Nature and Nanotechnology

  • S. C. Goheen
  • K. A. Gaither
  • A. R. Rayburn
Conference paper
Part of the NATO Science Series book series (NAII, volume 128)


Scientists and engineers are rapidly developing techniques to produce nanostructures for various applications: nano-devices include electronic components, catalysts, and mechanical systems such as levers and motors. Biomedical applications include nanobots intended to function in various body fluids, pumps and drug delivery products, and implantable biosensors. Nature has been developing processes and products at the nano scale throughout the evolutionary process. There are several biochemical processes that involve energy-producing reactors, synthesis, and various mechanical processes. The relationships between the recent accomplishments of scientists and engineers in nanotechnology and natural processes are the subject of this paper. Numerous examples are provided in which the structure of a biological system at the nano-scale relates to some elaborate biological function. The structure and function for biological systems and biochemicals can in some cases be correlated to the structure and function of man-made nanomaterials. In this paper, we focus on proteins, but similar insight can be attained from other biomolecules and a wide variety of biological processes.


Protein Adsorption Pacific Northwest National Laboratory Biomedical Material Research Fibrinogen Adsorption Plasma Polymer Surface 
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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  1. 1.
    Menezes, A.J., V.J. Kapoor, V.K. Goel, B.D. Cameron, and J.-Y. Lu, Within a nanometer of your life. Mechanical Engineering, 2001. August: p. 54–58.Google Scholar
  2. 2.
    Edwards, J.V. and S.C. Goheen, Design, synthesis and affinity properties of biologically active peptide and protein conjugates of cotton cellulose. Recent Research developments in Bioconjugational Chemistry, 2002.1: p. 113–121.Google Scholar
  3. 3.
    Prisyazhnoy, V.S., M. Fusek, and Y.B. Alakhov, Synthesis of high capacity immunoaffinity sorbents with oriented immobilized immunoglobulins or their F ab’ fragments for isolation of proteins. J. of Chromatography, 1988. 424: p. 243–253.CrossRefGoogle Scholar
  4. 4.
    Edwards, J.V., S.L. Batiste, B.M. Gibbins, and S.C. Goheen, Synthesis and activity of NH2-and COOH-terminal elastase recognition sequences on cotton. Journal of Peptide Research, 1999. 54: p. 536–543.CrossRefGoogle Scholar
  5. 5.
    Roder, H., G. Elove, and S.W. Englander, Structural characterization of folding intermediates in cytochrome c by H-exchange labeling and proton NMR. Nature, 1988. 335: p. 700–704.CrossRefGoogle Scholar
  6. 6.
    Lu, X.M., K. Benedek, and B.L. Karger, Conformational effects in the high-performance liquid chromatography of proteins: Further studies of the reversed-phase chromatographic behavior of ribonuclease a. Journal of Chromatography, 1986. 359: p. 19–29.CrossRefGoogle Scholar
  7. 7.
    Regnier, F.E., High-Performance Liquid Chromatography of Biopolymers. Science, 1983. 222: p. 245–252.CrossRefGoogle Scholar
  8. 8.
    Goheen, S.C. and J.L. Hilsenbeck, High-performance ion-exchange chromatography and adsorption of plasma proteins. J. Chromatography A, 1998. 816(1): p. 89–96.CrossRefGoogle Scholar
  9. 9.
    Goheen, S.C. and B.M. Gibbins, Protein losses in ion exchange and hydrophobic interaction HPLC. Journal of Chromatography A, 2000. 890: p. 73–80.CrossRefGoogle Scholar
  10. 10.
    Goheen, S.C, The Influence of pH and Acetonitrile on the High Performance Size Exclusion Profile of Proteins. Journal of chromatography, 1988. 11: p. 1221–1228.Google Scholar
  11. 11.
    McPherson, T., A. Kidane, I. Szleifer, and K. Park, Prevention of protein adsorption by tethered poly (ethylene oxide) layers: Experiments and single-chain mean-field analysis. Langmuir, 1998. 14: p. 176–186.Google Scholar
  12. 12.
