Summary. Silicatein in marine sponges catalyses the condensation of silica but the mechanism of layer-by-layer growth of the silica spicule is unknown since sufficient quantities of the protein are unavailable for biophysical characterisation. We have generated a series of chimeric (silicatein-cathepsin) enzymes that condense silica from silicic acid at neutral pH. The enzymes can be microstamped onto surfaces, creating the corresponding silica stamp on immersion in silicic acid. The nature of the enzyme-silica layers (thickness, roughness, density) is unknown but would be ideally suited to investigation by neutron reflectivity. Objectives: 1) Non-specifically adsorb chimeras to SiO2 at 50 and 500 mg/L, characterising the protein layer; 2) Compare layers in 1 to thiolate-gold adsorbed chimera; 3) Characterise the silica layer generated by the surface-adsorbed chimeras in 1 and 2.