Lattice Shrinkage by Incorporation of Recombinant Starmaker‐Like Protein within Bioinspired Calcium Carbonate Crystals. Issue 55 (12th August 2019)

• Record Type: Journal Article
• Authors: Różycka, Mirosława; Coronado, Ismael; Brach, Katarzyna; Olesiak‐Bańska, Joanna; Samoć, Marek; Zarębski, Mirosław; Dobrucki, Jerzy; Ptak, Maciej; Weber, Eva; Polishchuk, Iryna; Pokroy, Boaz; Stolarski, Jarosław; Ożyhar, Andrzej
• Is Part Of: Chemistry. Volume 25:Issue 55(2019)
• Page Start: 12740
• Page End: 12750
• Publication Date: 2019-08-12
• Subjects: biominerals -- calcium -- crystal growth -- proteins -- X-ray diffraction; Chemistry -- Periodicals; 540
• DOI: 10.1002/chem.201902157
• Languages: English
• ISSNs: 0947-6539

Abstract

Abstract: 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. Abstract : Controlled growth : The starmaker‐like (Stm‐l) protein promotes calcium carbonate nucleation and anisotropic tailoring of crystal morphology. Intracrystalline incorporation of protein results in shrinkage of the crystal lattice volume (see figure). The ring pattern, which is composed of a protein‐enriched region flanked by protein‐depleted regions, is a result of both the Ostwald‐like ripening process and intrinsic properties of Stm‐l.