    McPherson, T.B., S.J. Lee, and K. Park, Analysis of the Prevention of Protein Adsorption by Steric Repulsion Theory, in Proteins at Interfaces II: Fundamentals and Applications, J.L. Brash, Editor. 1995, American Chemical Society: Washington, D. C. p. 395–404.Google Scholar
  13. 13.
    Tiselius, A., A new apparatus for electrophoretic analysis of colloidal mixtures. Trans. Faraday Soc., 1937. 33: p. 524–531.CrossRefGoogle Scholar
  14. 14.
    Malmsten, M., D. Muller, and B. Lassen, Sequential adsorption of human serum albumin(HSA) Immunoglobulin G and Fibrinogen at HMDSO Plasma polymer surfaces. Journal of Colloid and Interface Science, 1997: p. 88–95.Google Scholar
  15. 15.
    Herbold, C.W., J.H. Miller, and S.C. Goheen, Cytochrome c unfolding on an anionic surface. Journal of Chromatography A, 1999. 863: p. 137–146.CrossRefGoogle Scholar
  16. 16.
    Goheen, S.C, B.M. Gibbins, J.L. Hilsenbeck, C.W. Herbold, and J.V. Edwards. Adsorption and surface-mediated unfolding of proteins, in National ACS Meeting. 1999. New Orleans, Louisiana.Google Scholar
  17. 17.
    Volger, E.A., J.C. Graper, G.R. Harper, H.W. Sugg, L.M. Lander, and W.J. Brittain, Contact activation of the plasma coagulation cascade. I. Coagulant surface chemistry and energy. Journal of Biomedical Materials Research, 1995. 29: p. 1005–1016.CrossRefGoogle Scholar
  18. 18.
    Vroman, L., What factors determine thrombogenicity”. Bull. N.Y. Acad. Med., 1972. 48: p. 302–310.Google Scholar
  19. 19.
    Horbett, T.A., Mass-action effects on competitive adsorption of fibrinogen from hemoglobin-solutions and from plasma. Thromb. Haemostas, 1984. 51(2): p. 174–181.Google Scholar
  20. 20.
    Slack, S.M. and T.A. Horbett, The Vroman Effect, in Proteins at Interfaces II. 1995. p. 112–128.CrossRefGoogle Scholar
  21. 21.
    Brash, J.L., C.F. Scott, P.T. Hove, P. Wojciechowski, and R.W. Colman, Mechanism of transient adsorption of fibrinogen from plasma to solid surfaces: Role of the contact and fibrinolytic systems. Blood, 1988. 71: p. 932–939.Google Scholar
  22. 22.
    Ryu, G.H., J. Kim, Z. Ruggeri, S.H. Han, J.H. Kim, and B.G. Min, Effect of Shear Stress on Fibrinogen Adsorption and Its Conformational Change. ASAIO Journal, 1995. 41: p. M384–M388.CrossRefGoogle Scholar
  23. 23.
    Shiba, E., J.N. Lindon, L. Kushner, M. Kloczewiak, J. Hawiger, G. Matsueda, B. Kudryk, and E.W. Salzman, Conformational changes in fibrinogen adsorbed on polymer surfaces detected by polyclonal and monoclonal antibodies, in Fibrinogen 3: Biochemistry, Biological Functions, Gene Regulation and Expression: Proceedings of the International Fibriongen Workshop, Mulwaukee, Wisconsin, 13-15 June 1988., J.P. DiOrio, Editor. 1988, Excerpta Medica: New York. p. 239–244.Google Scholar
  24. 24.
    Chinn, J.A., J. Richard E. Phillips, K.R. Lew, and T.A. Horbett, Tenacious Binding of fibrinogen and albumin to pyrolite carbon and biomer. Journal of Colloid and Interface Science, 1996. 184: p. 11–19.CrossRefGoogle Scholar
  25. 25.
    Grunkemeier, J.M. and T.A. Horbett, Fibrinogen adsorption to receptor-like biomaterials made by pre-adsorbing peptides to polystyrene substrates. Journal of Molecular Recognition, 1996. 9: p. 247–257.CrossRefGoogle Scholar
  26. 26.
    Tsai, W.-B., J.M. Grunkemeier, and T.A. Horbett, Human plasma fibrinogen adsorption and platelet adhesion to polystyrene. Journal of Biomedical Materials Research, 1999. 44: p. 130–139.CrossRefGoogle Scholar
  27. 27.
    Horbett, T.A. and K.R. Lew, Residence time effects on monoclonal antibody binding to adsorbed fibrinogen. Journal of Biomaterials Science Polymer Edition, 1994. 6(1): p. 15–33.CrossRefGoogle Scholar
  28. 28.
    Grunze, M., P. Harder, and R. Dahint. Adhesion of proteins on self-assembled organic model surfaces, in The 20th Annual Meeting of the Adhesion Society. 1997. Hilhar Head Island, South Carolina.Google Scholar
  29. 29.
    Tang, L., Mechanisms of fibrinogen domains: biomaterial interactions. Journal of Biomaterials Science: Polymer Edition, 1998. 9(12): p. 1257–1266.CrossRefGoogle Scholar
  30. 30.
