In situ formation of mineral particles by biocatalysis would be advantageous for occluding dentin tubules to reduce permeability or for sealing of material-tooth interfaces. One approach would require that the peptide-catalyst remain functional on the dentin surface. Based on recent observations of retained activity on other surfaces, we hypothesized that poly(L-lysine) (PLL), an analog of the protein catalyst responsible for silica formation in primitive marine species, would remain functional on dentin. PLL was applied to dentin discs along with a pre-hydrolyzed silica precursor, tetramethyl orthosilicate (TMOS). Discs were analyzed microscopically (scanning electron microscopy, SEM) and chemically (x-ray photoelectron spectroscopy, XPS). The treated discs, but not the negative controls, exhibited partial distinct coating whose XPS survey was consistent with that of silica, demonstrating that the polypeptide was required and retained its mediating activity. Peptide-catalysts that mediate mineral formation can retain functionality on dentin, suggesting a wide range of preventive and treatment strategies.
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