Calcium-Induced Molecular Rearrangement of Peptide Folds Enables Biomineralization of Vaterite Calcium Carbonate

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  • Hao Lu, Max Planck Institute for Polymer Research
  • ,
  • Helmut Lutz, Max Planck Institute for Polymer Research
  • ,
  • Steven J. Roeters
  • Matthew A. Hood, Max Planck Institute for Polymer Research
  • ,
  • Arne Schäfer, Max Planck Institute for Polymer Research
  • ,
  • Rafael MunÌoz-Espí, Max Planck Institute for Polymer Research, Universitat Politècnica de València
  • ,
  • Rüdiger Berger, Max Planck Institute for Polymer Research
  • ,
  • Mischa Bonn, Max Planck Institute for Polymer Research
  • ,
  • Tobias Weidner

Proteins can control mineralization of CaCO3 by selectively triggering the growth of calcite, aragonite or vaterite phases. The templating of CaCO3 by proteins must occur predominantly at the protein/CaCO3 interface, yet molecular-level insights into the interface during active mineralization have been lacking. Here, we investigate the role of peptide folding and structural flexibility on the mineralization of CaCO3. We study two amphiphilic peptides based on glutamic acid and leucine with β-sheet and α-helical structures. Though both sequences lead to vaterite structures, the β-sheets yield free-standing vaterite nanosheet with superior stability and purity. Surface-spectroscopy and molecular dynamics simulations reveal that reciprocal structuring of calcium ions and peptides lead to the effective synthesis of vaterite by mimicry of the (001) crystal plane.

OriginalsprogEngelsk
TidsskriftJournal of the American Chemical Society
Vol/bind140
Nummer8
Sider (fra-til)2793-2796
Antal sider4
ISSN0002-7863
DOI
StatusUdgivet - 28 feb. 2018

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