Cantarutti, C;
Bertoncin, P;
Corazza, A;
Giorgetti, S;
Mangione, PP;
Bellotti, V;
Fogolari, F;
(2017)
Short-Chain Alkanethiol Coating for Small-Size Gold Nanoparticles Supporting Protein Stability.
Magnetochemistry
, 3
(4)
, Article 40. 10.3390/magnetochemistry3040040.
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Abstract
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.
Type: | Article |
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Title: | Short-Chain Alkanethiol Coating for Small-Size Gold Nanoparticles Supporting Protein Stability |
Open access status: | An open access version is available from UCL Discovery |
DOI: | 10.3390/magnetochemistry3040040 |
Publisher version: | https://doi.org/10.3390/magnetochemistry3040040 |
Language: | English |
Additional information: | This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited https://creativecommons.org/licenses/by/4.0/ |
Keywords: | amyloidogenic protein-nanoparticle systems; nanoparticle stability; protein unfolding |
UCL classification: | UCL UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Medical Sciences UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Medical Sciences > Div of Medicine UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Medical Sciences > Div of Medicine > Inflammation |
URI: | https://discovery.ucl.ac.uk/id/eprint/10092660 |
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