    Whitlock, P.W., S.J. Clarson, and G.S. Retzinger, Fibrinogen adsorbs from aqueous media to microscopic droplets of poly(dimethylsiloxane) and remains coagulable. Journal of Biomedical Materials Research, 1999. 45: p. 55–61.CrossRefGoogle Scholar
  31. 31.
    Balasubramanian, V., N.K. Grusin, R.W. Bucher, V.T. Turitto, and S.M. Slack, Residence-time dependent changes in fibrinogen adsorbed to polymeric biomaterials. Journal of Biomedical Materials Research, 1999. 44(3): p. 253–260.CrossRefGoogle Scholar
  32. 32.
    Bohnert, J.L. and T.A. Horbett, Changes in adsorbed fibrinogen and albumin interactions with polymers indicated by decreases in detergent elutability. Journal of Colloid and Interface Science, 1986. 111(2): p. 363–377.CrossRefGoogle Scholar
  33. 33.
    Fabrizium-Homan, D.J. and S.L. Cooper, Competitive adsorption of vitronectin with albumin, fibrinogen, and fibronectin on polymeric biomaterials. Journal of Biomedical Materials Research, 1991. 25: p. 953–971.CrossRefGoogle Scholar
  34. 34.
    Chan, B. and J.L. Brash, Conformational change in fibrinogen desorbed from glass surface. Journal of Colloid and Interface Science, 1981. 84: p. 263–265.CrossRefGoogle Scholar
  35. 35.
    Zembala, M., J.C. Voegel, and P. Schaaf, Elution process of adsorbed fibrinogen by SDS: competition between removal and anchoring. Langmuir, 1998. 14: p. 2167–2173.Google Scholar
  36. 36.
    Ortega-Vinuesa, J.L., P. Tengvall, and I. Lundstrom, Aggregation of HSA, IgG and fibrinogen on methlyated silicon surfaces. Journal of Colloid and Interface Science, 1998: p. 228–239.Google Scholar
  37. 37.
    Lin, J.-C. and S.L. Cooper, In vitro fibrinogen adsorption from various dilutions of human blood plasma on grow discharge modified polythylene. Journal of Colloid and Interface Science, 1996: p. 315–325.Google Scholar
  38. 38.
    Furie, B. and B.C. Furie, The molecular basis of blood coagulation. Cell, 1988. 53: p. 505–518.CrossRefGoogle Scholar
  39. 39.
    Seigel, R.R., P. Harder, R. Dahint, M. Grunze, F. Josse, M. Mrksich, and G. Whitesides, On-Line Detection of Nonspecific Protein Adsorption at Artificial Surfaces. Analytical Chemistry, 1997. 69(16): p. 3321–3328.CrossRefGoogle Scholar
  40. 40.
    Chapman, R.G., E. Ostuni, S. Takayama, R.E. Holmlin, L. Yan, and G.M. Whitesides, Surveying for surfaces that resist the adsorption of proteins. Journal of the American Chemical Society, 2000. 122(34): p. 8303–8304.CrossRefGoogle Scholar
  41. 41.
    Prime, K.L. and G.M. Whitesides, Adsorption of proteins onto surfaces containing end-attached oligo(ethylene oxide): a model system using self-assembled monolayers. J. Am. Chem. Soc., 1993. 115: p. 10714–10721.CrossRefGoogle Scholar
  42. 42.
    Wirth, M.J., R.W.P. Fairbank, and H.O. Fatunmbi, Mixed self-assembled monolayers in chemical separations. Science, 1997. 275: p. 44–47.CrossRefGoogle Scholar
  43. 43.
    Wood, L.L., S.S. Cheng, P.l. Edmiston, and S.S. Saavedra, Molecular orientation distributions in protein films. II. Site-directed immobilization of yeast cytochrome c on thiol-capped, self-assembled monolayers. Journal of the American Chemical Society, 1997. 119: p. 571–576.CrossRefGoogle Scholar
  44. 44.
    Ratnoff, O.D. and H. Saito, Coagulation factors and the role of surface in their activation, in Annals of the New York Academy of Sciences, E.F. Leonard, Editor. 1977, New York Academy of Sciences: New York. p. 283.Google Scholar
  45. 45.
    Hess, H. and V. Vogel, Molecular shuttles based on motor proteins: active transport in synthetic environments. Reviews in Molecular Biotechnology, 2001. 82: p. 67–85.CrossRefGoogle Scholar
  46. 46.
    Luna, E.J. and A.L. Hitt, Cytoskeleton-Plasma Membrane interactions. Science, 1992. 258: p. 955–964.CrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media Dordrecht 2003

Authors and Affiliations

  • S. C. Goheen
    • 1
  • K. A. Gaither
    • 1
  • A. R. Rayburn
    • 1
  1. 1.Pacific Northwest National LaboratoryRichlandUSA

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