Abstract
The silaffin peptide R5 is instrumental to the mineralization of silica cell walls of diatom organisms. The peptide is also widely employed in biotechnology, for example, in the encapsulation of enzymes and for fusion proteins in tissue regeneration. Despite its scientific and technological importance, the interfacial structure of R5 during silica precipitation remains poorly understood. We herein elucidate the conformation of the peptide in its active form within silica sheets by interface-specific vibrational spectroscopy in combination with molecular dynamics simulations. Contrary to previous solution-state NMR studies, our data confirm that R5 maintains a defined structure when interacting with extended silica sheets. We show that the entire amino acid sequence of R5 interacts with silica during silica formation, leading to the intercalation of silica into the assembled peptide film.
Published Version
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