Amorphous calcium carbonate (ACC) plays important roles in biomineralization, and the phosphoproteins extracted from biogenic stable ACC can induce and stabilize synthetic ACC in vitro. Here, mineralization of square-shaped ACC plates with micrometer-sized channels has been reported in the presence of the amphiphilic phosphoprotein casein. Casein can be assumed to take a key role during ACC plate formation, where it serves as an effective stabilization agent for ACC and assembles spherical ACC particles into ACC plates. The stabilizing effect of casein arises from the electrostatic attraction between phosphate groups as well as carbonate groups (especially the former) and the calcium ions, preventing the transformation from unstable ACC to the more stable crystalline phase of CaCO(3). The assembling effect of casein mainly comes from the hydrophobic interaction between casein molecules bound on CaCO(3) particle surface. The inclusion of casein in ACC plates revealed by the thermogavimetric analysis confirms the proposed stabilizing and assembling mechanism. The ability to fabricate such novel hierarchical structured ACC holds the promise for creating more complex micro- and nanostructured materials by use of biological proteins with special structure.
Phosphoproteins have specific and prominent influences on mediating the crystallization of calcium carbonate. In this research, a new kind of calcium carbonate crystal with a novel self-organized spiky dumbbell-like superstructure was synthesized in the presence of one typical phosphoprotein-casein. A complex self-assembly process for the formation of the hierarchical superstructures in the presence of casein has been proposed. The effects of the concentration of calcium ion, the reaction time, and temperature are investigated. The results indicate that phosphate groups of casein play important roles in directing growth and self-assembly of hierarchical superstructures. Our studies may contribute to the understanding of the specific role of phosphoprotein in the biomineralization process. We also believe that our studies will provide new insights into controlling the structure and morphology of minerals under easily attainable reaction conditions in the presence of phosphoprotein.
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