N-terminal residues of silaffin peptides impact morphology of biomimetic silica particles

R5 is a synthetic silaffin peptide derived from diatoms that can precipitate monodisperse silica particles (SPs) from silicic acid under mild biomimetic conditions. Due to the range of potential applications, it is important to understand the mechanisms that govern such silica precipitation, however to date these mechanisms remain ambiguous. Here, we report that the N-terminal residues of R5 substantially impact the silica precipitating mechanism, most likely by affecting the self-assembling properties of the peptide. Our results show that the morphology of silaffin-derived SPs can be modulated by changing the N-terminus of the peptide.