Aragonite-Associated Mollusk Shell Protein Aggregates To Form Mesoscale "Smart" Hydrogels.

In the mollusk shell there exists a framework silk fibroin-polysaccharide hydrogel coating around nacre aragonite tablets， and this coating facilitates the synthesis and organization of mineral nanoparticles into mesocrystals. In this report， we identify that a protein component of this coating， n16.3， is a hydrogelator. Due to the presence of intrinsic disorder， aggregation-prone regions， and nearly equal balance of anionic and cationic side chains， this protein assembles to form porous mesoscale hydrogel particles in solution and on mica surfaces. These hydrogel particles change their dimensionality， organization， and internal structure in response to pH and ions， particularly Ca(II)， which indicates that these behave as ion-responsive or "smart" hydrogels. Thus， in addition to silk fibroins， the gel phase of the mollusk shell nacre framework layer may actually consist of several framework hydrogelator proteins， such as n16.3， which can promote mineral nanoparticle organization and assembly during the nacre biomineralization process and also serve as a model system for designing ion-responsive， composite， and smart hydrogels.