In the sea urchin embryo spicule, there exists a proteome of >200 proteins that are responsible for controlling the mineralization of the spicule and the formation of a fracture-resistant composite. In this report, using recombinant proteins, we identify that two protein components of the spicule, SM30B/C and SM50, are hydrogelators. Because of the presence of intrinsic disorder and aggregation-prone regions, these proteins assemble to form porous mesoscale hydrogel particles in solution. These hydrogel particles change their size, organization, and internal structure in response to pH and ions, particularly Ca(II), which indicates that these behave as ion-responsive or “smart” hydrogels. Using diffusion-or... More
In the sea urchin embryo spicule, there exists a proteome of >200 proteins that are responsible for controlling the mineralization of the spicule and the formation of a fracture-resistant composite. In this report, using recombinant proteins, we identify that two protein components of the spicule, SM30B/C and SM50, are hydrogelators. Because of the presence of intrinsic disorder and aggregation-prone regions, these proteins assemble to form porous mesoscale hydrogel particles in solution. These hydrogel particles change their size, organization, and internal structure in response to pH and ions, particularly Ca(II), which indicates that these behave as ion-responsive or “smart” hydrogels. Using diffusion-ordered spectroscopy NMR, we find that both hydrogels affect the diffusion of water, but only SM50 affects the diffusion of an anionic solute. Thus, the extracellular matrix of the spicule consists of several hydrogelator proteins which are responsive to solution conditions and can control the diffusion of water and solutes, and these proteins will serve as a model system for designing ion-responsive, composite, and smart hydrogels.
