Summary
The sol-gel process is a chemical technique for immobilizing biomolecules in an inorganic, transparent matrix. The dopant biomolecules reside in an interconnected mesoporous network and become part of the nanostructured architecture of the entire material. In this chapter, we review the sol-gel immobilization approach and discuss how it leads to the stabilization of a number of proteins against aggressive chemical and thermal environments. We also review the sensor applications of this material that result from having analyte molecules diffuse through the matrix and reach the immobilized biomolecule.
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References
Hench, L. L. and West, J. K. (1990) The sol-gel process. Chem. Rev. 90, 33–72.
Brinker, C. J., Keefer, K. D., Schaeffer, D. W., and Ashley, C. S. (1982) Sol-gel transition in simple silicates. J. Non-Cryst. Solids 48, 47–64.
Brinker, C. J. and Scherer, G. W. (1985) Sol-gel glass: gelation and gel structure. J. Non-Cryst. Solids 70, 301–322.
Brinker, C. J. and Scherer, G. W. (1990) The Physics and Chemistry of Sol-Gel Processing, Academic, San Diego.
Sakka, S. (1982) Gel method for making glass, in Treatise on Materials Science and Technology, vol. 22, (Herman, H. and Tomozawa, M., eds.), Academic, New York, pp. 129–167.
Rickus, J. L., Dunn, B., and Zink, J. I. (2002) Optically based sol-gel biosensor materials, in Optical Biosensors: Present and Future (Ligler, F. S. and Rowe-Taitt, C. A., eds.), Elsevier Science, Amsterdam, The Netherlands, pp. 427–456.
Braun, S., Rappoport, S., Zusman, R., Avnir, D., and Ottolenghi, M. (1990) Biochemically active sol-gel glasses—the trapping of enzymes. Mater. Lett. 10, 1–5.
Ellerby, L. M., Nishida, C. R., Nishida, F., Yamanaka, S. A., Dunn, B., Selverstone Valentine, J., and Zink, J. I. (1992) Encapsulation of proteins in transparent porous silicate-glasses prepared by the sol-gel method. Science 255, 1113–1115.
Avnir, D., Braun, S., Lev, O., and Ottolenghi, M. (1994) Enzymes and other proteins entrapped in sol-gel materials [review]. Chem. Mater. 6, 1605–1614.
Livage, J., Coradin, T., and Roux, C. (2001) Encapsulation of biomolecules in silica gels [review]. J. Phys. Condensed Matter 13, R673–R691.
Gill, I. (2001) Bio-doped nanocomposite polymers: sol-gel bioencapsulates [review]. Chem. Mater. 13, 3404–3421.
Zink, J. I., Valentine, J. S., and Dunn, B. (1994) Biomolecular materials based on sol-gel encapsulated proteins. N. J. Chem. 18, 1109–1115.
Chen, Q., Kenausis, G. L., and Heller, A. (1998) Stability of oxidases immobilized in silica gels. J. Am. Chem. Soc. 120, 4582–4585.
Heller, J. and Heller, A. (1998) Loss of activity or gain in stability of oxidases upon their immobilization in hydrated silica: significance of the electrostatic interactions of surface arginine residues at the entrances of the reaction channels. J. Am. Chem. Soc. 120, 4586–4590.
Lan, E. H., Dave, B. C., Fukuto, J. M., Dunn, B., Zink, J. I., and Valentine, J. S. (1999) Synthesis of sol-gel encapsulated heme proteins with chemical sensing properties. J. Mater. Chem. 9, 45–53.
Lan, E. H., Dunn, B., and Zink, J. I. (2000) Sol-gel encapsulated anti-trinitrotoluene antibodies in immunoassays for TNT. Chem. Mater. 12, 1874–1878.
Nguyen, D. T., Smit, M., Dunn, B., and Zink, J. I. (2002) Stabilization of creatine kinase encapsulated in silicate sol-gel materials and unusual temperature effects on its activity. Chem. Mater. 14, 4300–4306.
Miller, J. M., Dunn, B., Valentine, J. S., and Zink, J. I. (1996) Synthesis conditions for encapsulating cytochrome C and catalase in SiO2 sol-gel materials. J. Non-Cryst. Solids 202, 279–289.
Eggers, D. K. and Valentine, J. S. (2001) Molecular confinement influences protein structure and enhances thermal protein stability. Protein Sci. 10, 250–261.
Kawakami, K. and Yoshida, S. (1995) Sol-gel entrapment of lipase using a mixture of tetramethoxysilane and methyltrimethoxysilane as the alkoxide precursor—esterification activity in organic media. Biotechnol. Techniques 9, 701–704.
Shtelzer, S., Rappoport, S., Avnir, D., Ottolenghi, M., and Braun, S. (1992) Properties of trypsin and of acid-phosphatase immobilized in sol-gel glass matrices. Biotechnol. Appl. Biochem. 15, 227–235.
Eggers, D. K. and Valentine, J. S. (2001) Crowding and hydration effects on protein conformation: a study with sol-gel encapsulated proteins. J. Mol. Biol. 314, 911–922.
Schmid, F. X. (1990) Protein Structure: A Practical Approach, IRL Press, Oxford, UK.
