGoogle Scholar
  53. 53.
    W. G. Carter, M. C. Ryan, and P. J. Gahr, A new cell-adhesion ligand for integrin- Alpha-3-Beta-l in epiithelial basement membranes, Cell 65:599 (1991).PubMedCrossRefGoogle Scholar
  54. 54.
    C. R. Ruegg, R. Chiquet-Ehrismann, and S. S. Alkan, Tenascin, an extracellular matrix protein, exerts immunodulatory activities, Proc. Natl. Acad. Sci. USA 86:7437 (1989).PubMedCrossRefGoogle Scholar
  55. 55.
    K. Tashiro, G. C Sephel, B. Weeks, M. Sasaki, G. R. Martin, H. K. Kleinman, Y. Yamada, and G. R. Martin, A synthetic peptide containing the IKVAV sequence from the A chain of laminin mediates cell attatchment, migration, and neurite outgrowth, J. Biol. Chem. 264:16174 (1989).PubMedGoogle Scholar
  56. 56.
    A. Oldberg, A. Franzen, and D. Heinegard, Cloning and sequence analysis of rat bone sialoprotein (osteopontin) cDNA reveals an Arg-Gly-Asp cell binding sequence, Pro. Natl. Acad. Sci. USA 83:8819 (1986).CrossRefGoogle Scholar
  57. 57.
    A. Oldberg, A. Franzen, and D. Heinegard, The primary structure of a cell-binding bone sialoprotein, J. Biol. Chem. 263(36):19430 (1988).PubMedGoogle Scholar
  58. 58.
    S. D. Wright, C3bi receptor (complement receptor type 3) recognizes a region of complement protein C3 containing the sequence of ARG-GLY-ASP, Natl. Acad. Sci. USA 84:1965 (1987).CrossRefGoogle Scholar
  59. 59.
    E. Bell, Tissue engineering, an overview: reconstituting tissue and organ equivalents for grafting and for use as model systems, J. Cellular Biochem. Supplement 16F:116 (1992).Google Scholar
  60. 60.
    A. Nicol, D. C. Gowda, and D. W. Urry, Cell adhesion and growth on synthetic elastomeric matrices containing ARG-GLY-ASP-SER, J. Biomed. Mater. Res. 26:293 (1992).CrossRefGoogle Scholar
  61. 61.
    S. P. Massia and J. A. Hubbell, Covalent surface immobilization of Arg-Gly-Asp-and Tyr-Ile-Gly-Ser-Arg-containing peptides to obtain well defined cell-adhesive substrates, Analytical Biochemistry 187:292 (1990).PubMedCrossRefGoogle Scholar
  62. 62.
    L. G. Cima, J. P. Vacanti, C. Vacanti, D. Ingber, D. Mooney, and R. Langer, Tissue engineering by cell transplantation using degradable polymer substrates, J. Biomech. Eng. 113:143 (1991).PubMedCrossRefGoogle Scholar
  63. 63.
    J. A. McDonald and R. P. Mecham, eds., “Receptors for Extracellular Matrix,” Academic Press, Inc., San Diego (1991).Google Scholar
  64. 64.
    J. Engel, E. Odermatt, A. Engel, J. Madri, H. Furthmayer, H. Rohde, and R. Timpl, Shapes, domain organizations and flexibility of laminin and fibronectin, two multifunctional proteins of the extracellular matrix, J. Mol. Biol. 150:97 (1981).PubMedCrossRefGoogle Scholar
  65. 65.
    D. R. Abramhamson, M. H. Irwin, P. L. St. John, M. A. Accavitti, L. W. Heck, and J. R. Couchman, Selective immunoreactivities of kidney basement membranes to monoclonal antibodies against laminin: localization of the end of the long arms to discrete microdomains, J. Cell Biol. 109:3477 (1989).CrossRefGoogle Scholar
  66. 66.
    R. L. Trelsted, Matrix macromolecules: spatial relationships in two dimensions, Ann. N.Y. Acad. Sci. 580:391 (1990).CrossRefGoogle Scholar
  67. 67.
    R. O. Hynes and K. M. Yamada, Fibronectins-multifunctional modular glycoproteins issue #2, J. Cell. Biol. 95:369 (1982).PubMedCrossRefGoogle Scholar
  68. 68.
    R. B. Kemp, Heat dissipation and metabolism in isolated animal cells and whole tissues/organs, in: “Thermal and Energetic Studies of Cellular Biological Systems,” A. M. James, ed., IOP Publishing Ltd., Bristol, Great Britain (1987).Google Scholar
  69. 69.
    G. Binnig and H. Rohrer, Scanning tunneling microscopy, Surface Sci. 126:236 (1983).CrossRefGoogle Scholar
  70. 70.
    J. A. Golovchenko, The tunneling microscope: a new look at the atomic world, Science 232:48 (1986).PubMedCrossRefGoogle Scholar
  71. 71.
    M. E. Welland and M. E. Taylor, in: “Modern Microscopies: Techniques and Applications,” P. J. Duke and A. G. Michette, eds., Plenum Press, New York, N.Y. (1990).Google Scholar
  72. 72.
    R. J. Behm, N. Garcia, and H. Rohrer, “Scanning Tunneling Microscopy and Related Methods,” Academic Publishers, Dordrecht, The Netherlands (1990).CrossRefGoogle Scholar
  73. 73.
    D. Sarid, “Scanning Force Microscopy: With Applications to Electric, Magnetic, and Atomic Forces,” Oxford University Press, New York, N.Y. (1991).Google Scholar
  74. 74.
    P. D. Yurencho, E. C. Tsilibary, A. S. Charonis, and H. Furthmayr, Laminin polymerzation in vitro: evidence for a two-step assembly with domain specificity, J. Biol. Chem. 260(12):7636 (1985).Google Scholar
  75. 75.
    P. D. Yurencho, Y. Cheng, and J. C. Schittny, Heparin modulation of laminin polymerzation, J. Biol. Chem. 265(7):3981 (1990).Google Scholar
  76. 76.
    Z. Wang, T. Hartmann, W. Baumiester, and R. Guckenberger, Proc. N.Y. Acad. Sei., USA 87:9343 (1990).CrossRefGoogle Scholar
  77. 77.
    R. E. Baier, Role of surface energy in thrombogenesis, Bull. N.Y. Acad. Med. 48(2):257 (1972).PubMedGoogle Scholar
  78. 78.
    E. P. Plueddemann, “Silicone Coupling Agents,” Plenum Press, New York (1991).Google Scholar
  79. 79.
    F. Grinnell, Fibronectin adsorption on material surfaces, in: “Blood in Contact with Natural and Artiifcial Surfaces,” E. Leonard, V. T. Turitto, and L. Vroman, eds., Ann. N.Y. Acad. Sci. 516:280 (1987).Google Scholar
  80. 80.
    K. Lewandowska, N. Balachander, C. N. Sukenik, and L. A. Culp, Modulation of fibronectin adhesive proteins for fibroblasts and neural cells by chemically derivatized substrata, J. Cell. Physiol 141:334 (1989).PubMedCrossRefGoogle Scholar
  81. 81.
    S. R. Snyder and H. S. White, Scanning tunneling microscopy, atomic force microscopy, and related techniques, Analytical Chemistry 64(12):116R (1992).CrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media New York 1992

Authors and Affiliations

  • Vincent B. Pizziconi
    • 1
  • Darren L. Page
    • 1
  1. 1.Department of Chemical, Bio & Materials EngineeringArizona State UniversityTempeUSA

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