Comparative Study of Secondary Structure and Interactions of the R5 Peptide in Silicon Oxide and Titanium Oxide Coprecipitates Using Solid-State NMR Spectroscopy

A biomimetic, peptide-mediated approach to inorganic nanostructure formation is of great interest as an alternative to industrial production methods. To investigate the role of peptide structure on silica (SiO₂) and titania (TiO₂) morphologies, we use the R5 peptide domain derived from the silaffin protein to produce uniform SiO₂ and TiO₂ nanostructures from the precursor silicic acid and titanium bis­(am­monium lac­tato)­di­hydroxide, respectively. The resulting biosilica and biotitania nanostructures are characterized using scanning electron microscopy. To investigate the process of R5-mediated SiO₂ and TiO₂ formation, we carry out 1D and 2D solid-state NMR (ssNMR) studies on R5 samples with uniformly ¹³C- and ¹⁵N-labeled residues to determine the backbone and side-chain chemical shifts. ¹³C chemical shift data are in turn used to determine peptide backbone torsion angles and secondary structure for the R5 peptide neat, in silica, and in titania. We are thus able to assess the impact of the different mineral environments on peptide structure, and we can further elucidate from ¹³C chemical shifts change the degree to which various side chains are in close proximity to the mineral phases. These comparisons add to the understanding of the role of R5 and its structure in both SiO₂ and TiO₂ formation

Serine–Lysine Peptides as Mediators for the Production of Titanium Dioxide: Investigating the Effects of Primary and Secondary Structures Using Solid-State NMR Spectroscopy and DFT Calculations

A biomimetic approach to the formation of titania (TiO₂) nanostructures is desirable because of the mild conditions required in this form of production. We have identified a series of serine–lysine peptides as candidates for the biomimetic production of TiO₂ nanostructures. We have assayed these peptides for TiO₂-precipitating activity upon exposure to titanium bis­(ammonium lactato)­dihydroxide and have characterized the resulting coprecipitates using scanning electron microscopy. A subset of these assayed peptides efficiently facilitates the production of TiO₂ nanospheres. Here, we investigate the process of TiO₂ nanosphere formation mediated by the S–K peptides KSSKK- and SKSK₃SKS using one-dimensional and two-dimensional solid-state NMR (ssNMR) on peptide samples with uniformly ¹³C-enriched residues. ssNMR is used to assign ¹³C chemical shifts (CSs) site-specifically in each free peptide and TiO₂-embedded peptide, which are used to derive secondary structures in the neat and TiO₂ coprecipitated states. The backbone ¹³C CSs are used to assess secondary structural changes undergone during the coprecipitation process. Side-chain ¹³C CS changes are analyzed with density functional theory calculations and used to determine side-chain conformational changes that occur upon coprecipitation with TiO₂ and to determine surface orientation of lysine side chains in TiO₂–peptide composites