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.
An erratum to this chapter can be found at http://dx.doi.org/10.1007/978-94-007-3876-8_14
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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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Clarson, S.J., Gallardo, K., Patwardhan, S.V., Grazulis, L. (2012). On the Interactions of Proteins with Silicon-Based Materials. In: Owen, M., Dvornic, P. (eds) Silicone Surface Science. Advances in Silicon Science, vol 4. Springer, Dordrecht. https://doi.org/10.1007/978-94-007-3876-8_8
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