Abstract
This paper considers the nature of the interactions between the sol-gel derived inorganic matrix and a specific biomolecule, cytochrome c. Optical absorption and impedance spectroscopies are used to characterize the influence of synthesis conditions on the protein’s stability and conformation within the silica matrix. In some instances, encapsulation within the sol-gel matrix provides stabilization. For example, protein denaturation is reversible and aggregation is prevented. Moreover, the drying process does not negatively affect the protein; it is possible to regenerate the aged gel state by rehydration. The flexibility of the sol-gel process enables high quality cytochrome c-doped SiO2 thin films to be prepared. These films possess the characteristic reactivity and chemical function of cytochrome c in solution.
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Dave, B.C., Miller, J.M., Dunn, B. et al. Encapsulation of proteins in bulk and thin film sol-gel matrices. J Sol-Gel Sci Technol 8, 629–634 (1997). https://doi.org/10.1007/BF02436913
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DOI: https://doi.org/10.1007/BF02436913