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Stability of Ag nanoparticles dispersed in amphiphilic organic matrix
Nano- and thin-film technologies based on novel systems associating metals particles to polymer matrix open a broad range of different applications. Such composites were found to be more efficient and safe, for instance, in biomedical needs. The Ag/poly(N-vinyl-2-pyrrolidone) (Ag/PVP) composite inve...
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Published in: | Journal of crystal growth 2005-02, Vol.275 (1), p.e2351-e2356 |
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Main Authors: | , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | Nano- and thin-film technologies based on novel systems associating metals particles to polymer matrix open a broad range of different applications. Such composites were found to be more efficient and safe, for instance, in biomedical needs. The Ag/poly(N-vinyl-2-pyrrolidone) (Ag/PVP) composite investigated in the present work is a new bactericide mean applied in complicated cases of infected burns and purulent wounds. High-resolution transmission electron microscopy (HRTEM) and X-ray energy-dispersive (EDS) microanalysis were used to bring chemical and structural information in a study of the properties and stability of thin-film nanocomposite whih consisted of Ag nanoparticles dispersed in water-soluble organic matrix poly(N-vinyl-2-pyrrolidone). The nanostructural investigation of Ag/PVP composite by HRTEM and EDS exposed to SO
2 and H
2S from the atmosphere and some traces of S-containing substances explains the limited stability of this system by a structural modification associated with a phase change and formation of Ag
2S and Ag
2SO
3. However, formation of the hardly water-soluble Ag
2S and Ag
2SO
3 salts may play an important role in the suppression of bacterial growth. On the one hand, silver could block S–H groups in vital proteins and conduced to their destruction, in that way revealing the antibacterial power. On the other hand, antiseptic properties of Ag consist in binding the products of the protein decay. |
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ISSN: | 0022-0248 1873-5002 |
DOI: | 10.1016/j.jcrysgro.2004.11.333 |