
Abstract
With their unique ability for substrate recognition and their sequence-specific self-assembly properties, peptides play an important role in controlling the mineralization of inorganic materials in natural systems and in controlling the assembly of soft materials into complex structures required for biological functions. Here we report the use of an engineered heptapeptide that can differentiate between the crystalline anhydrous polymorphs of calcium carbonate. This peptide contains the positively charged amino acid arginine as well as proline rather than the prototypical negatively charged aspartate or glutamate units. Its affinity to vaterite compared to aragonite was demonstrated by fluorescence microscopy using biotinylated peptides. Crystallization experiments in the presence of the vaterite-affine peptide afforded only vaterite, whereas a mutant peptide, where a proline residue was replaced by glycine, exclusively leads to the formation of calcite.
Item Type: | Journal article |
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Form of publication: | Publisher's Version |
Faculties: | Chemistry and Pharmacy |
Subjects: | 500 Science > 540 Chemistry |
URN: | urn:nbn:de:bvb:19-epub-22641-9 |
ISSN: | 0959-9428 |
Alliance/National Licence: | This publication is with permission of the rights owner freely accessible due to an Alliance licence and a national licence (funded by the DFG, German Research Foundation) respectively. |
Annotation: | First publ. online. Print publ. June 2014 |
Language: | English |
Item ID: | 22641 |
Date Deposited: | 03. Feb 2015, 07:53 |
Last Modified: | 04. Nov 2020, 13:03 |