Biomineralizing organisms are unmatched in their ability to form micro-to nanoscale hierarchically structured 3D inorganic materials under ambient conditions. Although the genetic foundations of the species-specific 3D architectures of biominerals are not well understood, specific organic molecules (mostly proteins) are known to guide their deposition and morphogenesis.[1–3] It has been suggested that the molecules and mechanisms of biomineralization may provide new paradigms for the environmentally benign syntheses of advanced nanopatterned materials.[4–6] Indeed, pioneering work by Morse and co-workers demonstrated that proteins (named silicateins) involved in the biomineralization of sponge silica spicules are able to catalyze invitro the formation of silica and amorphous or partially crystallized, non-biological inorganic materials (titanium dioxide, titanium phosphates, gallium oxohydride, and gallium oxide).[7–12] Also, the hydrolytic enzyme lysozyme has been shown to induce formation of amorphous titania and silica.[13, 14] A different family of silica-forming proteins (named silaffins) has been characterized from diatoms, which are a group of unicellular microalgae (phytoplankton) that form intricately structured 3D silica microshells. Silaffins represent a unique family of phosphoproteins that share no sequence homology with sponge silicateins and exhibit a different mechanism of silica formation.[15a–c] Recently, poly (allylamine)[16a] and the synthetic non-phosphorylated 19-mer peptide R5, which corresponds to a repeat sequence of the silaffin