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On the Interactions of Proteins with Silicon-Based Materials

  • Stephen J. ClarsonEmail author
  • Kathy Gallardo
  • Siddharth V. Patwardhan
  • Larry Grazulis
Part of the Advances in Silicon Science book series (ADSS, volume 4)

Abstract

In this chapter we describe silica precipitation using unmodified synthetic R5 polypeptide—a nineteen amino acid sequence corresponding to the homologous repeating sequence in silaffin-1A protein extracted from diatom C. fusiformis. The particle formation was investigated using modern materials characterization methods, namely AFM, SEM and EDS. It was found that silica particles of sizes ∼150–200 nm were produced and that they formed aggregates. Furthermore, we propose that the R5 polypeptide self-organizes in solution and catalyzes and scaffolds the silica formation in vitro. We believe that silaffin proteins and other proteins facilitating silica formation in vivo behave in a similar fashion and this may provide insights into the role of proteins in biosilicification.

Keywords

Biomineralization Biosilicification Biosilica Proteins Silicatein Silaffin-1A catalysis of silica particles formation 

Notes

Acknowledgements

We thank Dr. Srinivas Subramaniam (CME, UC) for help with the SEM analysis. The financial support for the work described in this chapter was kindly provided by DAGSI.

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Copyright information

© Springer Science+Business Media Dordrecht 2012

Authors and Affiliations

  • Stephen J. Clarson
    • 1
    Email author
  • Kathy Gallardo
    • 1
  • Siddharth V. Patwardhan
    • 2
  • Larry Grazulis
    • 3
  1. 1.Department of Chemical and Materials Engineering and the Polymer Research CenterUniversity of CincinnatiCincinnatiUSA
  2. 2.Department of Chemical and Process EngineeringUniversity of StrathclydeGlasgowUK
  3. 3.University of Dayton Research InstituteDaytonUSA

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