Short-Chain Alkanethiol Coating for Small-Size Gold Nanoparticles Supporting Protein Stability
| Autor: | Cristina Cantarutti, Sofia Giorgetti, Alessandra Corazza, Federico Fogolari, Palma Mangione, Vittorio Bellotti, Paolo Bertoncin, Gennaro Esposito |
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| Přispěvatelé: | Cantarutti, Cristina, Bertoncin, Paolo, Corazza, Alessandra, Giorgetti, Sofia, Mangione, P., Bellotti, Vittorio, Fogolari, Federico, Esposito, Gennaro |
| Jazyk: | angličtina |
| Rok vydání: | 2017 |
| Předmět: |
Sonication
Nanoparticle Nanotechnology 02 engineering and technology engineering.material 010402 general chemistry 01 natural sciences Fluorescence spectroscopy lcsh:Chemistry Protein structure Coating Materials Chemistry chemistry.chemical_classification Biomolecule protein unfolding Nuclear magnetic resonance spectroscopy 021001 nanoscience & nanotechnology amyloidogenic protein-nanoparticle system 0104 chemical sciences Electronic Optical and Magnetic Materials chemistry lcsh:QD1-999 Chemistry (miscellaneous) Colloidal gold engineering amyloidogenic protein-nanoparticle systems nanoparticle stability 0210 nano-technology |
| Zdroj: | Magnetochemistry, Vol 3, Iss 4, p 40 (2017) Magnetochemistry; Volume 3; Issue 4; Pages: 40 |
| ISSN: | 2312-7481 |
| Popis: | The application of gold nanoparticles (AuNPs) is emerging in many fields, raising the need for a systematic investigation on their safety. In particular, for biomedical purposes, a relevant issue are certainly AuNP interactions with biomolecules, among which proteins are the most abundant ones. Elucidating the effects of those interactions on protein structure and on nanoparticle stability is a major task towards understanding their mechanisms at a molecular level. We investigated the interaction of the 3-mercaptopropionic acid coating of AuNPs (MPA-AuNPs) with β2-microglobulin (β2m), which is a paradigmatic amyloidogenic protein. To this aim, we prepared and characterized MPA-AuNPs with an average diameter of 3.6 nm and we employed NMR spectroscopy and fluorescence spectroscopy to probe protein structure perturbations. We found that β2m interacts with MPA-AuNPs through a highly localized patch maintaining its overall native structure with minor conformational changes. The interaction causes the reversible precipitation of clusters that can be easily re-dispersed through brief sonication. View Full-Text |
| Databáze: | OpenAIRE |
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