期刊
CHEMISTRY-A EUROPEAN JOURNAL
卷 25, 期 55, 页码 12740-12750出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/chem.201902157
关键词
biominerals; calcium; crystal growth; proteins; X-ray diffraction
资金
- National Science Centre grant [UMO-2015/19/B/ST10/02148]
- Polish Ministry of Science and Higher Education for the Faculty of Chemistry of Wroclaw University of Science and Technology
The biological mediation of mineral formation (biomineralization) is realized through diverse organic macromolecules that guide this process in a spatial and temporal manner. Although the role of these molecules in biomineralization is being gradually revealed, the molecular basis of their regulatory function is still poorly understood. In this study, the incorporation and distribution of the model intrinsically disordered starmaker-like (Stm-l) protein, which is active in fish otoliths biomineralization, within calcium carbonate crystals, is revealed. Stm-l promotes crystal nucleation and anisotropic tailoring of crystal morphology. Intracrystalline incorporation of Stm-l protein unexpectedly results in shrinkage (and not expansion, as commonly described in biomineral and bioinspired crystals) of the crystal lattice volume, which is described herein, for the first time, for bioinspired mineralization. A ring pattern was observed in crystals grown for 48 h; this was composed of a protein-enriched region flanked by protein-depleted regions. It can be explained as a result of the Ostwald-like ripening process and intrinsic properties of Stm-l, and bears some analogy to the daily growth layers of the otolith.
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