Diatom Mimics: Directing the Formation of Biosilica Nanoparticles by Controlled Folding of Lysine-Leucine Peptides

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  • Joe E. Baio, School of Chemical, Biological, and Environmental Engineering, Oregon State University , Corvallis, Oregon 97331, United States.
  • ,
  • Ariel Zane, University of Washington, Seattle, WA
  • ,
  • Vance Jaeger, University of Washington, Seattle, WA
  • ,
  • Adrienne M Roehrich, University of Washington, Seattle, WA
  • ,
  • Helmut Lutz, Max-Planck Institute for Polymer Research, Mainz
  • ,
  • Jim Pfaendtner, University of Washington, Seattle, WA
  • ,
  • Gary P Drobny, University of Washington, Seattle, WA
  • ,
  • Tobias Weidner

Silaffins, long chain polyamines, and other biomolecules found in diatoms are involved in the assembly of a large number of silica nanostructures under mild, ambient conditions. Nanofabrication researchers have sought to mimic the diatom's biosilica production capabilities by engineering proteins to resemble aspects of naturally occurring biomolecules. Such mimics can produce monodisperse biosilica nanospheres, but in vitro production of the variety of intricate biosilica nanostructures that compose the diatom frustule is not yet possible. In this study we demonstrate how LK peptides, composed solely of lysine (K) and leucine (L) amino acids arranged with varying hydrophobic periodicities, initiate the formation of different biosilica nanostructures in vitro. When L and K residues are arranged with a periodicity of 3.5 the α-helical form of the LK peptide produces monodisperse biosilica nanospheres. However, when the LK periodicity is changed to 3.0, corresponding to a 310 helix, the morphology of the nanoparticles changes to elongated rod-like structures. β-strand LK peptides with a periodicity of 2.0 induce wire-like silica morphologies. This study illustrates how the morphology of biosilica can be changed simply by varying the periodicity of polar and nonpolar amino acids.

TidsskriftJournal of the American Chemical Society
Sider (fra-til)15134-15137
Antal sider4
StatusUdgivet - 2014
Eksternt udgivetJa

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