Hierarchical architecture of sponge spicules: biocatalytic and structure-directing activity of silicatein proteins as model for bioinspired applications.

Since the first description of the silicateins, a group of enzymes that mediate the formation of the amorphous, hydrated biosilica of the skeleton of the siliceous sponges, much progress has been achieved in the understanding of this biomineralization process. These discoveries include, beside the proof of the enzymatic nature of the sponge biosilica formation, the dual property of the enzyme, to act both as a structure-forming and structure-guiding protein, and the demonstration that the initial product of silicatein is a soft, gel-like material that has to undergo a maturation process during which it achieves its favorable physical-chemical properties allowing the development of various technological or medical applications. This process comprises the hardening of the material by the removal of water and ions, its cast-molding to specific morphologies, as well as the fusion of the biosilica nanoparticles through a biosintering mechanism. The discovery that the enzymatically formed biosilica is morphogenetically active and printable also opens new applications in rapid prototyping and three-dimensional bioprinting of customized scaffolds/implants for biomedical use.