TY - JOUR
T1 - Short-chain alkanethiol coating for small-size gold nanoparticles supporting protein stability
AU - Cantarutti, Cristina
AU - Bertoncin, Paolo
AU - Corazza, Alessandra
AU - Giorgetti, Sofia
AU - Patrizia Mangione, P.
AU - Bellotti, Vittorio
AU - Fogolari, Federico
AU - Esposito, Gennaro
N1 - Funding Information:
This work received financial support from PRIN project No. 2012A7LMS3. We acknowledge the New York University Abu Dhabi for access to the Core Technology Platform. We also thank Makek A. for the assistance.
Publisher Copyright:
© 2017 by the authors. Licensee MDPI, Basel, Switzerland.
PY - 2017/12
Y1 - 2017/12
N2 - 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.
AB - 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.
KW - Amyloidogenic protein-nanoparticle systems
KW - Nanoparticle stability
KW - Protein unfolding
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U2 - 10.3390/magnetochemistry3040040
DO - 10.3390/magnetochemistry3040040
M3 - Article
AN - SCOPUS:85041512145
SN - 2312-7481
VL - 3
JO - Magnetochemistry
JF - Magnetochemistry
IS - 4
M1 - 40
ER -