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Biogenic and Synthetic Peptides with Oppositely Charged Amino Acids as Binding Sites for Mineralization

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Institute of Biomaterials and Biomolecular Systems (IBBS), Biobased Materials, University of Stuttgart, Pfaffenwaldring 57, 70569 Stuttgart, Germany
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Institute of Biomaterials and Biomolecular Systems (IBBS), Molecular Biology and Plant Virology, University of Stuttgart, Pfaffenwaldring 57, 70569 Stuttgart, Germany
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Projekthaus NanoBioMater, Allmandring 5B, 70569 Stuttgart, Germany
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Institute for Materials Science, Chair of Chemical Materials Synthesis, University of Stuttgart, Heisenbergstraße 3, 70569 Stuttgart, Germany
*
Author to whom correspondence should be addressed.
Academic Editor: Fabio Nudelman
Materials 2017, 10(2), 119; https://doi.org/10.3390/ma10020119
Received: 22 December 2016 / Revised: 18 January 2017 / Accepted: 24 January 2017 / Published: 28 January 2017
(This article belongs to the Special Issue Biological and Synthetic Organic–Inorganic Composite Materials)
Proteins regulate diverse biological processes by the specific interaction with, e.g., nucleic acids, proteins and inorganic molecules. The generation of inorganic hybrid materials, such as shell formation in mollusks, is a protein-controlled mineralization process. Moreover, inorganic-binding peptides are attractive for the bioinspired mineralization of non-natural inorganic functional materials for technical applications. However, it is still challenging to identify mineral-binding peptide motifs from biological systems as well as for technical systems. Here, three complementary approaches were combined to analyze protein motifs consisting of alternating positively and negatively charged amino acids: (i) the screening of natural biomineralization proteins; (ii) the selection of inorganic-binding peptides derived from phage display; and (iii) the mineralization of tobacco mosaic virus (TMV)-based templates. A respective peptide motif displayed on the TMV surface had a major impact on the SiO2 mineralization. In addition, similar motifs were found in zinc oxide- and zirconia-binding peptides indicating a general binding feature. The comparative analysis presented here raises new questions regarding whether or not there is a common design principle based on acidic and basic amino acids for peptides interacting with minerals. View Full-Text
Keywords: Inorganic-binding peptides; biomineralization; silicification; phage display Inorganic-binding peptides; biomineralization; silicification; phage display
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Lemloh, M.-L.; Altintoprak, K.; Wege, C.; Weiss, I.M.; Rothenstein, D. Biogenic and Synthetic Peptides with Oppositely Charged Amino Acids as Binding Sites for Mineralization. Materials 2017, 10, 119.

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