Nayal, M., Hitz, B. C., and Honig, B. (1999) GRASS: a server for the graphical representation and analysis of structures. Protein Sci. 8, 676–679.
Rickus, J. L., Chang, P. L., Tobin, A. J., Zink, J. I., and Dunn, B. (2004) Photochemical coenzyme regeneration in an enzymatically active optical material. J. Phys. Chem. B. 108, 9325–9332.
Lehninger, A. L., Nelson, D. L., and Cox, M. M. (1993) Principles of Biochemistry, Worth Publishers, New York.
Maccraith, B. D., McDonagh, C., McEvoy, A. K., Butler, T., Okeeffe, G., and Murphy, V. (1997) Optical chemical sensors based on sol-gel materials—recent advances and critical issues. J. Sol-Gel Sci. Technol. 8, 1053–1061.
Maccraith, B. D., McDonagh, C. M., Okeeffe, G., McEvoy, A. K., Butler, T., and Sheridan, F. R. (1995) Sol-gel coatings for optical chemical sensors and biosensors. Sens. Actuators B Chem. 29, 51–57.
McDonagh, C., Bowe, P., Mongey, K., and MacCraith, B. D. (2002) Characterisation of porosity and sensor response times of sol-gel-derived thin films for oxygen sensor applications. J. Non-Cryst. Solids 306, 138–148.
Altstein, M., Aharonson, N., Segev, G., Ben-Aziz, O., Avnir, D., Turniansky, A., and Bronshtein, A. (2000) Sol-gel-based enzymatic assays and immunoassays for residue analysis. Italian J. Food Sci. 12, 191–206.
Bronshtein, A., Aharonson, N., Avnir, D., Turniansky, A., and Altstein, M. (1997) Sol-gel matrixes doped with atrazine antibodies—atrazine binding properties. Chem. Mater. 9, 2632–2639.
Doody, M. A., Baker, G. A., Pandey, S., and Bright, F. V. (2000) Affinity and mobility of polyclonal anti-dansyl antibodies sequestered within sol-gel-derived biogels. Chem. Mater. 12, 1142–1147.
Grant, S. A. and Glass, R. S. (1999) Sol-gel-based biosensor for use in stroke treatment. IEEE Trans. Biomed. Eng. 46, 1207–1211.
Jiang, D. C., Tang, J., Liu, B. H., Yang, P. Y., and Kong, J. L. (2003) Ultrathin alumina sol-gel-derived films: allowing direct detection of the liver fibrosis markers by capacitance measurement. Anal. Chem. 75, 4578–4584.
Jordan, J. D., Dunbar, R. A., and Bright, F. V. (1996) Aerosol-generated sol-gel-derived thin films as biosensing platforms. Anal. Chim. Acta 332, 83–91.
Roux, C., Livage, J., Farhati, K., and Monjour, L. (1997) Antibody-antigen reactions in porous sol-gel matrices. J. Sol-Gel Sci. Technol. 8, 663–666.
Shabat, D., Grynszpan, F., Saphier, S., Turniansky, A., Avnir, D., and Keinan, E. (1997) An efficient sol-gel reactor for antibody-catalyzed transformations. Chem. Mater. 9, 2258–2260.
Turniansky, A., Avnir, D., Bronshtein, A., Aharonson, N., and Altstein, M. (1996) Sol-Gel entrapment of monoclonal anti-atrazine antibodies. J. Sol-Gel Sci. Technol. 7, 135–143.
Vazquez-Lira, J. C., Camacho-Frias, E., Pena-Alvarez, A., and Vera-Avila, L. E. (2003) Preparation and characterization of a sol-gel immunosorbent doped with 2,4-D antibodies. Chem. Mater. 15, 154–161.
Wang, R., Narang, U., Prasad, P. N., and Bright, F. V. (1993) Affinity of antifluorescein antibodies encapsulated within a transparent sol-gel glass. Anal. Chem. 65, 2671–2675.
Zhou, J. C., Chuang, M. H., Lan, E. H., Dunn, B., Smith, S. M., and Gillman, P. L. (2004) Immunoassays for cortisol using antibody-doped sol-gel silica. J. Mater. Chem. 14, 2311–2316.
Ashkar, F. S. (1983) Radiobioassay, CRC Press, Boca Raton, FL.
Pesce, A. J. and Kaplan, L. A. (1987) Methods in Clinical Chemistry, C. V. Mosby, St. Louis, MO.
Acknowledgments
We greatly appreciate the contributions of Dr. Dorothy Nguyen, Dr. Jenna Rickus, Jing C. Zhou, James R. Lim, Maria H. Chuang, and Pauline Chang to the work described in this review. We also gratefully acknowledge support for this research from NSF (DMR 0103952 and DMR 0099862) and NASA (NAG9-1252). This work was also partially supported by the Center for Cell Mimetic Space Exploration, a NASA University Research, Engineering and Technology Institute, through award no. NCC 2-1364.
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Lan, E.H., Dunn, B., Zink, J.I. (2005). Nanostructured Systems for Biological Materials. In: Vo-Dinh, T. (eds) Protein Nanotechnology. Methods in Molecular Biology™, vol 300. Humana Press. https://doi.org/10.1385/1-59259-858-7:053
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DOI: https://doi.org/10.1385/1-59259-858-7:053
Publisher Name: Humana Press
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