Short-Chain Alkanethiol Coating for Small-Size Gold Nanoparticles Supporting Protein Stability
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. Eluc...
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doaj-7793946d69484127b09b4c22f8c329562020-11-24T20:48:26ZengMDPI AGMagnetochemistry2312-74812017-11-01344010.3390/magnetochemistry3040040magnetochemistry3040040Short-Chain Alkanethiol Coating for Small-Size Gold Nanoparticles Supporting Protein StabilityCristina Cantarutti0Paolo Bertoncin1Alessandra Corazza2Sofia Giorgetti3P. Patrizia Mangione4Vittorio Bellotti5Federico Fogolari6Gennaro Esposito7DAME, Università di Udine, P.le Kolbe 4, 33100 Udine, ItalyDipartimento di Scienze della Vita, Università di Trieste, 34128 Trieste, ItalyDAME, Università di Udine, P.le Kolbe 4, 33100 Udine, ItalyDipartimento di Medicina Molecolare, Università di Pavia, Via Taramelli 3, 27100 Pavia, ItalyDipartimento di Medicina Molecolare, Università di Pavia, Via Taramelli 3, 27100 Pavia, ItalyDipartimento di Medicina Molecolare, Università di Pavia, Via Taramelli 3, 27100 Pavia, ItalyINBB—Viale Medaglie d’Oro 305, 00136 Roma, ItalyINBB—Viale Medaglie d’Oro 305, 00136 Roma, ItalyThe 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.https://www.mdpi.com/2312-7481/3/4/40amyloidogenic protein-nanoparticle systemsnanoparticle stabilityprotein unfolding |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Cristina Cantarutti Paolo Bertoncin Alessandra Corazza Sofia Giorgetti P. Patrizia Mangione Vittorio Bellotti Federico Fogolari Gennaro Esposito |
spellingShingle |
Cristina Cantarutti Paolo Bertoncin Alessandra Corazza Sofia Giorgetti P. Patrizia Mangione Vittorio Bellotti Federico Fogolari Gennaro Esposito Short-Chain Alkanethiol Coating for Small-Size Gold Nanoparticles Supporting Protein Stability Magnetochemistry amyloidogenic protein-nanoparticle systems nanoparticle stability protein unfolding |
author_facet |
Cristina Cantarutti Paolo Bertoncin Alessandra Corazza Sofia Giorgetti P. Patrizia Mangione Vittorio Bellotti Federico Fogolari Gennaro Esposito |
author_sort |
Cristina Cantarutti |
title |
Short-Chain Alkanethiol Coating for Small-Size Gold Nanoparticles Supporting Protein Stability |
title_short |
Short-Chain Alkanethiol Coating for Small-Size Gold Nanoparticles Supporting Protein Stability |
title_full |
Short-Chain Alkanethiol Coating for Small-Size Gold Nanoparticles Supporting Protein Stability |
title_fullStr |
Short-Chain Alkanethiol Coating for Small-Size Gold Nanoparticles Supporting Protein Stability |
title_full_unstemmed |
Short-Chain Alkanethiol Coating for Small-Size Gold Nanoparticles Supporting Protein Stability |
title_sort |
short-chain alkanethiol coating for small-size gold nanoparticles supporting protein stability |
publisher |
MDPI AG |
series |
Magnetochemistry |
issn |
2312-7481 |
publishDate |
2017-11-01 |
description |
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. |
topic |
amyloidogenic protein-nanoparticle systems nanoparticle stability protein unfolding |
url |
https://www.mdpi.com/2312-7481/3/4/40 |
work_keys_str_mv |
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