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.
Highlights
Proteins play a fundamental role in biological processes
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
Summary
Proteins play a fundamental role in biological processes. Their activity, on one hand supports the correct operation of an organism, but on the other, could be responsible for disease onset. The fact that the interaction profile can highlight the functions a protein performs implies that understanding the behaviour of a protein at the molecular level is a valuable strategy to get deep insights into the functional role and possibly into the design of new tools to master the protein activity. The spreading application of nanomaterials in different fields such as biomedicine, food, environmental, and material sciences [1,2], has stressed the relevance of understanding at a molecular level protein-nanoparticle interaction, because any contact of nanomaterials with a biological fluid is suddenly followed by the adsorption of proteins [3]. CFuitr-tAhuerNmPosrae,reitawbalestsohpowarntiathllaythCinitd‐AerutNhPesfiabrreilalobgleentoespisarotfiatlhlye mhionsdtearmthyelofiibdroiglleongiecnveasirsiaonftt,hneammoelsyt Dam76yNloiβd2omge[n1i5c].variant, namely D76N β2m [15]
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