Shedding light on peptide controlled silica mineralization

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Biominerals, composites of organic and inorganic matter, have evolved over millions of years, showcasing remarkable properties like toughness and strength, exemplified by the silica skeletons of diatoms. While the macroscopic formation of silica in diatoms is well understood, applying biomimetic silica formation in technology necessitates a molecular-level comprehension of how organic molecules influence silica morphology. This research focuses on peptides, which mimic biomolecules involved in diatom biosilicification, to explore how peptide structure and ordering at interfaces affect artificially generated silica morphology. The first chapter introduces silica mineralization in nature and the methods for studying peptide-mediated processes at interfaces. Chapter two reveals that helical and β-strand amphiphilic peptides yield distinct silica morphologies at the air-water interface, with even minor modifications, such as adding a protecting group, leading to significant morphological differences, a topic explored in Chapter three. Chapter four delves into the structural analysis of the R5 peptide, a derivative of the diatom peptide Silaffin, enhancing understanding of natural biosilicification. Lastly, Chapter five outlines a method to benchmark various parameter sets for molecular dynamics simulations of peptides at the air-water interface.