Chapter 16. Constrained Metal Oxide Mineralization: Lessons from Ferritin Applied to other Protein Cage Architectures

  1. Prof. Dr. Edmund Bäuerlein
  1. Mark A. Allen,
  2. M. Matthew Prissel,
  3. Mark J. Young and
  4. Trevor Douglas

Published Online: 20 MAR 2008

DOI: 10.1002/9783527619443.ch40

Handbook of Biomineralization: Biological Aspects and Structure Formation

Handbook of Biomineralization: Biological Aspects and Structure Formation

How to Cite

Allen, M. A., Prissel, M. M., Young, M. J. and Douglas, T. (2007) Constrained Metal Oxide Mineralization: Lessons from Ferritin Applied to other Protein Cage Architectures, in Handbook of Biomineralization: Biological Aspects and Structure Formation (ed E. Bäuerlein), Wiley-VCH Verlag GmbH, Weinheim, Germany. doi: 10.1002/9783527619443.ch40

Editor Information

  1. Max-Planck-Institute for Biochemistry, Department of Membrane Biochemistry, Am Klopferspitz 18 A, 82152 Planegg, Germany

Publication History

  1. Published Online: 20 MAR 2008
  2. Published Print: 25 MAY 2007

ISBN Information

Print ISBN: 9783527316410

Online ISBN: 9783527619443

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Keywords:

  • biomineralization;
  • biomimetic synthesis;
  • ferritin;
  • virus;
  • cowpea chlorotic mottle virus (CCMV);
  • protein cage;
  • dps;
  • heat shock protein

Summary

The process of biomineralization is characterized by control over mineral morphology, phase, orientation, and size. Spherical protein cages, similar to ferritin, that present an electrostatically distinct interior and exterior surface serve as model systems for biomineralization and biomimetic templated materials synthesis and encapsulation. Ferritin, ferritin-like proteins, and spherical viruses can serve as nano-containers that direct mineralization, which isolates stable particles inside a protein cage. The mineralization of metal oxide materials is dominated by the electrostatic characteristics of the interior of the protein cage, leading to the development of a model for biomimetic synthesis. The electrostatic model has been described using the Gouy-Chapman theory of charged interfaces to determine the electrostatic surface potential of the interior of the protein cage and to determine the effect that these nucleation sites have on incoming ions and forming the mineral core. This electrostatic model can be probed by genetic modification of the protein cages. The plant virus, Cowpea chlorotic mottle virus, has a positively charged interior surface for condensation and packaging of viral nucleic acid. Using site-directed mutagenesis, the positive charges can be altered to negatively charged glutamic acid residues and thus form a ferritin-like protein capable of mineralizing a range of transition-metal oxides.