The use of biomimetic approachesin the production of inorganicnanostructures is of great interest to the scientific and industrialcommunity due to the relatively moderate physical conditions needed.In this vein, taking cues from silaffin proteins used by unicellulardiatoms, several studies have identified peptide candidates for theproduction of silica nanostructures. In the current article, we studyintensively one such silica-precipitating peptide, LKα14 (Ac-LKKLLKLLKKLLKL-c),an amphiphilic lysine/leucine repeat peptide that self-organizes intoan α-helical secondary structure under appropriate concentrationand buffer conditions. The suggested mechanism of precipitation isthat the sequestration of hydrophilic lysines on one side of thishelix allows interaction with the negatively charged surface of silicananoparticles, which in turn can aggregate further into larger structures.To investigate the process, we carry out 1D and 2D solid-state NMR(ssNMR) studies on samples with one or two uniformly 13C- and 15N-labeled residues to determine the backboneand side-chain chemical shifts. We also further study the dynamicsof two leucine residues in the sequence through 13C spin–latticerelaxation times (T1) to determine theimpact of silica coprecipitation on their mobility. Our results confirmthe α-helical secondary structure in both the neat and silica-complexedstates of the peptide, and the patterns of chemical shift and relaxationtime changes between the two states suggest possible mechanisms ofself-aggregation and silica precipitation. [ABSTRACT FROM AUTHOR]