Silicatein Filaments and Subunits from a Marine Sponge Direct the Polymerization of Silica and Silicones in vitro

• Published in: Proceedings of the National Academy of Sciences - PNAS Vol. 96; no. 2; pp. 361 - 365
• Main Authors: Cha, Jennifer N., Shimizu, Katsuhiko, Zhou, Yan, Christiansen, Sean C., Chmelka, Bradley F., Stucky, Galen D., Morse, Daniel E.
• Format: Journal Article
• Language: English
• Published: United States National Academy of Sciences of the United States of America 19.01.1999; National Acad Sciences; National Academy of Sciences
• Subjects: Actin Cytoskeleton - ultrastructure; Alkoxides; Animals; Aquatic life; Biochemistry; Biological Sciences; Catalysis; Cathepsin L; Cathepsins - chemistry; Cathepsins - metabolism; Cathepsins - ultrastructure; Cellulose - metabolism; Cellulose - ultrastructure; Condensation; Cysteine Endopeptidases; Endopeptidases; Enzymes; Hydrogen Bonding; Magnetic Resonance Spectroscopy; Marine; Materials; Microscopy, Electron, Scanning; Molecular Structure; Polymerization; Polymers - metabolism; Porifera; Porifera - metabolism; Proteins; Silanes - metabolism; Silicon; Silicon Dioxide - chemistry; Siloxanes; Sponges
• ISSN: 0027-8424; 1091-6490
• DOI: 10.1073/pnas.96.2.361

Nanoscale control of the polymerization of silicon and oxygen determines the structures and properties of a wide range of siloxane-based materials, including glasses, ceramics, mesoporous molecular sieves and catalysts, elastomers, resins, insulators, optical coatings, and photoluminescent polymers. In contrast to anthropogenic and geological syntheses of these materials that require extremes of temperature, pressure, or pH, living systems produce a remarkable diversity of nanostructured silicates at ambient temperatures and pressures and at near-neutral pH. We show here that the protein filaments and their constituent subunits comprising the axial cores of silica spicules in a marine sponge chemically and spatially direct the polymerization of silica and silicone polymer networks from the corresponding alkoxide substrates in vitro, under conditions in which such syntheses otherwise require either an acid or base catalyst. Homology of the principal protein to the well known enzyme cathepsin L points to a possible reaction mechanism that is supported by recent site-directed mutagenesis experiments. The catalytic activity of the "silicatein" (silica protein) molecule suggests new routes to the synthesis of silicon-based materials.