Spectroscopic and electrochemical characterization of cytochrome c encapsulated in a bio sol-gel matrix
| Autor: | Nicola Rosato, Sara Emanuela Pagnotta, Roberto Santucci, Daniela Deriu |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2008 |
| Předmět: |
Protein Denaturation
Cyclic voltammetry Biocompatibility Protein encapsulation Protein Conformation Drug Compounding Cytochrome c chemistry.chemical_element Calcium Bio sol-gel Electrochemistry Calcium nitrate Redox Phase Transition General Biochemistry Genetics and Molecular Biology Biomaterials chemistry.chemical_compound Animals Horses Settore BIO/10 Nitrates biology Circular Dichroism Metals and Alloys Cytochromes c Sol gel matrix Calcium Compounds Hydrogen-Ion Concentration chemistry Biochemistry Chemical engineering biology.protein General Agricultural and Biological Sciences Gels Oxidation-Reduction |
| Popis: | Sol-gel technique represents a remarkably versatile method for protein encapsulation. To enhance sol-gel biocompatibility, systems envisaging the presence of calcium and phosphates in the sol-gel composition were recently prepared and investigated. Unfortunately, the low pH at which solutions were prepared (pH < 2.5) dramatically limited their application to proteins, because the acidic environment induces protein denaturation. In this paper we apply a new protocol based on the introduction of calcium nitrate to the inorganic phase, with formation of a binary bioactive system. In this case protein encapsulation results versatile and secure, being achieved at a pH close to neutrality (pH 6.0); also, the presence of calcium is expected to enhance system biocompatibility. To determine the properties of the salt-doped sol-gel and the influence exerted on entrapped biosystems, the structural and functional properties of embedded cytochrome c have been investigated. Data obtained indicate that the salt-doped sol-gel induces no significant change in the structure and the redox properties of the embedded protein; also, the matrix increases protein stability. Interestingly, the presence of calcium nitrate appears determinant for refolding of the acid-denatured protein. This is of interest in the perspective of future applications in biosensoristic area. |
| Databáze: | OpenAIRE |
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