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Laying out ground rules for protein-aided nanofabrication: ZnO synthesis at 70°C as a case study

  1. Sathana Kitayaporn,
  2. Weibin Zhou,
  3. Daniel T. Schwartz*,
  4. François Baneyx*

Article first published online: 24 FEB 2012

DOI: 10.1002/bit.24466

Issue

Biotechnology and Bioengineering

Biotechnology and Bioengineering

Volume 109, Issue 8, pages 1912–1918, August 2012

Additional Information

How to Cite

Kitayaporn, S., Zhou, W., Schwartz, D. T. and Baneyx, F. (2012), Laying out ground rules for protein-aided nanofabrication: ZnO synthesis at 70°C as a case study. Biotechnol. Bioeng., 109: 1912–1918. doi: 10.1002/bit.24466

Author Information

  1. Department of Chemical Engineering, Box 351750, University of Washington, Seattle, Washington 98195-1750; telephone: 206-685-4815 (D.T.S.)/206-685-7659 (F.B.); fax: 206-685-3451

*Department of Chemical Engineering, Box 351750, University of Washington, Seattle, Washington 98195-1750; telephone: 206-685-4815 (D.T.S.)/206-685-7659 (F.B.); fax: 206-685-3451.

Publication History

  1. Issue published online: 18 JUN 2012
  2. Article first published online: 24 FEB 2012
  3. Accepted manuscript online: 14 FEB 2012 01:25PM EST
  4. Manuscript Accepted: 1 FEB 2012
  5. Manuscript Revised: 27 JAN 2012
  6. Manuscript Received: 6 NOV 2011

Funded by

  • National Science Foundation (NSF). Grant Numbers: CMMI-0709131, DMR-0520567

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Keywords:

  • molecular biomimetics;
  • bionanotechnology;
  • solid-binding peptides;
  • inorganic-binding peptides

Abstract

Designer proteins that incorporate solid-binding peptides hold promise to control the nucleation, growth, morphology, and assembly of inorganic phases under mild conditions of temperature and pressure. However, protein-aided nanofabrication remains more art than science and some materials can only be synthesized at temperatures that cause most mesophilic proteins to unfold. Using zinc oxide (ZnO) synthesis at 70°C as case study, we show here that seemingly unimportant variables, such as the carry-over concentration of Tris buffer and the “empty” host protein scaffold can exert a significant influence on materials morphology. We also show that, once well-controlled conditions are established, thermodynamic predictions and adsorption isotherms are powerful tools to understand how various ZnO-binding sequence inserted within the thermostable framework of Escherichia coli thioredoxin A (TrxA) affect inorganic morphogenesis. Biotechnol. Bioeng. 2012; 109:1912–1918. © 2012 Wiley Periodicals, Inc.

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