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Proteins Encapsulated in Porous Sol-Gels: Biomolecules as Pore Structure Templates

Published online by Cambridge University Press:  10 February 2011

B. C. Dave
Affiliation:
Deparment of Materials Science and Engineering, University of California, Los Angeles, CA 90095 Department of Chemistry and Biochemistry, University of California, Los Angeles, CA 90095.
B. Dunn
Affiliation:
Deparment of Materials Science and Engineering, University of California, Los Angeles, CA 90095
J. S. Valentine
Affiliation:
Department of Chemistry and Biochemistry, University of California, Los Angeles, CA 90095.
J. I. Zink
Affiliation:
Department of Chemistry and Biochemistry, University of California, Los Angeles, CA 90095.
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Abstract

Porous inorganic SiO2 glasses obtained by the sol-gel route represent a unique matrix for encapsulation of biomolecules wherein the pores act as enclosures for high molecular weight proteins. These hybrid materials are characterized by a pore-biomolecule interface between the pore walls and the protein surface. As a specific model protein, cytochrome c (cyt c) is used to elucidate the nature of physical and chemical interactions between the pores of the matrix and the protein. Evidence from optical absorption, and resonance Raman (RR) spectroscopy methods indicates that the dopant protein alters the structural features of the pore walls. The optical and vibrational measurements strongly suggest that the pores that contain the trapped protein undergo little or no structural change during aging and drying as compared to protein-free pores. Vibrational RR analysis of the trapped cyt c also suggests that the protein resides in a pore where the pore dimensions conform to the shape of the protein. The results indicate that noncovalent interactions between the surface of the protein and the pore walls govern the dynamics of pore formation during gelation and individual biomolecules act as structural templates to design local pore structure.

Type
Research Article
Copyright
Copyright © Materials Research Society 1996

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References

1. Dave, B. C., Dunn, B., Valentine, J. S., and Zink, J. I., Anal. Chem. 66, 1120A (1994).CrossRefGoogle Scholar
2. Salemme, F. R., Ann. Rev. Biochem.46, pp. 299329 (1977).CrossRefGoogle Scholar
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4. Ellerby, L. M., Nishida, C. R., Nishida, F., Yamanaka, S. A., Dunn, B., Valentine, J. S., Zink, J. I., Science 255, 1113 (1992).CrossRefGoogle Scholar
5. Cartling, B. in Biological Applications of Raman Spectroscopy. Vol 3., John Wiley, New York, 1988, pp. 217248.Google Scholar

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