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2000
Volume 19, Issue 17
  • ISSN: 1385-2728
  • E-ISSN: 1875-5348

Abstract

The development of silica-based sol-gel techniques compatible with the retention of protein structure and function started more than 20 years ago, mainly for the design of biotechnological devices or biomedical applications. Silica gels are optically transparent, exhibit good mechanical stability, are manufactured with different geometries, and are easily separated from the reaction media. Biomolecules encapsulated in silica gel normally retain their structural and functional properties, are stabilized with respect to chemical and physical insults, and can sometimes exhibit enhanced activity in comparison to the soluble form. This review briefly describes the chemistry of protein encapsulation within the pores of a silica gel three-dimensional network, the mechanism of interaction between the protein and the gel matrix, and its effects on protein structure, function, stability and dynamics. The main applications in the field of biosensor design are described. Special emphasis is devoted to silica gel encapsulation as a tool to selectively stabilize subsets of protein conformations for biochemical and biophysical studies, an application where silica-based encapsulation demonstrated superior performance with respect to other immobilization techniques.

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/content/journals/coc/10.2174/1385272819666150601211349
2015-09-01
2025-01-17
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/content/journals/coc/10.2174/1385272819666150601211349
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  • Article Type:
    Research Article
Keyword(s): conformational transitions; encapsulation; heme proteins; protein dynamics; Sol-gel
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