Controlled silica deposition on self-assembled peptide nanostructures via varying molecular structures of short amphiphilic peptides
Cationic amphiphilic peptides are highly similar to native silaffins and silicateins for biosilicification in terms of their composition, amphiphilicity, and self-assembling propensity. To understand the relationship between organic molecular structures, molecular self-assembly and silica morphogenesis during biosilicification, we have prepared a series of short self-assembling peptide amphiphiles (I3–5K, I4K2, I3–4R, and I4R2) and investigated their capability to mediate silicification under ambient conditions. I3K self-assembled into tubular nanofibrils while I4K1–2 and I5K formed solid nanofibrils in aqueous solution with their outer diameters decreasing as the number of hydrophobic or hydrophilic amino acid residues increased. Changes in molecular structure thus altered their self-assembled geometries, and the exposed surfaces and surface lysine densities under different geometries then played different mediating roles in silicification, leading to different silica deposition patterns and final silica nanostructures. The templating capacity was weakened or lost when lysine was replaced by arginine, despite the fact that I3–4R and I4R2 self-assembled into nanofibrils and nanoribbons under similar conditions.