Modulation of Crystal Growth by the Terminal Sequences of the Prismatic-Associated Asprich Protein
| Autor: | Christine A. Orme, John Spencer Evans, Jennifer L. Giocondi, Katya Delak |
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| Rok vydání: | 2008 |
| Předmět: | |
| Zdroj: | Crystal Growth & Design. 8:4481-4486 |
| ISSN: | 1528-7505 1528-7483 |
| DOI: | 10.1021/cg8004294 |
| Popis: | The formation of calcite in the mollusk shell prismatic layer requires the participation of various proteins. Recent studies indicate that the prismatic-associated protein superfamily, Asprich, is capable of in vitro stabilization of amorphous calcium carbonate (ACC), a precursor phase of prismatic calcite. To learn more about the molecular behavior of Asprich, we performed experiments on two highly conserved sequences derived from Asprich: Fragment-1, a 48 AA N-terminal cationic−anionic sequence, and Fragment-2, a previously characterized 42 C-terminal AA anionic sequence. SEM analyses reveal that Fragment-1 induces polycrystalline, radial aggregate assemblies of calcite, with evidence of surface porosities. AFM flow cell experiments demonstrate that Fragment-1 is multifunctional and its mineralization behavior is qualitatively similar to that reported for Fragment-2 except for hillock step kinetics. Surprisingly, when Fragment-1 and Fragment-2 are present together within the same assay, we observe phase... |
| Databáze: | OpenAIRE |
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