5 years ago

The Structure of the Diatom Silaffin Peptide R5 within Freestanding Two-Dimensional Biosilica Sheets

The Structure of the Diatom Silaffin Peptide R5 within Freestanding Two-Dimensional Biosilica Sheets
Lars Schmüser, Jim Pfaendtner, Vance Jaeger, Helmut Lutz, Mischa Bonn, Tobias Weidner
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. Biosilica windows: The diatom silaffin peptide R5 was used to fabricate freestanding, nanometer-thin biosilica sheets. These provided a realistic model system to determine the mode of action by which R5 fabricates extended silica structures by using sum-frequency generation and molecular dynamics simulations.

Publisher URL: http://onlinelibrary.wiley.com/resolve/doi

DOI: 10.1002/anie.201702707

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