Infiltration of Silica Inside Fibrillar Collagen

Diatoms frustules are created under the control of biomolecules (silaffins, silacidins and long-chain polyamines) at close to physiologic conditions.[1–4] The mechanism of biosilica formation was traditionally based on the ability of zwitterionic water-soluble proteins to create macromolecular assemblies for silica polymerization.[5–7] Recent discoveries of water-insoluble collagen matrices within certain sponge biosilica spicules[8], chitin-based scaffolds in sponge and diatom biosilica formations[9,10], as well as cingulins within diatom girdle bands[4], revive the use of insoluble biomimetic organic templates for morphogenesis of non-porous silica structures. The use of fibrillar collagen as templates for biosilica synthesis was unsuccessful in the past as only extrafibrillar silica deposition was observed.[11,12] Intrafibrillar mineralization of collagen has important implications from a biophysical perspective.[13] Here, we report a collagen biosilicification scheme based on fusion of stabilized polysilicic acid into a fluidic precursor phase upon their infiltration into polyamine-enriched collagen. The latter serves as a template and catalyst for polymerization of the precursor phase into silica that faithfully reproduces the collagen tertiary architecture. Our findings provide a new concept in biosilica materials synthesis which does not require phosphate supplements.